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Solute carrier family 22 member 1 (Organic cation transporter 1) (rOCT1)

 S22A1_RAT               Reviewed;         556 AA.
Q63089; O35882; Q6AYW1;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
23-MAY-2018, entry version 128.
RecName: Full=Solute carrier family 22 member 1;
AltName: Full=Organic cation transporter 1;
Short=rOCT1;
Name=Slc22a1; Synonyms=Oct1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=7990927; DOI=10.1038/372549a0;
Gruendemann D., Gorboulev V., Gambaryan S., Veyhl M., Koepsell H.;
"Drug excretion mediated by a new prototype of polyspecific
transporter.";
Nature 372:549-552(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=9195965; DOI=10.1074/jbc.272.26.16548;
Zhang L., Dresser M.J., Chun J.K., Babbitt P.C., Giacomini K.M.;
"Cloning and functional characterization of a rat renal organic cation
transporter isoform (rOCT1A).";
J. Biol. Chem. 272:16548-16554(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=8955087; DOI=10.1074/jbc.271.51.32599;
Busch A.E., Quester S., Ulzheimer J.C., Waldegger S., Gorboulev V.,
Arndt P., Lang F., Koepsell H.;
"Electrogenic properties and substrate specificity of the polyspecific
rat cation transporter rOCT1.";
J. Biol. Chem. 271:32599-32604(1996).
[5]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9703985; DOI=10.1006/bbrc.1998.9034;
Meyer-Wentrup F., Karbach U., Gorboulev V., Arndt P., Koepsell H.;
"Membrane localization of the electrogenic cation transporter rOCT1 in
rat liver.";
Biochem. Biophys. Res. Commun. 248:673-678(1998).
[6]
FUNCTION.
PubMed=9776363; DOI=10.1038/sj.bjp.0702065;
Breidert T., Spitzenberger F., Gruendemann D., Schoemig E.;
"Catecholamine transport by the organic cation transporter type 1
(OCT1).";
Br. J. Pharmacol. 125:218-224(1998).
[7]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=9808712;
Urakami Y., Okuda M., Masuda S., Saito H., Inui K.;
"Functional characteristics and membrane localization of rat
multispecific organic cation transporters, OCT1 and OCT2, mediating
tubular secretion of cationic drugs.";
J. Pharmacol. Exp. Ther. 287:800-805(1998).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10997918;
Karbach U., Kricke J., Meyer-Wentrup F., Gorboulev V., Volk C.,
Loffing-Cueni D., Kaissling B., Bachmann S., Koepsell H.;
"Localization of organic cation transporters OCT1 and OCT2 in rat
kidney.";
Am. J. Physiol. 279:F679-F687(2000).
[9]
FUNCTION.
PubMed=11502595;
Arndt P., Volk C., Gorboulev V., Budiman T., Popp C.,
Ulzheimer-Teuber I., Akhoundova A., Koppatz S., Bamberg E., Nagel G.,
Koepsell H.;
"Interaction of cations, anions, and weak base quinine with rat renal
cation transporter rOCT2 compared with rOCT1.";
Am. J. Physiol. 281:F454-F468(2001).
[10]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11792693; DOI=10.1124/dmd.30.2.212;
Slitt A.L., Cherrington N.J., Hartley D.P., Leazer T.M.,
Klaassen C.D.;
"Tissue distribution and renal developmental changes in rat organic
cation transporter mRNA levels.";
Drug Metab. Dispos. 30:212-219(2002).
[11]
INDUCTION.
PubMed=15122767; DOI=10.1002/hep.20176;
Denk G.U., Soroka C.J., Mennone A., Koepsell H., Beuers U.,
Boyer J.L.;
"Down-regulation of the organic cation transporter 1 of rat liver in
obstructive cholestasis.";
Hepatology 39:1382-1389(2004).
[12]
FUNCTION.
PubMed=16142924; DOI=10.1021/bi050676c;
Keller T., Elfeber M., Gorboulev V., Reilaender H., Koepsell H.;
"Purification and functional reconstitution of the rat organic cation
transporter OCT1.";
Biochemistry 44:12253-12263(2005).
[13]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15640376; DOI=10.1124/dmd.104.002519;
Ishiguro N., Saito A., Yokoyama K., Morikawa M., Igarashi T.,
Tamai I.;
"Transport of the dopamine D2 agonist pramipexole by rat organic
cation transporters OCT1 and OCT2 in kidney.";
Drug Metab. Dispos. 33:495-499(2005).
[14]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16272756; DOI=10.2133/dmpk.20.379;
Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T.,
Inui K.;
"Metformin is a superior substrate for renal organic cation
transporter OCT2 rather than hepatic OCT1.";
Drug Metab. Pharmacokinet. 20:379-386(2005).
[15]
MUTAGENESIS OF SER-286; SER-292; THR-296; SER-328 AND THR-550, AND
PHOSPHORYLATION.
PubMed=15829703; DOI=10.1681/ASN.2004040256;
Ciarimboli G., Koepsell H., Iordanova M., Gorboulev V., Durner B.,
Lang D., Edemir B., Schroter R., Van Le T., Schlatter E.;
"Individual PKC-phosphorylation sites in organic cation transporter 1
determine substrate selectivity and transport regulation.";
J. Am. Soc. Nephrol. 16:1562-1570(2005).
[16]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16581093; DOI=10.1016/j.neuropharm.2006.01.005;
Amphoux A., Vialou V., Drescher E., Bruess M., Mannoury La Cour C.,
Rochat C., Millan M.J., Giros B., Boenisch H., Gautron S.;
"Differential pharmacological in vitro properties of organic cation
transporters and regional distribution in rat brain.";
Neuropharmacology 50:941-952(2006).
[17]
FUNCTION, AND MUTAGENESIS OF CYS-26; CYS-155; CYS-179; CYS-322;
CYS-358; CYS-418; CYS-437; CYS-451; CYS-470 AND CYS-474.
PubMed=17567940; DOI=10.1152/ajprenal.00106.2007;
Sturm A., Gorboulev V., Gorbunov D., Keller T., Volk C., Schmitt B.M.,
Schlachtbauer P., Ciarimboli G., Koepsell H.;
"Identification of cysteines in rat organic cation transporters rOCT1
(C322, C451) and rOCT2 (C451) critical for transport activity and
substrate affinity.";
Am. J. Physiol. 293:F767-F779(2007).
[18]
INDUCTION.
PubMed=17553914; DOI=10.1124/dmd.107.015842;
Maeda T., Oyabu M., Yotsumoto T., Higashi R., Nagata K., Yamazoe Y.,
Tamai I.;
"Effect of pregnane X receptor ligand on pharmacokinetics of
substrates of organic cation transporter Oct1 in rats.";
Drug Metab. Dispos. 35:1580-1586(2007).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Translocates a broad array of organic cations with
various structures and molecular weights including the model
compounds 1-methyl-4-phenylpyridinium (MPP), tetraethylammonium
(TEA), N-1-methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-
N-methylpyridinium (ASP), the endogenous compounds choline,
guanidine, histamine, epinephrine, adrenaline, noradrenaline and
dopamine, and the drugs quinine, and metformin. The transport of
organic cations is inhibited by a broad array of compounds like
tetramethylammonium (TMA), cocaine, lidocaine, NMDA receptor
antagonists, atropine, prazosin, cimetidine, TEA and NMN,
guanidine, cimetidine, choline, procainamide, quinine,
tetrabutylammonium, and tetrapentylammonium. Translocates organic
cations in an electrogenic and pH-independent manner. Translocates
organic cations across the plasma membrane in both directions.
Transports the polyamines spermine and spermidine. Transports
pramipexole across the basolateral membrane of the proximal
tubular epithelial cells. The choline transport is activated by
MMTS. Regulated by various intracellular signaling pathways
including inhibition by protein kinase A activation, and
endogenously activation by the calmodulin complex, the calmodulin-
dependent kinase II and LCK tyrosine kinase.
{ECO:0000269|PubMed:11502595, ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16142924, ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:16581093, ECO:0000269|PubMed:17567940,
ECO:0000269|PubMed:7990927, ECO:0000269|PubMed:8955087,
ECO:0000269|PubMed:9195965, ECO:0000269|PubMed:9776363,
ECO:0000269|PubMed:9808712}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=3.73 mM for metformin {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=42 uM for TEA {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=9.6 uM for MPP {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=0.34 mM for NMN {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=1.1 mM for choline {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=49.5 uM for pramipexole {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=1.6 mM for dopamine {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=0.9 mM for serotonin {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=0.8 mM for norepinephrine {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
KM=1.1 mM for epinephrine {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
Vmax=145 pmol/min/mg enzyme uptake {ECO:0000269|PubMed:15640376,
ECO:0000269|PubMed:16272756, ECO:0000269|PubMed:16581093,
ECO:0000269|PubMed:8955087, ECO:0000269|PubMed:9195965};
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-5261153, EBI-5261153;
-!- SUBCELLULAR LOCATION: Basolateral cell membrane
{ECO:0000269|PubMed:10997918, ECO:0000269|PubMed:7990927,
ECO:0000269|PubMed:9703985, ECO:0000269|PubMed:9808712}; Multi-
pass membrane protein {ECO:0000269|PubMed:10997918,
ECO:0000269|PubMed:7990927, ECO:0000269|PubMed:9703985,
ECO:0000269|PubMed:9808712}. Note=Within sinusoidal membrane of
hepatocytes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q63089-1; Sequence=Displayed;
Name=2; Synonyms=rOCT1A;
IsoId=Q63089-2; Sequence=VSP_033591, VSP_033592;
-!- TISSUE SPECIFICITY: Expressed in kidney, kidney cortex, kidney
medulla, liver, intestine and colon. Expressed in proximal tubules
in kidney, hepatocytes in liver and enterocytes of villi and
crypts in smallintestine. Expressed throughout the liver lobuli.
Expressed in hepatocytes surrounding the central veins (at protein
level). Expressed in S1, S2 segments of proximal tubules in kidney
(at protein level). Highly expressed in kidney and spleen,
moderately in skin, and weakly in the gastrointestinal tract,
brain, lung, thymus, muscle, and prostate. Weakly expressed in
some white matter regions like the corpus callosum and in the
granular layer of the cerebellum. {ECO:0000269|PubMed:10997918,
ECO:0000269|PubMed:11792693, ECO:0000269|PubMed:7990927,
ECO:0000269|PubMed:9195965, ECO:0000269|PubMed:9703985}.
-!- DEVELOPMENTAL STAGE: Renal level increases gradually from
postnatal day 0 through day 45 in both genders.
{ECO:0000269|PubMed:11792693}.
-!- INDUCTION: Down-regulated in obstructive cholestasis. Up-regulated
by treatment with pregnenolone-16 alpha-carbonitrile (PCN) and by
overexpression of pregnane X receptor (PXR).
{ECO:0000269|PubMed:15122767, ECO:0000269|PubMed:17553914}.
-!- PTM: Phosphorylated. {ECO:0000269|PubMed:15829703}.
-!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
superfamily. Organic cation transporter (TC 2.A.1.19) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH78883.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; X78855; CAA55411.1; -; mRNA.
EMBL; U76379; AAB67702.1; -; mRNA.
EMBL; BC078883; AAH78883.1; ALT_INIT; mRNA.
PIR; S50862; S50862.
RefSeq; NP_036829.1; NM_012697.1. [Q63089-1]
UniGene; Rn.11186; -.
ProteinModelPortal; Q63089; -.
IntAct; Q63089; 1.
STRING; 10116.ENSRNOP00000022254; -.
BindingDB; Q63089; -.
ChEMBL; CHEMBL2073670; -.
TCDB; 2.A.1.19.1; the major facilitator superfamily (mfs).
iPTMnet; Q63089; -.
PhosphoSitePlus; Q63089; -.
PaxDb; Q63089; -.
PRIDE; Q63089; -.
Ensembl; ENSRNOT00000022068; ENSRNOP00000022068; ENSRNOG00000016337. [Q63089-2]
Ensembl; ENSRNOT00000022254; ENSRNOP00000022254; ENSRNOG00000016337. [Q63089-1]
GeneID; 24904; -.
KEGG; rno:24904; -.
CTD; 6580; -.
RGD; 3224; Slc22a1.
eggNOG; ENOG410IRH7; Eukaryota.
eggNOG; ENOG410XR5P; LUCA.
GeneTree; ENSGT00760000118852; -.
HOGENOM; HOG000234568; -.
HOVERGEN; HBG061545; -.
InParanoid; Q63089; -.
KO; K08198; -.
OMA; ILMYLWF; -.
OrthoDB; EOG091G05AC; -.
PhylomeDB; Q63089; -.
Reactome; R-RNO-112311; Neurotransmitter clearance.
Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
Reactome; R-RNO-2161517; Abacavir transmembrane transport.
Reactome; R-RNO-442660; Na+/Cl- dependent neurotransmitter transporters.
Reactome; R-RNO-549127; Organic cation transport.
PRO; PR:Q63089; -.
Proteomes; UP000002494; Chromosome 1.
Bgee; ENSRNOG00000016337; -.
Genevisible; Q63089; RN.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:MGI.
GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IDA:RGD.
GO; GO:0005329; F:dopamine transmembrane transporter activity; IDA:RGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008504; F:monoamine transmembrane transporter activity; IDA:RGD.
GO; GO:0005333; F:norepinephrine transmembrane transporter activity; IDA:RGD.
GO; GO:0008514; F:organic anion transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:RGD.
GO; GO:0042803; F:protein homodimerization activity; IDA:RGD.
GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:RGD.
GO; GO:0008513; F:secondary active organic cation transmembrane transporter activity; IDA:RGD.
GO; GO:0015872; P:dopamine transport; IDA:RGD.
GO; GO:0006855; P:drug transmembrane transport; IDA:RGD.
GO; GO:0048241; P:epinephrine transport; IDA:RGD.
GO; GO:0010248; P:establishment or maintenance of transmembrane electrochemical gradient; IDA:RGD.
GO; GO:0015844; P:monoamine transport; IDA:RGD.
GO; GO:0015874; P:norepinephrine transport; IDA:RGD.
GO; GO:0015695; P:organic cation transport; IDA:RGD.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0015697; P:quaternary ammonium group transport; IDA:RGD.
CDD; cd06174; MFS; 1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR004749; Orgcat_transp/SVOP.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF00083; Sugar_tr; 1.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00898; 2A0119; 1.
PROSITE; PS50850; MFS; 1.
PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Ion transport; Membrane; Phosphoprotein; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 556 Solute carrier family 22 member 1.
/FTId=PRO_0000333879.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 150 Extracellular. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TOPO_DOM 172 177 Cytoplasmic. {ECO:0000255}.
TRANSMEM 178 198 Helical. {ECO:0000255}.
TOPO_DOM 199 211 Extracellular. {ECO:0000255}.
TRANSMEM 212 231 Helical. {ECO:0000255}.
TOPO_DOM 232 238 Cytoplasmic. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 263 Extracellular. {ECO:0000255}.
TRANSMEM 264 284 Helical. {ECO:0000255}.
TOPO_DOM 285 348 Cytoplasmic. {ECO:0000255}.
TRANSMEM 349 369 Helical. {ECO:0000255}.
TOPO_DOM 370 377 Extracellular. {ECO:0000255}.
TRANSMEM 378 398 Helical. {ECO:0000255}.
TOPO_DOM 399 403 Cytoplasmic. {ECO:0000255}.
TRANSMEM 404 424 Helical. {ECO:0000255}.
TOPO_DOM 425 429 Extracellular. {ECO:0000255}.
TRANSMEM 430 452 Helical. {ECO:0000255}.
TOPO_DOM 453 465 Cytoplasmic. {ECO:0000255}.
TRANSMEM 466 486 Helical. {ECO:0000255}.
TOPO_DOM 487 493 Extracellular. {ECO:0000255}.
TRANSMEM 494 514 Helical. {ECO:0000255}.
TOPO_DOM 515 556 Cytoplasmic. {ECO:0000255}.
SITE 451 451 Involved in affinity and selectivity of
cations as well as in translocation.
MOD_RES 334 334 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 543 543 Phosphothreonine.
{ECO:0000250|UniProtKB:O15245}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 1 126 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9195965}.
/FTId=VSP_033591.
VAR_SEQ 127 172 VYDTPGSSIVTEFNLVCGDAWKVDLFQSCVNLGFFLGSLVV
GYIAD -> MRWTGTRAPLTVWTHCPAWLPTGVSCHWAPAS
MAGYTTLPAPPSSL (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9195965}.
/FTId=VSP_033592.
MUTAGEN 26 26 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
155; A-179; S-322; A-358; A-418; S-437;
A-470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 155 155 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-179; S-322; A-358; A-418; S-437; A-
470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 179 179 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; S-322; A-358; A-418; S-437; A-
470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 286 286 S->A: No effect of PKC-induced
stimulation on ASP uptake. No effect of
PKC-induced stimulation on ASP uptake;
when associated with A-292; A-296; A-328
and A-550. No effect of PKA activation on
ASP uptake. No effect of PKA activation
on ASP uptake; when associated with A-
292; A-296; A-328 and A-550. Significant
reduction of ASP uptake by p56(lck)
tyrosine kinase-induced inhibition.
Significant reduction of ASP uptake by
p56(lck) tyrosine kinase-induced
inhibition; when associated with A-292;
A-296; A-328 and A-550. No significant
effect on trafficking from intracellular
pools to the cell membrane; when
associated with A-292; A-296; A-328 and
A-550. suppresses phosphorylation by PKC;
when associated with A-292; A-296; A-328
and A-550. {ECO:0000269|PubMed:15829703}.
MUTAGEN 292 292 S->A: No effect of PKC-induced
stimulation on ASP uptake. No effect of
PKC-induced stimulation on ASP uptake;
when associated with A-286; A-296; A-328
and A-550. No effect of PKA activation on
ASP uptake. No effect of PKA activation
on ASP uptake; when associated with A-
286; A-296; A-328 and A-550. Significant
reduction of ASP uptake by p56(lck)
tyrosine kinase-induced inhibition.
Significant reduction of ASP uptake by
p56(lck) tyrosine kinase-induced
inhibition; when associated with A-286;
A-296; A-328 and A-550. No significant
effect on trafficking from intracellular
pools to the cell membrane; when
associated with A-286; A-296; A-328 and
A-550. suppresses phosphorylation by PKC;
when associated with A-286; A-296; A-328
and A-550. {ECO:0000269|PubMed:15829703}.
MUTAGEN 296 296 T->A: No effect of PKC-induced
stimulation on ASP uptake. No effect of
PKC-induced stimulation on ASP uptake;
when associated with A-286; A-292; A-328;
A-550. Significant increase of the ASP
uptake by PKA activation. No effect of
PKA activation on ASP uptake; when
associated with A-286; A-292; A-328; A-
550. Significant reduction of ASP uptake
by p56(lck) tyrosine kinase-induced
inhibition. Significant reduction of ASP
uptake by p56(lck) tyrosine kinase-
induced inhibition; when associated with
A-286; A-292; A-328; A-550. No
significant effect on trafficking from
intracellular pools to the cell membrane;
when associated with A-286; A-292; A-328
and A-550. suppresses phosphorylation by
PKC; when associated with A-286; A-292;
A-328 and A-550.
{ECO:0000269|PubMed:15829703}.
MUTAGEN 322 322 C->S: Reduces the activation by MMTS.
Abolishes the activation by MMTs; when
associated with M-451. Choline affinity
is increased fivefold by MMTS. Choline
affinity is increased fourfold by MMTS;
when associated with A-26; A-155; A-179;
A-358; A-418; S-437; A-470 and A-474.
Choline affinity is increased four-to
fivefold; when associated with M-451.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 328 328 S->A: No effect of PKC-induced
stimulation on ASP uptake. No effect of
PKC-induced stimulation on ASP uptake;
when associated with A-286; A-292; A-296
and A-550. No effect of PKA activation on
ASP uptake. No effect of PKA activation
on ASP uptake; when associated with A-
286; A-292; A-296 and A-550. Significant
reduction of ASP uptake by p56(lck)
tyrosine kinase-induced inhibition.
Significant reduction of ASP uptake by
p56(lck) tyrosine kinase-induced
inhibition; when associated with A-286;
A-292; A-296; A-550. No significant
effect on trafficking from intracellular
pools to the cell membrane; when
associated with A-286; A-292; A-296 and
A-550. suppresses phosphorylation by PKC;
when associated with A-286; A-292; A-296
and A-550. {ECO:0000269|PubMed:15829703}.
MUTAGEN 358 358 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; A-179; S-322; A-418; S-437; A-
470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 418 418 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; A-179; S-322; A-358; S-437; A-
470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 437 437 C->S: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; A-179; S-322; A-358; A-418; A-
470 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 451 451 C->M: Reduces the activation by MMTS.
Abolishes the activation by MMTs; when
associated with S-322. Abolishes the
effect of MMTs on choline-induced
currents. Choline affinity is not
influenced by MMTS. Choline affinity is
increased four-to fivefold; when
associated with S-322.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 470 470 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; A-179; S-322; A-358; A-418; A-
437 and A-474.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 474 474 C->A: Choline affinity is increased
fourfold by MMTS; when associated with A-
26; A-155; A-179; S-322; A-358; A-418; A-
437 and A-470.
{ECO:0000269|PubMed:17567940}.
MUTAGEN 550 550 T->A: No effect of PKC-induced
stimulation on ASP uptake. No effect of
PKC-induced stimulation on ASP uptake;
when associated with A-286; A-292; A-296;
A-328. Significant increase of the ASP
uptake by PKA activation. No effect of
PKA activation on ASP uptake; when
associated with A-286; A-292; A-296 and
A-328. Significant reduction of ASP
uptake by p56(lck) tyrosine kinase-
induced inhibition. Significant reduction
of ASP uptake by p56(lck) tyrosine
kinase-induced inhibition; when
associated with A-286; A-292; A-296; A-
328. No significant effect on trafficking
from intracellular pools to the cell
membrane; when associated with A-286; A-
292; A-296 and A-328. suppresses
phosphorylation by PKC; when associated
with A-286; A-292; A-296 and A-328.
{ECO:0000269|PubMed:15829703}.
SEQUENCE 556 AA; 61541 MW; 9F42131CCCEC0920 CRC64;
MPTVDDVLEQ VGEFGWFQKQ AFLLLCLISA SLAPIYVGIV FLGFTPGHYC QNPGVAELSQ
RCGWSQAEEL NYTVPGLGPS DEASFLSQCM RYEVDWNQST LDCVDPLSSL VANRSQLPLG
PCEHGWVYDT PGSSIVTEFN LVCGDAWKVD LFQSCVNLGF FLGSLVVGYI ADRFGRKLCL
LVTTLVTSVS GVLTAVAPDY TSMLLFRLLQ GMVSKGSWVS GYTLITEFVG SGYRRTTAIL
YQMAFTVGLV GLAGVAYAIP DWRWLQLAVS LPTFLFLLYY WFVPESPRWL LSQKRTTRAV
RIMEQIAQKN GKVPPADLKM LCLEEDASEK RSPSFADLFR TPNLRKHTVI LMYLWFSCAV
LYQGLIMHVG ATGANLYLDF FYSSLVEFPA AFIILVTIDR IGRIYPIAAS NLVTGAACLL
MIFIPHELHW LNVTLACLGR MGATIVLQMV CLVNAELYPT FIRNLGMMVC SALCDLGGIF
TPFMVFRLME VWQALPLILF GVLGLTAGAM TLLLPETKGV ALPETIEEAE NLGRRKSKAK
ENTIYLQVQT GKSSST


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