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Membrane transport protein
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A membrane transport protein (or simply transporter) is a membrane protein[1] involved in the movement of ions, small molecules, or macromolecules, such as another protein, across a biological membrane. Transport proteins are integral transmembrane proteins; that is they exist permanently within and span the membrane across which they transport substances. The proteins may assist in the movement of substances by facilitated diffusion or active transport. The two main types of proteins involved in such transport are broadly categorized as either channels or carriers. The solute carriers and atypical SLCs[2] are secondary active or facilitative transporters in humans.[3][4]
Contents
[hide]
1 Difference between channels and carriers
2 Active transport
3 Facilitated diffusion
4 Reverse transport
5 Types
5.1 1: Channels/pores
5.2 2: Electrochemical potential-driven transporters
5.3 3: Primary active transporters
5.4 4: Group translocators
5.5 5: Electron carriers
6 Examples
7 Pathology
8 See also
9 References
10 External links
Difference between channels and carriers[edit]
A carrier is not open simultaneously to both the extracellular and intracellular environments. Either its inner gate is open, or outer gate is open. In contrast, a channel can be open to both environments at the same time, allowing the molecules to diffuse without interruption. Carriers have binding sites, but pores and channels do not.[5][6][7] When a channel is opened, millions of ions can pass through the membrane per second, but only 100 to 1000 molecules typically pass through a carrier molecule in the same time.[8] Each carrier protein is designed to recognize only one substance or one group of very similar substances. Research has correlated defects in specific carrier proteins with specific diseases.[9]
Active transport[edit]
Main article: Active transport
The action of the sodium-potassium pump is an example of primary active transport. The two carrier proteins on the left are using ATP to move sodium out of the cell against the concentration gradient. The proteins on the right are using secondary active transport to move potassium into the cell.
Active transport is the movement of a substance across a membrane against its concentration gradient. This is usually to accumulate high concentrations of molecules that a cell needs, such as glucose or amino acids. When the lipid bilayer is impermeable to the molecule needing transport, active transport is also necessary. If the process uses chemical energy, such as adenosine triphosphate (ATP), it is called primary active transport. Secondary active transport involves the use of an electrochemical gradient, and does not use energy produced in the cell.[10] Unlike channel proteins which only transport substances through membranes passively, carrier proteins can transport ions and molecules either passively through facilitated diffusion, or via secondary active transport.[11] A carrier protein is required to move particles from areas of low concentration to areas of high concentration. These carrier proteins have receptors that bind to a specific molecule (substrate) needing transport. The molecule or ion to be transported (the substrate) must first bind at a binding site at the carrier molecule, with a certain binding affinity. Following binding, and while the binding site is facing the same way, the carrier will capture or occlude (take in and retain) the substrate within its molecular structure and cause an internal translocation so that the opening in the protein now faces the other side of the plasma membrane.[12] The carrier protein substrate is released at that site, according to its binding affinity there.
Facilitated diffusion[edit]
Main article: Facilitated diffusion
Facilitated diffusion in cell membrane, showing ion channels (left) and carrier proteins (three on the right).
Facilitated diffusion is the passage of molecules or ions across a biological membrane through specific transport proteins and requires no energy input. Facilitated diffusion is used especially in the case of large polar molecules and charged ions; once such ions are dissolved in water they cannot diffuse freely across cell membranes due to the hydrophobic nature of the fatty acid tails of the phospholipids that make up the bilayers. The type of carrier proteins used in facilitated diffusion is slightly different from those used in active transport. They are still transmembrane carrier proteins, but these are gated transmembrane channels, meaning they do not internally translocate, nor require ATP to function. The substrate is taken in one side of the gated carrier, and without using ATP the substrate is released into the cell. They may be used as potential biomarkers
Reverse transport[edit]
Main article: Reverse transport
Reverse transport, or transporter reversal, is a phenomenon in which the substrates of a membrane transport protein are moved in the opposite direction to that of their typical movement by the transporter.[13][14][15][16][17] Transporter reversal typically occurs when a membrane transport protein is phosphorylated by a particular protein kinase, which is an enzyme that adds a phosphate group to proteins.[13][14]
Types[edit]
(Grouped by Transporter Classification database categories)
1: Channels/pores[edit]
α-helical protein channels such as voltage-gated ion channel (VIC), ligand-gated ion channels(LGICs)
β-barrel porins such as aquaporin
channel-forming toxins, including colicins, diphtheria toxin, and others
Nonribosomally synthesized channels such as gramicidin
Holins; which function in export of enzymes that digest bacterial cell walls in an early step of cell lysis.
Facilitated diffusion occurs in and out of the cell membrane via channels/pores and carriers/porters.
Note:
Channels:
Channels are either in open state or closed state. When a channel is opened with a slight conformational switch, it is open to both environment simultaneously (extracellular and intracellular)
This picture represents symport. The yellow triangle shows the concentration gradient for the yellow circles while the green triangle shows the concentration gradient for the green circles and the purple rods are the transport protein bundle. The green circles are moving against their concentration gradient through a transport protein which requires energy while the yellow circles move down their concentration gradient which releases energy. The yellow circles produce more energy through chemiosmosis than what is required to move the green circles so the movement is coupled and some energy is cancelled out. One example is the lactose permease which allows protons to go down its concentration gradient into the cell while also pumping lactose into the cell.
Pores:
Pores are continuously open to these both environment, because they do not undergo conformational changes. They are always open and active.
2: Electrochemical potential-driven transporters[edit]
2.A: Porters ( uniporters, symporters, antiporters), SLCs.[4]
The picture represents uniport. The yellow triangle shows the concentration gradient for the yellow circles and the purple rods are the transport protein bundle. Since they move down their concentration gradient through a transport protein, they can release energy as a result of chemiosmosis. One example is GLUT1 which moves glucose down its concentration gradient into the cell.
Excitatory amino acid transporters (EAATs)
EAAT1
EAAT2
EAAT3
EAAT4
EAAT5
Glucose transporter
Monoamine transporters, including:
Dopamine transporter (DAT)
Norepinephrine transporter (NET)
Serotonin transporter (SERT)
Vesicular monoamine transporters (VMAT)
Adenine nucleotide translocator (ANT)
2.B: Nonribosomally synthesized porters, such as
The Nigericin (Nigericin) Family
The Ionomycin (Ionomycin) Family
2.C: Ion-gradient-driven energizers
3: Primary active transporters[edit]
3.A: P-P-bond-hydrolysis-driven transporters :
ATP-binding cassette transporter (ABC transporter), such as MDR, CFTR
V-type ATPase ; ( "V" related to vacuolar ).
P-type ATPase ; ( "P" related to phosphorylation), such as :
Na+/K+-ATPase
Plasma membrane Ca2+ ATPase
Proton pump
This picture represents antiport. The yellow triangle shows the concentration gradient for the yellow circles while the blue triangle shows the concentration gradient for the blue circles and the purple rods are the transport protein bundle. The blue circles are moving against their concentration gradient through a transport protein which requires energy while the yellow circles move down their concentration gradient which releases energy. The yellow circles produce more energy through chemiosmosis than what is required to move the blue circles so the movement is coupled and some energy is cancelled out. One example is the sodium-proton exchanger which allows protons to go down their concentration gradient into the cell while pumping sodium out of the cell.
F-type ATPase; ("F" related to factor), including: mitochondrial ATP synthase, chloroplast ATP synthase1
3.B: Decarboxylation-driven transporters
3.C: Methyltransfer-driven transporters
3.D: Oxidoreduction-driven transporters
3.E: Light absorption-driven transporters, such as rhodopsin
4: Group translocators[edit]
The group translocators provide a special mechanism for the phosphorylation of sugars as they are transported into bacteria (PEP group translocation)
5: Electron carriers[edit]
The transmembrane electron transfer carriers in the membrane include two-electron carriers, such as the disulfide bond oxidoreductases (DsbB and DsbD in E. coli) as well as one-electron carriers such as NADPH oxidase. Often these redox proteins are not considered transport proteins.
Examples[edit]
Each carrier protein, even within the same cell membrane, is specific to one type or family of molecules. For example, GLUT1 is a named carrier protein found in almost all animal cell membranes that transports glucose across the bilayer. Other specific carrier proteins also help the body function in important ways. Cytochromes operate in the electron transport chain as carrier proteins for electrons.[10]
Pathology[edit]
A number of inherited diseases involve defects in carrier proteins in a particular substance or group of cells. Cysteinuria (cysteine in the urine and the bladder) is such a disease involving defective cysteine carrier proteins in the kidney cell membranes. This transport system normally removes cysteine from the fluid destined to become urine and returns this essential amino acid to the blood. When this carrier malfunctions, large quantities of cysteine remain in the urine, where it is relatively insoluble and tends to precipitate. This is one cause of urinary stones.[18] Some vitamin carrier proteins have been shown to be overexpressed in patients with malignant disease. For example, levels of riboflavin carrier protein (RCP) have been shown to be significantly elevated in people with breast cancer.[19]
See also[edit]
Cotransport
Cotransporter
Ion channel
Permease
P-loop
Solute carrier family (classification)
TC number (classification)
Translocase
Vesicular transport protein
References[edit]
Jump up ^ Membrane transport proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
Jump up ^ Perland, Emelie; Bagchi, Sonchita; Klaesson, Axel; Fredriksson, Robert (2017-09-01). "Characteristics of 29 novel atypical solute carriers of major facilitator superfamily type: evolutionary conservation, predicted structure and neuronal co-expression". Open Biology. 7 (9): 170142. doi:10.1098/rsob.170142. ISSN 2046-2441. PMC 5627054  . PMID 28878041.
Jump up ^ Hediger, Matthias A.; Romero, Michael F.; Peng, Ji-Bin; Rolfs, Andreas; Takanaga, Hitomi; Bruford, Elspeth A. (February 2004). "The ABCs of solute carriers: physiological, pathological and therapeutic implications of human membrane transport proteinsIntroduction". Pflügers Archiv: European Journal of Physiology. 447 (5): 465–468. doi:10.1007/s00424-003-1192-y. ISSN 0031-6768. PMID 14624363.
^ Jump up to: a b Perland, Emelie; Fredriksson, Robert (March 2017). "Classification Systems of Secondary Active Transporters". Trends in Pharmacological Sciences. 38 (3): 305–315. doi:10.1016/j.tips.2016.11.008. ISSN 1873-3735. PMID 27939446.
Jump up ^ Sadava, David, et al. Life, the Science of Biology, 9th Edition. Macmillan Publishers, 2009. ISBN 1-4292-1962-9. p. 119.
Jump up ^ Cooper, Geoffrey (2009). The Cell: A Molecular Approach. Washington, DC: ASM Press. p. 62. ISBN 9780878933006.
Jump up ^ Thompson, Liz A. Passing the North Carolina End of Course Test for Biology. American Book Company, Inc. 2007. ISBN 1-59807-139-4. p. 97.
Jump up ^ Assmann, Sarah (2015). "Solute Transport". In Taiz, Lincoln; Zeiger, Edward. Plant Physiology and Development. Sinauer. p. 151.
Jump up ^ Sadava, David, Et al. Life, the Science of Biology, 9th Edition. Macmillan Publishers, 2009. ISBN 1-4292-1962-9. p. 119.
^ Jump up to: a b Ashley, Ruth. Hann, Gary. Han, Seong S. Cell Biology. New Age International Publishers. ISBN 8122413978. p. 113.
Jump up ^ Taiz, Lincoln. Zeigler, Eduardo. Plant Physiology and Development. Sinauer Associates, 2015. ISBN 978-1-60535-255-8. pp. 151.
Jump up ^ Kent, Michael. Advanced Biology. Oxford University Press US, 2000. ISBN 0-19-914195-9. pp. 157–158.
^ Jump up to: a b Bermingham DP, Blakely RD (October 2016). "Kinase-dependent Regulation of Monoamine Neurotransmitter Transporters". Pharmacol. Rev. 68 (4): 888–953. doi:10.1124/pr.115.012260. PMC 5050440  . PMID 27591044.
^ Jump up to: a b Miller GM (January 2011). "The emerging role of trace amine-associated receptor 1 in the functional regulation of monoamine transporters and dopaminergic activity". Journal of Neurochemistry. 116 (2): 164–176. doi:10.1111/j.1471-4159.2010.07109.x. PMC 3005101  . PMID 21073468.
Jump up ^ Scholze P, Nørregaard L, Singer EA, Freissmuth M, Gether U, Sitte HH (2002). "The role of zinc ions in reverse transport mediated by monoamine transporters". The Journal of Biological Chemistry. 277 (24): 21505–13. doi:10.1074/jbc.M112265200. PMID 11940571.
Jump up ^ Robertson SD, Matthies HJ, Galli A (2009). "A closer look at amphetamine-induced reverse transport and trafficking of the dopamine and norepinephrine transporters". Molecular Neurobiology. 39 (2): 73–80. doi:10.1007/s12035-009-8053-4. PMC 2729543  . PMID 19199083.
Jump up ^ Kasatkina LA, Borisova TA (November 2013). "Glutamate release from platelets: exocytosis versus glutamate transporter reversal". The International Journal of Biochemistry & Cell Biology. 45 (11): 2585–2595. doi:10.1016/j.biocel.2013.08.004. PMID 23994539.
Jump up ^ Sherwood, Lauralee. 7th Edition. Human Physiology. From Cells to Systems. Cengage Learning, 2008. p. 67
Jump up ^ Rao, PN, Levine, E et al. Elevation of Serum Riboflavin Carrier Protein in Breast Cancer. Cancer Epidemiol Biomarkers Prev. Volume 8 No 11. pp. 985–990
External links[edit]
"Transport protein" at Dorland's Medical Dictionary
DDI Regulatory Guidance Request a guide to drug-drug interaction regulatory recommendations.
[show]
v
t
e
Proteins: carrier proteins
Fatty acid
FABP1
FABP2
FABP3
FABP4
FABP5
FABP6
FABP7
Hormone
peptide hormone: Follistatin
Growth hormone binding protein
Insulin-like growth factor binding protein
IGFBP1
IGFBP2
IGFBP3
IGFBP4
IGFBP5
IGFBP6
IGFBP7
Neurophysins
Neurophysin I
II
steroid hormone: Sex hormone binding globulin/Androgen binding protein
Transcortin
Thyroxine-binding globulin
Transthyretin
Metal/element
calcium
Calcium-binding protein
Calmodulin-binding proteins
copper
Ceruloplasmin
iron
Iron-binding proteins
Transferrin receptor
Vitamin
Retinol binding protein
1
2
3
4
Transcobalamin
Pigment
Plant Light-Harvesting Complex
Orange Carotenoid Protein
Phycobiliprotein
Photosynthetic Reaction Centers
Phytochrome
Rhodopsin
Other
Acyl carrier protein
Adaptor protein
Cholesterylester transfer protein
F-box protein
GTP-binding protein
Latent TGF-beta binding protein
Major urinary proteins
Membrane transport protein
Odorant binding protein
[show]
v
t
e
Membrane transport protein: ion channels (TC 1A)
[show]
Ca2+: Calcium channel
Ligand-gated
Inositol trisphosphate receptor
1
2
3
Ryanodine receptor
1
2
3
Voltage-gated
L-type/Cavα
1.1
1.2
1.3
1.4
N-type/Cavα2.2
P-type/Cavα
2.1
Q-type/Cavα2.1
R-type/Cavα2.3
T-type/Cavα
3.1
3.2
3.3
α2δ-subunits
1
2
β-subunits
β1
β2
β3
β4
γ-subunits
γ1
γ2
γ3
γ4
Cation channels of sperm
1
2
3
4
Two-pore channel
1
2
[show]
Na+: Sodium channel
Constitutively active
Epithelial sodium channel
α
β
γ
δ
Proton-gated
Amiloride-sensitive cation channel
1
2
3
4
Voltage-gated
Navα
1.1
1.2
1.3
1.4
1.5
1.6
1.7
1.8
1.9
7A
Navβ
1
2
3
4
[show]
K+: Potassium channel
Calcium-activated
BK channel
α1
β1
β2
β3
β4
SK channel
SK1
SK2
SK3
IK channel
IK1
KCa
1.1
2.1
2.2
2.3
3.1
4.1
4.2
5.1
Inward-rectifier
KATP
Kir
1.1
2.1
2.2
2.3
2.4
2.6
GIRK/Kir
3.1
3.2
3.3
3.4
Kir
4.1
4.2
5.1
6.1
6.2
7.1
Tandem pore domain
K2P
1
2
3
4
5
6
7
9
10
12
13
15
16
17
18
Voltage-gated
Kvα1-6
1.1
1.2
1.3
1.4
1.5
1.6
1.7
1.8
2.1
2.2
3.1
3.2
3.3
3.4
4.1
4.2
4.3
5.1
6.1
6.2
6.3
6.4
Kvα7-12
7.1
7.2
7.3
7.4
7.5
8.1
8.2
9.1
9.2
9.3
10.1
10.2
11.1/hERG
11.2
11.3
12.1
12.2
12.3
Kvβ
1
2
3
KCNIP
1
2
3
4
minK/ISK
minK/ISK-like
MiRP
1
2
3
Shaker gene
[show]
Miscellaneous
Cl−: Chloride channel
Calcium-activated chloride channels
Anoctamin
ANO1
Bestrophin
1
2
Chloride Channel Accessory
1
2
3
4
CFTR
CLCN
1
2
3
4
5
6
7
KA
KB
CLIC
1
2
3
4
5
6
L1
CLNS
1A
1B
H+: Proton channel
HVCN1
M+: CNG cation channel
α
1
2
3
4
β
1
2
3
HCN
FC
1
2
3
4
M+: TRP cation channel
TRPA (1)
TRPC
1
2
3
4
4AP
5
6
7
TRPM
1
2
3
4
5
6
7
8
TRPML
1
2
3
TRPN
TRPP
1
2
TRPV
1
2
3
4
5
6
H2O (+ solutes): Porin
Aquaporin
0
1
2
3
4
5
6
7
8
9
Voltage-dependent anion channel
1
2
3
General bacterial porin family
Cytoplasm: Gap junction
Connexin
A
GJA1
GJA3
GJA4
GJA5
GJA8
GJA9
GJA10
B
GJB1
GJB2
GJB3
GJB4
GJB5
GJB6
GJB7
C
GJC1
GJC2
GJC3
D
GJD2
GJD3
GJD4
Innexin
[show]
By gating mechanism
Ion channel class
Ligand-gated
Light-gated
Voltage-gated
Stretch-activated
see also disorders
[show]
v
t
e
Membrane proteins, carrier proteins: membrane transport proteins solute carrier (TC 2A)
[show]
By group
[show]
SLC1–10
(1):
high affinity glutamate and neutral amino-acid transporter
SLC1A1
2
3
4
5
6
7
(2):
facilitative GLUT transporter
SLC2A1
2
3
4
5
6
7
8
9
10
11
12
13
14
(3):
heavy subunits of heterodimeric amino-acid transporters
SLC3A1
2
(4):
bicarbonate transporter
SLC4A1
2
3
4
5
6
7
8
9
10
11
(5):
sodium glucose cotransporter
SLC5A1
2
3
4
5
6
7
8
9
10
11
12
(6):
sodium- and chloride- dependent sodium:neurotransmitter symporters
SLC6A1
SLC6A2
SLC6A3
SLC6A4
SLC6A5
SLC6A6
SLC6A7
SLC6A8
SLC6A9
SLC6A10
SLC6A11
SLC6A12
SLC6A13
SLC6A14
SLC6A15
SLC6A16
SLC6A17
SLC6A18
SLC6A19
SLC6A20
(7):
cationic amino-acid transporter/glycoprotein-associated
SLC7A1
SLC7A2
SLC7A3
SLC7A4
glycoprotein-associated/light or catalytic subunits of heterodimeric amino-acid transporters
SLC7A5
SLC7A6
SLC7A7
SLC7A8
SLC7A9
SLC7A10
SLC7A11
SLC7A13
SLC7A14
(8):
Na+/Ca2+ exchanger
SLC8A1
SLC8A2
SLC8A3
(9):
Na+/H+ exchanger
SLC9A1
SLC9A2
SLC9A3
SLC9A4
SLC9A5
SLC9A6
SLC9A7
SLC9A8
SLC9A9
SLC9A10
SLC9A11
(10):
sodium bile salt cotransport
SLC10A1
SLC10A2
SLC10A3
SLC10A4
SLC10A5
SLC10A6
SLC10A7
10A1
10A2
10A3
10A7
[show]
SLC11–20
(11):
proton coupled metal ion transporter
SLC11A1
SLC11A211A3
(12):
electroneutral cation-Cl cotransporter
SLC12A1
SLC12A2
SLC12A3
SLC12A4
SLC12A5
SLC12A6
SLC12A7
SLC12A8
SLC12A9
(13):
human Na+-sulfate/carboxylate cotransporter
SLC13A1
SLC13A2
SLC13A3
SLC13A4
SLC13A5
(14):
urea transporter
SLC14A1
SLC14A2
(15):
proton oligopeptide cotransporter
SLC15A1
SLC15A2
SLC15A3
SLC15A4
(16):
monocarboxylate transporter
SLC16A1
SLC16A2
SLC16A3
SLC16A4
SLC16A5
SLC16A6
SLC16A7
SLC16A8
SLC16A9
SLC16A10
SLC16A11
SLC16A12
SLC16A13
SLC16A14
(17):
Vesicular glutamate transporter 1
SLC17A1
SLC17A2
SLC17A3
SLC17A4
SLC17A5
SLC17A6
SLC17A7
SLC17A8
SLC17A9
(18):
vesicular monoamine transporter
SLC18A1
SLC18A2
SLC18A3
(19):
folate/thiamine transporter
SLC19A1
SLC19A2
SLC19A3
(20):
type III Na+-phosphate cotransporter
SLC20A1
SLC20A2
[show]
SLC21–30
(21):
Organic anion-transporting polypeptide
SLCO1A2
SLCO1B1
SLCO1B3
SLCO1B4
SLCO1C1
SLCO2A1
SLCO2B1
SLCO3A1
SLCO4A1
SLCO4C1
SLCO5A1(SLCO6A1)
(22):
organic cation/anion/zwitterion transporter
SLC22A1
SLC22A2
SLC22A3
SLC22A4
SLC22A5
SLC22A6
SLC22A7
SLC22A8
SLC22A9
SLC22A10
SLC22A11
SLC22A12
SLC22A13
SLC22A14
SLC22A15
SLC22A16
SLC22A17
SLC22A18
SLC22A19
SLC22A20
(23):
Na+-dependent ascorbic acid transporter
SLC23A1
SLC23A2
SLC23A3
SLC23A4
(24):
Na+/(Ca2+-K+) exchanger
SLC24A1
SLC24A2
SLC24A3
SLC24A4
SLC24A5
SLC24A6
(25):
mitochondrial carrier
SLC25A1
SLC25A2
SLC25A3
SLC25A4
SLC25A5
SLC25A6
SLC25A7
SLC25A8
SLC25A9
SLC25A10
SLC25A11
SLC25A12
SLC25A13
SLC25A14
SLC25A15
SLC25A16
SLC25A17
SLC25A18
SLC25A19
SLC25A20
SLC25A21
SLC25A22
SLC25A23
SLC25A24
SLC25A25
SLC25A26
SLC25A27
SLC25A28
SLC25A29
SLC25A30
SLC25A31
SLC25A32
SLC25A33
SLC25A34
SLC25A35
SLC25A36
SLC25A37
SLC25A38
SLC25A39
SLC25A40
SLC25A41
SLC25A42
SLC25A43
SLC25A44
SLC25A45
SLC25A46
(26):
multifunctional anion exchanger
SLC26A1
SLC26A2
SLC26A3
SLC26A4
SLC26A5
SLC26A6
SLC26A7
SLC26A8
SLC26A9
SLC26A10
SLC26A11
(27):
fatty acid transport proteins
SLC27A1
SLC27A2
SLC27A3
SLC27A4
SLC27A5
SLC27A6
(28):
Na+-coupled nucleoside transport (SLC28A1
SLC28A2
SLC28A3
(29):
facilitative nucleoside transporter
SLC29A1
SLC29A2
SLC29A3
SLC29A4
(30):
zinc efflux
SLC30A1
SLC30A2
SLC30A3
SLC30A4
SLC30A5
SLC30A6
SLC30A7
SLC30A8
SLC30A9
SLC30A10
[show]
SLC31–40
(31):
copper transporter
SLC31A1
(32):
Vesicular glutamate transporter 1
SLC32A1
(33):
Acetyl-CoA transporter
SLC33A1
(34):
type II Na+-phosphate cotransporter
SLC34A1
SLC34A2
SLC34A3
(35):
nucleoside-sugar transporter
SLC35A1
SLC35A2
SLC35A3
SLC35A4
SLC35A5
SLC35B1
SLC35B2
SLC35B3
SLC35B4
SLC35C1
SLC35C2
SLC35D1
SLC35D2
SLC35D3
SLC35E1
SLC35E2
SLC35E3
SLC35E4
(36):
proton-coupled amino-acid transporter
SLC36A1
SLC36A2
SLC36A3
SLC36A436A2
(37):
sugar-phosphate/phosphate exchanger
SLC37A1
SLC37A2
SLC37A3
SLC37A4
(38):
System A & N, sodium-coupled neutral amino-acid transporter
SLC38A1
SLC38A2
SLC38A3
SLC38A4
SLC38A5
SLC38A6
SLC38A10
(39):
metal ion transporter
SLC39A1
SLC39A2
SLC39A3
SLC39A4
SLC39A5
SLC39A6
SLC39A7
SLC39A8
SLC39A9
SLC39A10
SLC39A11
SLC39A12
SLC39A13
SLC39A14
(40):
basolateral iron transporter
SLC40A1
[show]
SLC41–48
(41):
Magnesium transporter E
SLC41A1
SLC41A2
SLC41A3
(42):
Ammonia transporter
RhAG
RhBG
RhCG
(43):
Na+-independent, system-L like amino-acid transporter
SLC43A1
SLC43A2
SLC43A3
(44):
Choline-like transporter
SLC44A1
SLC44A2
SLC44A3
SLC44A4
SLC44A5
(45):
Putative sugar transporter
SLC45A1
SLC45A2
SLC54A3
SLC45A4
(46):
Folate transporter
SLC46A1
SLC46A2
(47):
multidrug and toxin extrusion
SLC47A1
SLC47A2
(48):
Heme transporter
[show]
SLCO1–4
O1A2
O1B1
O1B3
O2B1
O431
O4A1
[show]
Ion pumps
Symporter, Cotransporter
Na+/K+,Cl−
Na+/Pi3
Na+/Cl−
Na+/glucose
Na+/I−
Cl−/K+
4
5
Antiporter (exchanger)
Na+/H+
Na+/Ca2+
Na+/(Ca2+-K+) - Cl−/HCO−
3 (Band 3)
Cl−-formate
Cl−-oxalate
see also solute carrier disorders
[show]
v
t
e
Membrane transport protein: neurotransmitter transporters (TC 2.A.1.2)
Vesicular
Vesicular monoamine
VMAT1
VMAT2
Vesicular acetylcholine
Vesicular glutamate
Vesicular GABA
Other
Monoamine
DAT
NET
SERT
PMAT
Excitatory amino-acid transporter
GABA transporter
[show]
v
t
e
Membrane proteins, carrier proteins: membrane transport proteins ABC-transporter (TC 3A1)
A
A1
A2
A3
A4
A7
A8
A12
A13
B
B1
B2-3 (B2
B3)
B4
B5
B6
B7
B9
B11
C
C1
C2
C3
C4
C5
C6
C7
C8-9 (C8, C9)
C10
C11
C13
D
D1
D2
D3
D4
E
E1
F
F1
F2
G
G1
G2
G4
Sterolin (G5, G8)
see also ABC transporter disorders
[show]
v
t
e
Membrane transport protein: ion pumps, ATPases / ATP synthase (TC 3A2-3A3)
F-, V-, and A-type ATPase (3.A.2)
H+ (F-type)
H+ transporting, mitochondrial: ATP5A1
ATP5B
ATP5C1
ATP5C2
ATP5D
ATP5E
ATP5F1
ATP5G1
ATP5G2
ATP5G3
ATP5H
ATP5I
ATP5J
ATP5J2
ATP5L
ATP5L2
ATP5O
ATP5S
H+ (V-type)
H+ transporting, lysosomal: ATP6AP1
ATP6AP2
ATP6V1A
ATP6V1B1
ATP6V1B2
ATP6V1C1
ATP6V1C2
ATP6V1D
ATP6V1E1
ATP6V1E2
ATP6V1F
ATP6V1G1
ATP6V1G2
ATP6V1G3
ATP6V1H
ATP6V0A1
ATP6V0A2
ATP6V0A4
ATP6V0B
ATP6V0C
ATP6V0D1
ATP6V0D2
ATP6V0E
ATP6V0E1
TCIRG1
A-ATPase
found in Archea
P-type ATPase (3.A.3)
3.A.3.1.1: Na+/K+ transporting: ATP1A1
ATP1A2
ATP1A3
ATP1A4
ATP1B1
ATP1B2
ATP1B3
ATP1B4
ATP1G1
3.A.3.1.2: H+/K+
H+/K+ exchanging: ATP4A
ATP4B
3.A.3.1.4: H+/K+ transporting, nongastric: ATP12A
3.A.3.2: Ca2+ (SERCA, PMCA, SPCA) / Ca2+ transporting: ATP2A1
ATP2A2
ATP2A3
ATP2B1
ATP2B2
ATP2B3
ATP2B4
ATP2C1
3.A.3.5: Cu2+ transporting: ATP7A
ATP7B
3.A.3.8.8: flippase: ATP8A2
Other/ungrouped:
Na+/K+ – H+
Mg2+ transporting: ATP3
Class I, type 8: ATP8A1
ATP8B1
ATP8B2
ATP8B3
ATP8B4
Class II, type 9: ATP9A
ATP9B
Class V, type 10: ATP10A
ATP10B
ATP10D
Class VI, type 11: ATP11A
ATP11B
ATP11C
type 13: ATP13A1
ATP13A2
ATP13A3
ATP13A4
ATP13A5
see also ATPase disorders
Retrieved from "https://en.wikipedia.org/w/index.php?title=Membrane_transport_protein&oldid=841862195"
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Zinc efflux

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text:
I Got a Line on You
From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
"I Got a Line on You"
Single by Spirit
from the album The Family That Plays Together
B-side
"She Smiled"
Released
1968
Genre
Rock
Length
2:37
Label
Ode Records
Songwriter(s)
Randy California
Producer(s)
Lou Adler
Spirit singles chronology
"Mechanical World"
(1968) "I Got a Line on You"
(1968) "Dark Eyed Woman"
(1969)
"Mechanical World"
(1968) "I Got a Line on You"
(1968) "Dark Eyed Woman"
(1969)
"I Got a Line on You"
Song by Spirit
from the album The Family That Plays Together
Released
October, 1968
Recorded
March 11-September 18, 1968
Genre
Rock
Length
2:39
Label
Ode Records
Songwriter(s)
Randy California
Producer(s)
Lou Adler
"I Got a Line on You" is a rock song by American rock band Spirit, originally recorded during the sessions for their second album, The Family That Plays Together, between March 11 and September 18, 1968. The song was composed by guitarist/singer Randy California, recorded in sessions produced by Lou Adler. The single credits engineering by Eric Wienbang. Released as a single ahead of the album by Ode Records in the US in October 1968,[1] it began a slow rise up the charts.
It was picked up by college radio in late November.[2] It was the second single released by the band. The B-side was "She Smiled" (Ode catalog number ZS7-115).[3] 2:37 in length, the song finally peaked at #25 on the U.S. Top 100 on March 15, 1969, and #28 in Canada, March 24th.[4]
Some international versions were released later in 1968 and early 1969, distributed by CBS Records or Columbia Records. Some were produced in psychedelic colored vinyl patterns, while the Ode release was on plain black vinyl with a plain yellow label.[5] The album version was slightly longer at 2:39, while the greatest hits version is timed at 2:41. A 7:34 version appears on the band's final reunion album, 1984's The Thirteenth Dream.
Reviews[edit]
A Billboard review brief called it "the near definitive rock single".[6] Matthew Greenwald of AllMusic said it is "Driven by a fabulously funky guitar riff and some very accessible lyrics, the song is a rock classic from beginning to end."[7]
Cover versions[edit]
The song has been covered by Blackfoot, Patrick Cowley, Alice Cooper, Jeff Healey, Juicy Lucy, Who Watchiz Ze Watchmain,[8] Ile Kallio,[9] Kim Mitchell, Mushroom with Gary Floyd,[10] The Woggles,[11] and most recently by the supergroup Hollywood Vampires. Cover versions by Joe Moss[12] and the Danish band Lost and Found were released as "I've Got A Line On You".[13] Country band 1880 released a version titled "I Gotta Line on You".[14] Because of the lyrics, occasionally "Babe" has been added to the end of the song title.
References[edit]
Jump up ^ "45cat - Spirit - I Got A Line On You / She Smiles - Ode - USA - ZS7 115". 45cat.com.
Jump up ^ https://books.google.com/books?id=G0UEAAAAMBAJ&pg=RA1-PA80&lpg=RA1-PA80&dq=%22I%27ve+got+a+line+on+you%22+billboard&source=bl&ots=CNEK_TSzpA&sig=gQQKop0I7mb0ndfvCdaAfdS-AZ8&hl=en&sa=X&ei=IJ90VdD5OIbUoASC7YEY&ved=0CCYQ6AEwAw#v=onepage&q=%22I've%20got%20a%20line%20on%20you%22%20billboard&f=false Billboard November 30, 1968
Jump up ^ "B". badcatrecords.com.
Jump up ^ "RPM" (PDF).
Jump up ^ "45cat - Spirit - I Got A Line On You / She Smiles - CBS - Germany - 3880". 45cat.com.
Jump up ^ "Billboard Album Reviews". Billboard. July 8, 1972. p. 45. Retrieved 2016-06-16.
Jump up ^ Matthew Greenwald. "I Got a Line on You – Spirit – Listen, Appearances, Song Review – AllMusic". AllMusic.
Jump up ^ "Tent of miracles - the unofficial Spirit homepage - CoversUnreleased". erjobe.info.
Jump up ^ "Ile Kallio". secondhandsongs.com.
Jump up ^ "Mushroom with Gary Floyd". secondhandsongs.com.
Jump up ^ "Discogs reference".
Jump up ^ "I've Got a Line On You / Build Me Up Butter Cup by Joe Moss [60s] (Single): Reviews, Ratings, Credits, Song list - Rate Your Music". rateyourmusic.com.
Jump up ^ http://www.discogs.com/Lost-Found-Ive-Been-Hurt-Ive-Got-A-Line-On-You/master/741572
Jump up ^ "1880". secondhandsongs.com.
hide
v
t
e
Spirit
Mark Andes
Randy California
Ed Cassidy
Jay Ferguson
John Locke
Al Staehely
Dave Waterbury
Studio albums
Spirit (1968)
The Family That Plays Together (1969)
Clear (1969)
Twelve Dreams of Dr. Sardonicus (1970)
Feedback (1972)
Spirit of '76 (1975)
Son of Spirit (1975)
Farther Along (1976)
Future Games (1977)
...Potato Land (1981)
The Thirteenth Dream (1984)
Rapture in the Chambers (1988)
Tent of Miracles (1990)
California Blues (1996)
Live albums
Live at La Paloma (1993)
Live from the Time Coast (2004)
Compilations
Time Circle, 1968–1972 (1991)
Chronicles, 1967–1992 (1992)
Soundtrack
Model Shop (1968)
Retrieved from "https://en.wikipedia.org/w/index.php?title=I_Got_a_Line_on_You&oldid=815473705"
Categories:
1968 songs
Song recordings produced by Lou Adler
Songs written by Randy California
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This page was last edited on 15 December 2017, at 01:22 (UTC).
Text is available under the Creative Commons Attribution-ShareAlike License; additional terms may apply. By using this site, you agree to the Terms of Use and Privacy Policy. Wikipedia® is a registered trademark of the Wikimedia Foundation, Inc., a non-profit organization.
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/wiki/I_Got_a_Line_on_You
View the content page [ctrl-alt-c]
c

values: Discussion about the content page [ctrl-alt-t]

values: p-namespaces navigation vectorTabs p-namespaces-label

values:
p-variants
navigation
vectorMenu emptyPortlet
p-variants-label

values: Past revisions of this page [ctrl-alt-h]

values: p-views navigation vectorTabs p-views-label

values:
p-cactions
navigation
vectorMenu emptyPortlet
p-cactions-label

values:
mw-wiki-logo
/wiki/Main_Page
Visit the main page

values:
/wiki/Main_Page
Visit the main page [ctrl-alt-z]
z

values: Featured content – the best of Wikipedia

values: Find background information on current events

values:
/wiki/Special:Random
Load a random article [ctrl-alt-x]
x

values: portal navigation p-navigation p-navigation-label

values: Guidance on how to use and edit Wikipedia

values: About the project, what you can do, where to find things

values: A list of recent changes in the wiki [ctrl-alt-r]

values: portal navigation p-interaction p-interaction-label

values: List of all English Wikipedia pages containing links to this page [ctrl-alt-j]

values: Recent changes in pages linked from this page [ctrl-alt-k]

values:
/wiki/Wikipedia:File_Upload_Wizard
Upload files [ctrl-alt-u]
u

values: A list of all special pages [ctrl-alt-q]

values: Permanent link to this revision of the page

values: Link to connected data repository item [ctrl-alt-g]

values: /static/images/wikimedia-button-1.5x.png 1.5x, /static/images/wikimedia-button-2x.png 2x

values: /static/images/poweredby_mediawiki_132x47.png 1.5x, /static/images/poweredby_mediawiki_176x62.png 2x

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