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O08966 (S22A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 22 member 1
Alternative name(s):
Organic cation transporter 1
Short name=mOCT1
Gene names
Name:Slc22a1
Synonyms:Lx1, Oct1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length556 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.2 Ref.3

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein.

Tissue specificity

Highly expressed in liver, kidney and intestine. Weakly expressed in adrenals and in lacting mammary glands. Ref.1 Ref.7

Developmental stage

Weakly expressed 2 days before birth, but gradually increased during the first 3 weeks of age, reaching a plateau around day 22 in both kidney and liver. At 45 days of age, renal and hepatic levels is 4 to 6 times higher than the level immediately after birth. Ref.7

Induction

Increased by PPARA and PPARG treatment in both liver and H35 cells. Ref.6

Post-translational modification

Phosphorylated By similarity.

Sequence similarities

Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcation transport

Inferred from direct assay Ref.3. Source: MGI

dopamine transport

Inferred from electronic annotation. Source: Ensembl

drug transmembrane transport

Inferred from electronic annotation. Source: Ensembl

epinephrine transport

Inferred from electronic annotation. Source: Ensembl

establishment or maintenance of transmembrane electrochemical gradient

Inferred from electronic annotation. Source: Ensembl

norepinephrine transport

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasolateral plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence alignment Ref.3. Source: MGI

   Molecular_functionacetylcholine transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

dopamine transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

norepinephrine transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

organic cation transmembrane transporter activity

Inferred from direct assay Ref.3. Source: MGI

quaternary ammonium group transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

secondary active organic cation transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556Solute carrier family 22 member 1
PRO_0000333876

Regions

Topological domain1 – 2121Cytoplasmic Potential
Transmembrane22 – 4221Helical; Potential
Topological domain43 – 150108Extracellular Potential
Transmembrane151 – 17121Helical; Potential
Topological domain172 – 1776Cytoplasmic Potential
Transmembrane178 – 19821Helical; Potential
Topological domain199 – 21113Extracellular Potential
Transmembrane212 – 23120Helical; Potential
Topological domain232 – 2387Cytoplasmic Potential
Transmembrane239 – 25921Helical; Potential
Topological domain260 – 2634Extracellular Potential
Transmembrane264 – 28421Helical; Potential
Topological domain285 – 34864Cytoplasmic Potential
Transmembrane349 – 36921Helical; Potential
Topological domain370 – 3778Extracellular Potential
Transmembrane378 – 39821Helical; Potential
Topological domain399 – 4035Cytoplasmic Potential
Transmembrane404 – 42421Helical; Potential
Topological domain425 – 4295Extracellular Potential
Transmembrane430 – 45223Helical; Potential
Topological domain453 – 46513Cytoplasmic Potential
Transmembrane466 – 48621Helical; Potential
Topological domain487 – 4937Extracellular Potential
Transmembrane494 – 51421Helical; Potential
Topological domain515 – 55642Cytoplasmic Potential

Sites

Site4511Involved in affinity and selectivity of cations as well as in translocation By similarity

Amino acid modifications

Glycosylation711N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict261C → Y in AAB19097. Ref.1
Sequence conflict1441G → V in AAB19097. Ref.1
Sequence conflict5061S → T in AAB19097. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O08966 [UniParc].

Last modified May 20, 2008. Version 2.
Checksum: 0230EF5A2B1E2723

FASTA55661,521
        10         20         30         40         50         60 
MPTVDDVLEH VGEFGWFQKQ AFLLLCLISA SLAPIYVGIV FLGFTPDHHC RSPGVAELSQ 

        70         80         90        100        110        120 
RCGWSPAEEL NYTVPGLGSA GEASFLSQCM KYEVDWNQST LDCVDPLSSL AANRSHLPLS 

       130        140        150        160        170        180 
PCEHGWVYDT PGSSIVTEFN LVCGDAWKVD LFQSCVNLGF FLGSLVVGYI ADRFGRKLCL 

       190        200        210        220        230        240 
LVTTLVTSLS GVLTAVAPDY TSMLLFRLLQ GMVSKGSWVS GYTLITEFVG SGYRRTTAIL 

       250        260        270        280        290        300 
YQVAFTVGLV GLAGVAYAIP DWRWLQLAVS LPTFLFLLYY WFVPESPRWL LSQKRTTQAV 

       310        320        330        340        350        360 
RIMEQIAQKN RKVPPADLKM MCLEEDASER RSPSFADLFR TPSLRKHTLI LMYLWFSCAV 

       370        380        390        400        410        420 
LYQGLIMHVG ATGANLYLDF FYSSLVEFPA AFIILVTIDR IGRIYPIAAS NLVAGAACLL 

       430        440        450        460        470        480 
MIFIPHELHW LNVTLACLGR MGATIVLQMV CLVNAELYPT FIRNLGMMVC SALCDLGGIF 

       490        500        510        520        530        540 
TPFMVFRLME VWQALPLILF GVLGLSAGAV TLLLPETKGV ALPETIEEAE NLGRRKSKAK 

       550 
ENTIYLQVQT GKSPHT 

« Hide

References

« Hide 'large scale' references
[1]"The Lx1 gene maps to mouse chromosome 17 and codes for a protein that is homologous to glucose and polyspecific transmembrane transporters."
Schweifer N., Barlow D.P.
Mamm. Genome 7:735-740(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: C57BL/6.
Tissue: Liver.
[2]"Cloning and functional expression of a mouse liver organic cation transporter."
Green R.M., Lo K., Sterritt C., Beier D.R.
Hepatology 29:1556-1562(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: C57BL/6 X CBA.
[3]"Functional characterization of mouse cation transporter mOCT2 compared with mOCT1."
Kakehi M., Koyabu N., Nakamura T., Uchiumi T., Kuwano M., Ohtani H., Sawada Y.
Biochem. Biophys. Res. Commun. 296:644-650(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
Strain: ddY.
Tissue: Kidney.
[4]"Genomic sequence analysis in the mouse T-complex region."
Brathwaite M., Waeltz P., Qian Y., Dudekula D., Schlessinger D., Nagaraja R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129S6/SvEvTac.
[5]"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].
Strain: FVB/N.
Tissue: Liver.
[6]"Transcriptional regulation of murine Slc22a1 (Oct1) by peroxisome proliferator agonist receptor-alpha and -gamma."
Nie W., Sweetser S., Rinella M., Green R.M.
Am. J. Physiol. 288:G207-G212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Tissue distribution and ontogeny of organic cation transporters in mice."
Alnouti Y., Petrick J.S., Klaassen C.D.
Drug Metab. Dispos. 34:477-482(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38652 mRNA. Translation: AAB19097.1.
AF010259 mRNA. Translation: AAC98884.1.
AF481054 Genomic DNA. Translation: AAM22157.1.
BC021651 mRNA. Translation: AAH21651.1.
RefSeqNP_033228.2. NM_009202.5.
UniGeneMm.594.

3D structure databases

ProteinModelPortalO08966.
SMRO08966. Positions 153-519.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000024596.

Chemistry

ChEMBLCHEMBL2073664.

Proteomic databases

PaxDbO08966.
PRIDEO08966.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024596; ENSMUSP00000024596; ENSMUSG00000023829.
GeneID20517.
KEGGmmu:20517.
UCSCuc008akx.1. mouse.

Organism-specific databases

CTD6580.
MGIMGI:108111. Slc22a1.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00730000110561.
HOGENOMHOG000234568.
HOVERGENHBG061545.
InParanoidO08966.
KOK08198.
OMAVCADSWK.
OrthoDBEOG78PV8N.
PhylomeDBO08966.
TreeFamTF315847.

Gene expression databases

BgeeO08966.
GenevestigatorO08966.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005828. Sub_transporter.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 1 hit.
TIGRFAMsTIGR00898. 2A0119. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio298731.
PROO08966.
SOURCESearch...

Entry information

Entry nameS22A1_MOUSE
AccessionPrimary (citable) accession number: O08966
Secondary accession number(s): Q9R1Q4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot