Solute carrier family 22 member 1 - Mus musculus (Mouse)

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O08966 (S22A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Solute carrier family 22 member 1

Alternative name(s):
Organic cation transporter 1
Short name=mOCT1

Gene names

Name:	Slc22a1
Synonyms:	Lx1, Oct1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	556 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Ion transport Transport
Cellular component	Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
PTM	Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	dopamine transport Inferred from electronic annotation. Source: Compara drug transmembrane transport Inferred from electronic annotation. Source: Compara epinephrine transport Inferred from electronic annotation. Source: Compara establishment or maintenance of transmembrane electrochemical gradient Inferred from electronic annotation. Source: Compara norepinephrine transport Inferred from electronic annotation. Source: Compara
Cellular_component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from sequence alignment Ref.3. Source: MGI
Molecular_function	acetylcholine transmembrane transporter activity Inferred from electronic annotation. Source: Compara dopamine transmembrane transporter activity Inferred from electronic annotation. Source: Compara norepinephrine transmembrane transporter activity Inferred from electronic annotation. Source: Compara organic cation transmembrane transporter activity Inferred from direct assay Ref.3. Source: MGI secondary active organic cation transmembrane transporter activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 556

556

Solute carrier family 22 member 1

PRO_0000333876

Regions

Topological domain

1 – 21

Cytoplasmic Potential

Transmembrane

22 – 42

Helical; Potential

Topological domain

43 – 150

108

Extracellular Potential

Transmembrane

151 – 171

Helical; Potential

Topological domain

172 – 177

Cytoplasmic Potential

Transmembrane

178 – 198

Helical; Potential

Topological domain

199 – 211

Extracellular Potential

Transmembrane

212 – 231

Helical; Potential

Topological domain

232 – 238

Cytoplasmic Potential

Transmembrane

239 – 259

Helical; Potential

Topological domain

260 – 263

Extracellular Potential

Transmembrane

264 – 284

Helical; Potential

Topological domain

285 – 348

Cytoplasmic Potential

Transmembrane

349 – 369

Helical; Potential

Topological domain

370 – 377

Extracellular Potential

Transmembrane

378 – 398

Helical; Potential

Topological domain

399 – 403

Cytoplasmic Potential

Transmembrane

404 – 424

Helical; Potential

Topological domain

425 – 429

Extracellular Potential

Transmembrane

430 – 452

Helical; Potential

Topological domain

453 – 465

Cytoplasmic Potential

Transmembrane

466 – 486

Helical; Potential

Topological domain

487 – 493

Extracellular Potential

Transmembrane

494 – 514

Helical; Potential

Topological domain

515 – 556

Cytoplasmic Potential

Sites

Site

451

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

Amino acid modifications

Glycosylation

N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict

C → Y in AAB19097. Ref.1

Sequence conflict

144

G → V in AAB19097. Ref.1

Sequence conflict

506

S → T in AAB19097. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O08966 [UniParc].

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

FASTA

556

61,521

        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' referencesShow '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.
IPI	IPI00331032.
RefSeq	NP_033228.2. NM_009202.5.
UniGene	Mm.594.
3D structure databases
ProteinModelPortal	O08966.
SMR	O08966. Positions 158-306.
ModBase	Search...
Protein-protein interaction databases
STRING	10090.ENSMUSP00000024596.
Proteomic databases
PaxDb	O08966.
PRIDE	O08966.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000024596; ENSMUSP00000024596; ENSMUSG00000023829.
GeneID	20517.
KEGG	mmu:20517.
UCSC	uc008akx.1. mouse.
Organism-specific databases
CTD	6580.
MGI	MGI:108111. Slc22a1.
Phylogenomic databases
eggNOG	COG0477.
GeneTree	ENSGT00700000104151.
HOGENOM	HOG000234568.
HOVERGEN	HBG061545.
InParanoid	O08966.
KO	K08198.
OMA	TIYLQVQ.
OrthoDB	EOG4S4PG6.
Gene expression databases
Bgee	O08966.
Genevestigator	O08966.
Family and domain databases
InterPro	IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR004749. Orgcat_transp. IPR005828. Sub_transporter. IPR005829. Sugar_transporter_CS. [Graphical view]
Pfam	PF00083. Sugar_tr. 1 hit. [Graphical view]
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR00898. 2A0119. 1 hit.
PROSITE	PS50850. MFS. 1 hit. PS00216. SUGAR_TRANSPORT_1. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	298731.
SOURCE	Search...

Entry information

Entry name

S22A1_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents