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Protein

Solute carrier family 22 member 1

Gene

Slc22a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.11 Publications

Kineticsi

  1. KM=3.73 mM for metformin5 Publications
  2. KM=42 µM for TEA5 Publications
  3. KM=9.6 µM for MPP5 Publications
  4. KM=0.34 mM for NMN5 Publications
  5. KM=1.1 mM for choline5 Publications
  6. KM=49.5 µM for pramipexole5 Publications
  7. KM=1.6 mM for dopamine5 Publications
  8. KM=0.9 mM for serotonin5 Publications
  9. KM=0.8 mM for norepinephrine5 Publications
  10. KM=1.1 mM for epinephrine5 Publications
  1. Vmax=145 pmol/min/mg enzyme uptake5 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei451 – 4511Involved in affinity and selectivity of cations as well as in translocation

GO - Molecular functioni

  • acetylcholine transmembrane transporter activity Source: RGD
  • dopamine transmembrane transporter activity Source: RGD
  • identical protein binding Source: IntAct
  • monoamine transmembrane transporter activity Source: RGD
  • norepinephrine transmembrane transporter activity Source: RGD
  • organic cation transmembrane transporter activity Source: RGD
  • protein homodimerization activity Source: RGD
  • quaternary ammonium group transmembrane transporter activity Source: RGD
  • secondary active organic cation transmembrane transporter activity Source: RGD

GO - Biological processi

  • acetate ester transport Source: GOC
  • ammonium transmembrane transport Source: GOC
  • dopamine transport Source: RGD
  • drug transmembrane transport Source: RGD
  • epinephrine transport Source: RGD
  • establishment or maintenance of transmembrane electrochemical gradient Source: RGD
  • monoamine transport Source: RGD
  • neurotransmitter transport Source: GOC
  • norepinephrine transport Source: RGD
  • organic cation transport Source: RGD
  • protein homooligomerization Source: RGD
  • quaternary ammonium group transport Source: RGD
Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-2161517. Abacavir transmembrane transport.
R-RNO-549127. Organic cation transport.

Protein family/group databases

TCDBi2.A.1.19.1. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 22 member 1
Alternative name(s):
Organic cation transporter 1
Short name:
rOCT1
Gene namesi
Name:Slc22a1
Synonyms:Oct1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi3224. Slc22a1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Topological domaini43 – 150108ExtracellularSequence analysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence analysisAdd
BLAST
Topological domaini172 – 1776CytoplasmicSequence analysis
Transmembranei178 – 19821HelicalSequence analysisAdd
BLAST
Topological domaini199 – 21113ExtracellularSequence analysisAdd
BLAST
Transmembranei212 – 23120HelicalSequence analysisAdd
BLAST
Topological domaini232 – 2387CytoplasmicSequence analysis
Transmembranei239 – 25921HelicalSequence analysisAdd
BLAST
Topological domaini260 – 2634ExtracellularSequence analysis
Transmembranei264 – 28421HelicalSequence analysisAdd
BLAST
Topological domaini285 – 34864CytoplasmicSequence analysisAdd
BLAST
Transmembranei349 – 36921HelicalSequence analysisAdd
BLAST
Topological domaini370 – 3778ExtracellularSequence analysis
Transmembranei378 – 39821HelicalSequence analysisAdd
BLAST
Topological domaini399 – 4035CytoplasmicSequence analysis
Transmembranei404 – 42421HelicalSequence analysisAdd
BLAST
Topological domaini425 – 4295ExtracellularSequence analysis
Transmembranei430 – 45223HelicalSequence analysisAdd
BLAST
Topological domaini453 – 46513CytoplasmicSequence analysisAdd
BLAST
Transmembranei466 – 48621HelicalSequence analysisAdd
BLAST
Topological domaini487 – 4937ExtracellularSequence analysis
Transmembranei494 – 51421HelicalSequence analysisAdd
BLAST
Topological domaini515 – 55642CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • basolateral plasma membrane Source: RGD
  • integral component of plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi26 – 261C → 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. 1 Publication
Mutagenesisi155 – 1551C → 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. 1 Publication
Mutagenesisi179 – 1791C → 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. 1 Publication
Mutagenesisi286 – 2861S → 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 phosphopylation by PKC; when associated with A-292; A-296; A-328 and A-550. 1 Publication
Mutagenesisi292 – 2921S → 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 phosphopylation by PKC; when associated with A-286; A-296; A-328 and A-550. 1 Publication
Mutagenesisi296 – 2961T → 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. 1 Publication
Mutagenesisi322 – 3221C → 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. 1 Publication
Mutagenesisi328 – 3281S → 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 phosphopylation by PKC; when associated with A-286; A-292; A-296 and A-550. 1 Publication
Mutagenesisi358 – 3581C → 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. 1 Publication
Mutagenesisi418 – 4181C → 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. 1 Publication
Mutagenesisi437 – 4371C → 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. 1 Publication
Mutagenesisi451 – 4511C → 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. 1 Publication
Mutagenesisi470 – 4701C → 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. 1 Publication
Mutagenesisi474 – 4741C → 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. 1 Publication
Mutagenesisi550 – 5501T → 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 phosphopylation by PKC; when associated withA-286; A-292; A-296 and A-328. 1 Publication

Chemistry

ChEMBLiCHEMBL2073670.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 556556Solute carrier family 22 member 1PRO_0000333879Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi71 – 711N-linked (GlcNAc...)Sequence analysis
Modified residuei334 – 3341PhosphoserineCombined sources
Modified residuei543 – 5431PhosphothreonineBy similarity

Post-translational modificationi

Phosphorylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ63089.
PRIDEiQ63089.

PTM databases

iPTMnetiQ63089.
PhosphoSiteiQ63089.

Expressioni

Tissue specificityi

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.5 Publications

Developmental stagei

Renal level increases gradually from postnatal day 0 through day 45 in both genders.1 Publication

Inductioni

Down-regulated in obstructive cholestasis. Up-regulated by treatment with pregnenolone-16 alpha-carbonitrile (PCN) and by overexpression of pregnane X receptor (PXR).2 Publications

Gene expression databases

GenevisibleiQ63089. RN.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
itself4EBI-5261153,EBI-5261153

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: RGD

Protein-protein interaction databases

IntActiQ63089. 1 interaction.
MINTiMINT-8292690.
STRINGi10116.ENSRNOP00000022254.

Chemistry

BindingDBiQ63089.

Structurei

3D structure databases

ProteinModelPortaliQ63089.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410IRH7. Eukaryota.
ENOG410XR5P. LUCA.
GeneTreeiENSGT00760000118852.
HOGENOMiHOG000234568.
HOVERGENiHBG061545.
InParanoidiQ63089.
KOiK08198.
OMAiDLFQSCL.
OrthoDBiEOG78PV8N.
PhylomeDBiQ63089.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR004749. Orgcat_transp/SVOP.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00898. 2A0119. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q63089-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPTVDDVLEQ VGEFGWFQKQ AFLLLCLISA SLAPIYVGIV FLGFTPGHYC
60 70 80 90 100
QNPGVAELSQ RCGWSQAEEL NYTVPGLGPS DEASFLSQCM RYEVDWNQST
110 120 130 140 150
LDCVDPLSSL VANRSQLPLG PCEHGWVYDT PGSSIVTEFN LVCGDAWKVD
160 170 180 190 200
LFQSCVNLGF FLGSLVVGYI ADRFGRKLCL LVTTLVTSVS GVLTAVAPDY
210 220 230 240 250
TSMLLFRLLQ GMVSKGSWVS GYTLITEFVG SGYRRTTAIL YQMAFTVGLV
260 270 280 290 300
GLAGVAYAIP DWRWLQLAVS LPTFLFLLYY WFVPESPRWL LSQKRTTRAV
310 320 330 340 350
RIMEQIAQKN GKVPPADLKM LCLEEDASEK RSPSFADLFR TPNLRKHTVI
360 370 380 390 400
LMYLWFSCAV LYQGLIMHVG ATGANLYLDF FYSSLVEFPA AFIILVTIDR
410 420 430 440 450
IGRIYPIAAS NLVTGAACLL MIFIPHELHW LNVTLACLGR MGATIVLQMV
460 470 480 490 500
CLVNAELYPT FIRNLGMMVC SALCDLGGIF TPFMVFRLME VWQALPLILF
510 520 530 540 550
GVLGLTAGAM TLLLPETKGV ALPETIEEAE NLGRRKSKAK ENTIYLQVQT

GKSSST
Length:556
Mass (Da):61,541
Last modified:November 1, 1996 - v1
Checksum:i9F42131CCCEC0920
GO
Isoform 2 (identifier: Q63089-2) [UniParc]FASTAAdd to basket

Also known as: rOCT1A

The sequence of this isoform differs from the canonical sequence as follows:
     1-126: Missing.
     127-172: VYDTPGSSIV...GSLVVGYIAD → MRWTGTRAPL...TTLPAPPSSL

Show »
Length:430
Mass (Da):47,678
Checksum:iB5C5FA5A304430B4
GO

Sequence cautioni

The sequence AAH78883.1 differs from that shown. Reason: Erroneous initiation. Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 126126Missing in isoform 2. 2 PublicationsVSP_033591Add
BLAST
Alternative sequencei127 – 17246VYDTP…GYIAD → MRWTGTRAPLTVWTHCPAWL PTGVSCHWAPASMAGYTTLP APPSSL in isoform 2. 2 PublicationsVSP_033592Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78855 mRNA. Translation: CAA55411.1.
U76379 mRNA. Translation: AAB67702.1.
BC078883 mRNA. Translation: AAH78883.1. Different initiation.
PIRiS50862.
RefSeqiNP_036829.1. NM_012697.1. [Q63089-1]
UniGeneiRn.11186.

Genome annotation databases

EnsembliENSRNOT00000022068; ENSRNOP00000022068; ENSRNOG00000016337. [Q63089-2]
ENSRNOT00000022254; ENSRNOP00000022254; ENSRNOG00000016337. [Q63089-1]
GeneIDi24904.
KEGGirno:24904.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78855 mRNA. Translation: CAA55411.1.
U76379 mRNA. Translation: AAB67702.1.
BC078883 mRNA. Translation: AAH78883.1. Different initiation.
PIRiS50862.
RefSeqiNP_036829.1. NM_012697.1. [Q63089-1]
UniGeneiRn.11186.

3D structure databases

ProteinModelPortaliQ63089.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63089. 1 interaction.
MINTiMINT-8292690.
STRINGi10116.ENSRNOP00000022254.

Chemistry

BindingDBiQ63089.
ChEMBLiCHEMBL2073670.

Protein family/group databases

TCDBi2.A.1.19.1. the major facilitator superfamily (mfs).

PTM databases

iPTMnetiQ63089.
PhosphoSiteiQ63089.

Proteomic databases

PaxDbiQ63089.
PRIDEiQ63089.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000022068; ENSRNOP00000022068; ENSRNOG00000016337. [Q63089-2]
ENSRNOT00000022254; ENSRNOP00000022254; ENSRNOG00000016337. [Q63089-1]
GeneIDi24904.
KEGGirno:24904.

Organism-specific databases

CTDi6580.
RGDi3224. Slc22a1.

Phylogenomic databases

eggNOGiENOG410IRH7. Eukaryota.
ENOG410XR5P. LUCA.
GeneTreeiENSGT00760000118852.
HOGENOMiHOG000234568.
HOVERGENiHBG061545.
InParanoidiQ63089.
KOiK08198.
OMAiDLFQSCL.
OrthoDBiEOG78PV8N.
PhylomeDBiQ63089.

Enzyme and pathway databases

ReactomeiR-RNO-2161517. Abacavir transmembrane transport.
R-RNO-549127. Organic cation transport.

Miscellaneous databases

PROiQ63089.

Gene expression databases

GenevisibleiQ63089. RN.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR005828. MFS_sugar_transport_like.
IPR004749. Orgcat_transp/SVOP.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00898. 2A0119. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Drug excretion mediated by a new prototype of polyspecific transporter."
    Gruendemann D., Gorboulev V., Gambaryan S., Veyhl M., Koepsell H.
    Nature 372:549-552(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Cloning and functional characterization of a rat renal organic cation transporter isoform (rOCT1A)."
    Zhang L., Dresser M.J., Chun J.K., Babbitt P.C., Giacomini K.M.
    J. Biol. Chem. 272:16548-16554(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Kidney.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  4. "Electrogenic properties and substrate specificity of the polyspecific rat cation transporter rOCT1."
    Busch A.E., Quester S., Ulzheimer J.C., Waldegger S., Gorboulev V., Arndt P., Lang F., Koepsell H.
    J. Biol. Chem. 271:32599-32604(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  5. "Membrane localization of the electrogenic cation transporter rOCT1 in rat liver."
    Meyer-Wentrup F., Karbach U., Gorboulev V., Arndt P., Koepsell H.
    Biochem. Biophys. Res. Commun. 248:673-678(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Catecholamine transport by the organic cation transporter type 1 (OCT1)."
    Breidert T., Spitzenberger F., Gruendemann D., Schoemig E.
    Br. J. Pharmacol. 125:218-224(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Functional characteristics and membrane localization of rat multispecific organic cation transporters, OCT1 and OCT2, mediating tubular secretion of cationic drugs."
    Urakami Y., Okuda M., Masuda S., Saito H., Inui K.
    J. Pharmacol. Exp. Ther. 287:800-805(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  8. "Localization of organic cation transporters OCT1 and OCT2 in rat kidney."
    Karbach U., Kricke J., Meyer-Wentrup F., Gorboulev V., Volk C., Loffing-Cueni D., Kaissling B., Bachmann S., Koepsell H.
    Am. J. Physiol. 279:F679-F687(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  9. "Interaction of cations, anions, and weak base quinine with rat renal cation transporter rOCT2 compared with rOCT1."
    Arndt P., Volk C., Gorboulev V., Budiman T., Popp C., Ulzheimer-Teuber I., Akhoundova A., Koppatz S., Bamberg E., Nagel G., Koepsell H.
    Am. J. Physiol. 281:F454-F468(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Tissue distribution and renal developmental changes in rat organic cation transporter mRNA levels."
    Slitt A.L., Cherrington N.J., Hartley D.P., Leazer T.M., Klaassen C.D.
    Drug Metab. Dispos. 30:212-219(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  11. "Down-regulation of the organic cation transporter 1 of rat liver in obstructive cholestasis."
    Denk G.U., Soroka C.J., Mennone A., Koepsell H., Beuers U., Boyer J.L.
    Hepatology 39:1382-1389(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  12. "Purification and functional reconstitution of the rat organic cation transporter OCT1."
    Keller T., Elfeber M., Gorboulev V., Reilaender H., Koepsell H.
    Biochemistry 44:12253-12263(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Transport of the dopamine D2 agonist pramipexole by rat organic cation transporters OCT1 and OCT2 in kidney."
    Ishiguro N., Saito A., Yokoyama K., Morikawa M., Igarashi T., Tamai I.
    Drug Metab. Dispos. 33:495-499(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  14. "Metformin is a superior substrate for renal organic cation transporter OCT2 rather than hepatic OCT1."
    Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T., Inui K.
    Drug Metab. Pharmacokinet. 20:379-386(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  15. "Individual PKC-phosphorylation sites in organic cation transporter 1 determine substrate selectivity and transport regulation."
    Ciarimboli G., Koepsell H., Iordanova M., Gorboulev V., Durner B., Lang D., Edemir B., Schroter R., Van Le T., Schlatter E.
    J. Am. Soc. Nephrol. 16:1562-1570(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF SER-286; SER-292; THR-296; SER-328 AND THR-550, PHOSPHORYLATION.
  16. "Differential pharmacological in vitro properties of organic cation transporters and regional distribution in rat brain."
    Amphoux A., Vialou V., Drescher E., Bruess M., Mannoury La Cour C., Rochat C., Millan M.J., Giros B., Boenisch H., Gautron S.
    Neuropharmacology 50:941-952(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  17. "Identification of cysteines in rat organic cation transporters rOCT1 (C322, C451) and rOCT2 (C451) critical for transport activity and substrate affinity."
    Sturm A., Gorboulev V., Gorbunov D., Keller T., Volk C., Schmitt B.M., Schlachtbauer P., Ciarimboli G., Koepsell H.
    Am. J. Physiol. 293:F767-F779(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-26; CYS-155; CYS-179; CYS-322; CYS-358; CYS-418; CYS-437; CYS-451; CYS-470 AND CYS-474.
  18. "Effect of pregnane X receptor ligand on pharmacokinetics of substrates of organic cation transporter Oct1 in rats."
    Maeda T., Oyabu M., Yotsumoto T., Higashi R., Nagata K., Yamazoe Y., Tamai I.
    Drug Metab. Dispos. 35:1580-1586(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  19. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-334, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiS22A1_RAT
AccessioniPrimary (citable) accession number: Q63089
Secondary accession number(s): O35882, Q6AYW1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.