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Q9Z0E8 (S22A5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. 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 5
Alternative name(s):
High-affinity sodium-dependent carnitine cotransporter
Organic cation/carnitine transporter 2
Gene names
Name:Slc22a5
Synonyms:Octn2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length557 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Sodium-ion dependent, high affinity carnitine transporter. Involved in the active cellular uptake of carnitine. Transports one sodium ion with one molecule of carnitine. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Also relative uptake activity ratio of carnitine to TEA is 11.3.

Subunit structure

Interacts with PDZK1. Ref.6

Subcellular location

Apical cell membrane; Multi-pass membrane protein. Note: Colocalizes with PDZK1 on apical membranes of kidney proximal tubules. Ref.6

Tissue specificity

Widely expressed. Expressed in kidney, liver and testis. Ref.5

Involvement in disease

Defects in Slc22a5 are the cause of the juvenile visceral steatosis (JVS) phenotype. JVS is an autosomal recessive animal model of systemic carnitine deficiency. Ref.2

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
Sodium transport
Symport
Transport
   Cellular componentCell membrane
Membrane
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
Sodium
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadult heart development

Inferred from mutant phenotype PubMed 9140816. Source: MGI

carnitine metabolic process

Inferred from mutant phenotype PubMed 15240869PubMed 17027329PubMed 1996978PubMed 7914432PubMed 8325377. Source: MGI

carnitine transmembrane transport

Inferred from direct assay Ref.5. Source: GOC

carnitine transport

Inferred from direct assay Ref.5. Source: MGI

locomotory behavior

Inferred from mutant phenotype PubMed 17027329. Source: MGI

mitochondrion organization

Inferred from mutant phenotype PubMed 7773507. Source: MGI

quaternary ammonium group transport

Inferred from direct assay Ref.5. Source: MGI

reproductive structure development

Inferred from mutant phenotype PubMed 10100867. Source: MGI

sodium ion transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentapical plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

brush border membrane

Inferred from direct assay Ref.6. Source: BHF-UCL

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

membrane

Inferred by curator Ref.5. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

carnitine transmembrane transporter activity

Inferred from direct assay Ref.5. Source: MGI

quaternary ammonium group transmembrane transporter activity

Inferred from direct assay Ref.5. Source: MGI

symporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 557557Solute carrier family 22 member 5
PRO_0000220501

Regions

Topological domain1 – 2020Cytoplasmic Potential
Transmembrane21 – 4121Helical; Name=1; Potential
Topological domain42 – 142101Extracellular Potential
Transmembrane143 – 16321Helical; Name=2; Potential
Topological domain164 – 1729Cytoplasmic Potential
Transmembrane173 – 19321Helical; Name=3; Potential
Topological domain194 – 1974Extracellular Potential
Transmembrane198 – 21821Helical; Name=4; Potential
Topological domain219 – 23214Cytoplasmic Potential
Transmembrane233 – 25321Helical; Name=5; Potential
Topological domain254 – 2574Extracellular Potential
Transmembrane258 – 27821Helical; Name=6; Potential
Topological domain279 – 34163Cytoplasmic Potential
Transmembrane342 – 36221Helical; Name=7; Potential
Topological domain363 – 37311Extracellular Potential
Transmembrane374 – 39421Helical; Name=8; Potential
Topological domain395 – 40612Cytoplasmic Potential
Transmembrane407 – 42721Helical; Name=9; Potential
Topological domain428 – 4303Extracellular Potential
Transmembrane431 – 45121Helical; Name=10; Potential
Topological domain452 – 46211Cytoplasmic Potential
Transmembrane463 – 48321Helical; Name=11; Potential
Topological domain484 – 4885Extracellular Potential
Transmembrane489 – 50921Helical; Name=12; Potential
Topological domain510 – 55748Cytoplasmic Potential
Nucleotide binding218 – 2258ATP Potential

Amino acid modifications

Modified residue4861Phosphotyrosine By similarity
Modified residue5501Phosphothreonine Ref.7
Glycosylation571N-linked (GlcNAc...) Potential
Glycosylation641N-linked (GlcNAc...) Potential
Glycosylation911N-linked (GlcNAc...) Potential

Natural variations

Natural variant3521L → R in JVS. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9Z0E8 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6093F0EE9612B204

FASTA55762,780
        10         20         30         40         50         60 
MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFNGMSIV FLAGTPEHRC LVPHTVNLSS 

        70         80         90        100        110        120 
AWRNHSIPLE TKDGRQVPQK CRRYRLATIA NFSELGLEPG RDVDLEQLEQ ESCLDGWEYD 

       130        140        150        160        170        180 
KDVFLSTIVT EWDLVCKDDW KAPLTTSLFF VGVLMGSFIS GQLSDRFGRK NVLFLTMGMQ 

       190        200        210        220        230        240 
TGFSFLQVFS VNFEMFTVLF VLVGMGQISN YVAAFVLGTE ILSKSIRIIF ATLGVCIFYA 

       250        260        270        280        290        300 
FGFMVLPLFA YFIRDWRMLL LALTVPGVLC GALWWFIPES PRWLISQGRI KEAEVIIRKA 

       310        320        330        340        350        360 
AKINGIVAPS TIFDPSELQD LNSTKPQLHH IYDLIRTRNI RVITIMSIIL WLTISVGYFG 

       370        380        390        400        410        420 
LSLDTPNLHG DIYVNCFLLA AVEVPAYVLA WLLLQYLPRR YSISAALFLG GSVLLFMQLV 

       430        440        450        460        470        480 
PSELFYLSTA LVMVGKFGIT SAYSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF 

       490        500        510        520        530        540 
VYLGAYDRFL PYILMGSLTI LTAILTLFFP ESFGVPLPDT IDQMLRVKGI KQWQIQSQTR 

       550 
MQKDGEESPT VLKSTAF 

« Hide

References

« Hide 'large scale' references
[1]"Primary systemic carnitine deficiency is caused by mutations in a gene encoding sodium ion-dependent carnitine transporter."
Nezu J., Tamai I., Oku A., Ohashi R., Yabuuchi H., Hashimoto N., Nikaido H., Sai Y., Koizumi A., Shoji Y., Takada G., Matsuishi T., Yashino M., Kato H., Ohura T., Tsujimoto G., Hayakawa J., Shimane M., Tsuji A.
Nat. Genet. 21:91-94(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6J.
Tissue: Kidney.
[2]"A missense mutation of mouse OCTN2, a sodium-dependent carnitine cotransporter, in the juvenile visceral steatosis mouse."
Lu K., Nishimori H., Nakamura Y., Shima K., Kuwajima M.
Biochem. Biophys. Res. Commun. 252:590-594(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT JVS ARG-352.
Strain: C3H.
[3]"Functional characteristics and tissue distribution pattern of organic cation transporter 2 (OCTN2), an organic cation/carnitine transporter."
Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H., Chen J., Conway S.J., Ganapathy V.
J. Pharmacol. Exp. Ther. 290:1482-1492(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION.
[4]"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: Colon.
[5]"Molecular and functional characterization of organic cation/carnitine transporter family in mice."
Tamai I., Ohashi R., Nezu J., Sai Y., Kobayashi D., Oku A., Shimane M., Tsuji A.
J. Biol. Chem. 275:40064-40072(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[6]"PDZK1 directly regulates the function of organic cation/carnitine transporter OCTN2."
Kato Y., Sai Y., Yoshida K., Watanabe C., Hirata T., Tsuji A.
Mol. Pharmacol. 67:734-743(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PDZK1.
[7]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB015800 mRNA. Translation: BAA36590.1.
AF111425 mRNA. Translation: AAC99787.1.
AF110417 mRNA. Translation: AAD54060.1.
BC031118 mRNA. Translation: AAH31118.1.
RefSeqNP_035526.1. NM_011396.3.
UniGeneMm.42253.

3D structure databases

ProteinModelPortalQ9Z0E8.
SMRQ9Z0E8. Positions 144-514.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000019044.

Chemistry

ChEMBLCHEMBL2073665.

PTM databases

PhosphoSiteQ9Z0E8.

Proteomic databases

PaxDbQ9Z0E8.
PRIDEQ9Z0E8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000019044; ENSMUSP00000019044; ENSMUSG00000018900.
GeneID20520.
KEGGmmu:20520.
UCSCuc007ixc.2. mouse.

Organism-specific databases

CTD6584.
MGIMGI:1329012. Slc22a5.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00750000117473.
HOGENOMHOG000234570.
HOVERGENHBG061545.
InParanoidQ9Z0E8.
KOK08202.
OMAGMKHRKT.
OrthoDBEOG7C8GH9.
PhylomeDBQ9Z0E8.
TreeFamTF315847.

Gene expression databases

ArrayExpressQ9Z0E8.
BgeeQ9Z0E8.
GenevestigatorQ9Z0E8.

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

NextBio298743.
PROQ9Z0E8.
SOURCESearch...

Entry information

Entry nameS22A5_MOUSE
AccessionPrimary (citable) accession number: Q9Z0E8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 111 of the entry and version 1 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