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O75751 (S22A3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 22 member 3
Alternative name(s):
Extraneuronal monoamine transporter
Short name=EMT
Organic cation transporter 3
Gene names
Name:SLC22A3
Synonyms:EMTH, OCT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

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

General annotation (Comments)

Function

Mediates potential-dependent transport of a variety of organic cations. May play a significant role in the disposition of cationic neurotoxins and neurotransmitters in the brain. Ref.1 Ref.6

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in placenta, skeletal muscle, prostate, aorta, liver, fetal lung, salivary gland, adrenal gland, kidney and brain cortex. No expression detected in spleen. Ref.1 Ref.5 Ref.6

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 componentMembrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdopamine transport

Inferred from electronic annotation. Source: Ensembl

drug transmembrane transport

Traceable author statement. Source: Reactome

histamine uptake

Inferred from electronic annotation. Source: Ensembl

organic cation transport

Inferred from direct assay Ref.6PubMed 16024787. Source: MGI

quaternary ammonium group transport

Inferred from direct assay Ref.6. Source: MGI

regulation of appetite

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of plasma membrane

Traceable author statement Ref.5. Source: ProtInc

membrane

Traceable author statement Ref.5. Source: ProtInc

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functiondopamine transmembrane transporter activity

Inferred from electronic annotation. Source: Ensembl

organic cation transmembrane transporter activity

Inferred from direct assay Ref.6PubMed 16024787. Source: MGI

quaternary ammonium group transmembrane transporter activity

Inferred from direct assay Ref.6. Source: MGI

toxin transporter activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ABL1P005192EBI-1752674,EBI-375543

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 556556Solute carrier family 22 member 3
PRO_0000220503

Regions

Transmembrane21 – 4121Helical; Potential
Transmembrane182 – 20221Helical; Potential
Transmembrane241 – 26121Helical; Potential
Transmembrane269 – 28921Helical; Potential
Transmembrane381 – 40121Helical; Potential
Transmembrane468 – 48821Helical; Potential
Transmembrane498 – 51821Helical; Potential

Amino acid modifications

Glycosylation721N-linked (GlcNAc...) Potential
Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential

Natural variations

Natural variant441T → M.
Corresponds to variant rs8187715 [ dbSNP | Ensembl ].
VAR_020351
Natural variant1161A → S.
Corresponds to variant rs8187717 [ dbSNP | Ensembl ].
VAR_020352

Sequences

Sequence LengthMass (Da)Tools
O75751 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: C3CA2D77DD21C658

FASTA55661,280
        10         20         30         40         50         60 
MPSFDEALQR VGEFGRFQRR VFLLLCLTGV TFAFLFVGVV FLGTQPDHYW CRGPSAAALA 

        70         80         90        100        110        120 
ERCGWSPEEE WNRTAPASRG PEPPERRGRC QRYLLEAAND SASATSALSC ADPLAAFPNR 

       130        140        150        160        170        180 
SAPLVPCRGG WRYAQAHSTI VSEFDLVCVN AWMLDLTQAI LNLGFLTGAF TLGYAADRYG 

       190        200        210        220        230        240 
RIVIYLLSCL GVGVTGVVVA FAPNFPVFVI FRFLQGVFGK GTWMTCYVIV TEIVGSKQRR 

       250        260        270        280        290        300 
IVGIVIQMFF TLGIIILPGI AYFIPNWQGI QLAITLPSFL FLLYYWVVPE SPRWLITRKK 

       310        320        330        340        350        360 
GDKALQILRR IAKCNGKYLS SNYSEITVTD EEVSNPSFLD LVRTPQMRKC TLILMFAWFT 

       370        380        390        400        410        420 
SAVVYQGLVM RLGIIGGNLY IDFFISGVVE LPGALLILLT IERLGRRLPF AASNIVAGVA 

       430        440        450        460        470        480 
CLVTAFLPEG IAWLRTTVAT LGRLGITMAF EIVYLVNSEL YPTTLRNFGV SLCSGLCDFG 

       490        500        510        520        530        540 
GIIAPFLLFR LAAVWLELPL IIFGILASIC GGLVMLLPET KGIALPETVD DVEKLGSPHS 

       550 
CKCGRNKKTP VSRSHL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular identification of the corticosterone-sensitive extraneuronal catecholamine transporter."
Gruendemann D., Schechinger B., Rappold G.A., Schoemig E.
Nat. Neurosci. 1:349-351(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Tongue.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Cloning of the mouse and human solute carrier 22a3 (Slc22a3/SLC22A3) identifies a conserved cluster of three organic cation transporters on mouse chromosome 17 and human 6q26-q27."
Verhaagh S., Schweifer N., Barlow D.P., Zwart R.
Genomics 55:209-218(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 513-556, TISSUE SPECIFICITY.
[6]"Structure, function, and regional distribution of the organic cation transporter OCT3 in the kidney."
Wu X., Huang W., Ganapathy M.E., Wang H., Kekuda R., Conway S.J., Leibach F.H., Ganapathy V.
Am. J. Physiol. 279:F449-F458(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
Tissue: Kidney.
[7]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ001417 mRNA. Translation: CAA04751.1.
AK314590 mRNA. Translation: BAG37164.1.
AL591069, AL355506 Genomic DNA. Translation: CAI16539.1.
AL355506, AL591069 Genomic DNA. Translation: CAI20340.1.
CH471051 Genomic DNA. Translation: EAW47599.1.
AF078749 mRNA. Translation: AAD20977.1.
RefSeqNP_068812.1. NM_021977.3.
UniGeneHs.567337.

3D structure databases

ProteinModelPortalO75751.
SMRO75751. Positions 163-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActO75751. 2 interactions.
STRING9606.ENSP00000275300.

Chemistry

ChEMBLCHEMBL2073673.

Protein family/group databases

TCDB2.A.1.19.24. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteO75751.

Proteomic databases

PaxDbO75751.
PRIDEO75751.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000275300; ENSP00000275300; ENSG00000146477.
GeneID6581.
KEGGhsa:6581.
UCSCuc003qti.4. human.

Organism-specific databases

CTD6581.
GeneCardsGC06P160739.
HGNCHGNC:10967. SLC22A3.
HPAHPA029750.
MIM604842. gene.
neXtProtNX_O75751.
PharmGKBPA330.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0477.
HOGENOMHOG000234568.
HOVERGENHBG061545.
KOK08200.
OrthoDBEOG78PV8N.
PhylomeDBO75751.
TreeFamTF315847.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressO75751.
BgeeO75751.
CleanExHS_SLC22A3.
GenevestigatorO75751.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00898. 2A0119. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLC22A3. human.
GeneWikiSLC22A3.
GenomeRNAi6581.
NextBio25609.
PROO75751.
SOURCESearch...

Entry information

Entry nameS22A3_HUMAN
AccessionPrimary (citable) accession number: O75751
Secondary accession number(s): Q5SYN6, Q9UP02
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1998
Last modified: April 16, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM