TCDB is operated by the Saier Lab Bioinformatics Group
« See all members of the family


2.A.1.19.30
Solute carrier family 22 member 2 (Organic cation transporter 2) (hOCT2).  Oct2 is a low affinity high efficiency choline transporter, enriched in synaptic vesicles of cholinergic neurons (Nakata et al. 2013).  May also transport peptides and peptide derivatives (Volková et al. 2015). It also transports L-carnitine (Adeva-Andany et al. 2017). OCT2 is a multispecific transporter with cholesterol-dependent allosteric features. The role of cholesterol recognition/interaction amino acid consensus sequences (CRAC and CARC) in the allosteric binding to 1-methyl-4-phenylpyridinium (MPP+) has been reported (Sutter et al. 2021). Comparisons of the inhibitory potential of elacridar and imazalil on metformin uptake with that on MPP uptake revealed substrate-dependent differences in hOCT2 and mOct2 for both inhibitors (Kuehne et al. 2022).

Accession Number:O15244
Protein Name:Solute carrier family 22 member 2
Length:555
Molecular Weight:62581.00
Species:Homo sapiens (Human) [9606]
Number of TMSs:12
Location1 / Topology2 / Orientation3: Membrane1 / Multi-pass membrane protein2
Substrate

Cross database links:

Entrez Gene ID: 6582   
Pfam: PF00083   
KEGG: hsa:6582   

Gene Ontology

GO:0005887 C:integral to plasma membrane
GO:0005624 C:membrane fraction
GO:0015101 F:organic cation transmembrane transporter activity
GO:0007589 P:body fluid secretion
GO:0042136 P:neurotransmitter biosynthetic process
GO:0007269 P:neurotransmitter secretion

References (23)

[1] “Cloning and characterization of two human polyspecific organic cation transporters.”  Gorboulev V.et.al.   9260930
[2] “cDNA cloning, functional characterization, and tissue distribution of an alternatively spliced variant of organic cation transporter hOCT2 predominantly expressed in the human kidney.”  Urakami Y.et.al.   12089365
[3] “Complete sequencing and characterization of 21,243 full-length human cDNAs.”  Ota T.et.al.   14702039
[4] “The DNA sequence and analysis of human chromosome 6.”  Mungall A.J.et.al.   14574404
[5] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[6] “Gene structures of the human non-neuronal monoamine transporters EMT and OCT2.”  Gruendemann D.et.al.   10942111
[7] “Human neurons express the polyspecific cation transporter hOCT2, which translocates monoamine neurotransmitters, amantadine, and memantine.”  Busch A.E.et.al.   9687576
[8] “Distinct characteristics of organic cation transporters, OCT1 and OCT2, in the basolateral membrane of renal tubules.”  Urakami Y.et.al.   11758759
[9] “Gene expression levels and immunolocalization of organic ion transporters in the human kidney.”  Motohashi H.et.al.   11912245
[10] “Agmatine is efficiently transported by non-neuronal monoamine transporters extraneuronal monoamine transporter (EMT) and organic cation transporter 2 (OCT2).”  Grundemann D.et.al.   12538837
[11] “Different transport properties between famotidine and cimetidine by human renal organic ion transporters (SLC22A).”  Motohashi H.et.al.   15496291
[12] “Cisplatin nephrotoxicity is critically mediated via the human organic cation transporter 2.”  Ciarimboli G.et.al.   16314463
[13] “Metformin is a superior substrate for renal organic cation transporter OCT2 rather than hepatic OCT1.”  Kimura N.et.al.   16272756
[14] “A species difference in the transport activities of H2 receptor antagonists by rat and human renal organic anion and cation transporters.”  Tahara H.et.al.   16006492
[15] “Metformin transport by renal basolateral organic cation transporter hOCT2.”  Kimura N.et.al.   15783073
[16] “Characterization of regulatory mechanisms and states of human organic cation transporter 2.”  Biermann J.et.al.   16394027
[17] “Organic cation transporters are determinants of oxaliplatin cytotoxicity.”  Zhang S.et.al.   16951202
[18] “Interactions of fluoroquinolone antibacterials, DX-619 and levofloxacin, with creatinine transport by renal organic cation transporter hOCT2.”  Okuda M.et.al.   17072098
[19] “Cisplatin and oxaliplatin, but not carboplatin and nedaplatin, are substrates for human organic cation transporters (SLC22A1-3 and multidrug and toxin extrusion family).”  Yonezawa A.et.al.   16914559
[20] “Differential contribution of organic cation transporters, OCT2 and MATE1, in platinum agent-induced nephrotoxicity.”  Yokoo S.et.al.   17582384
[21] “The organic cation transporters (OCT1, OCT2, EMT) and the plasma membrane monoamine transporter (PMAT) show differential distribution and cyclic expression pattern in human endometrium and early pregnancy decidua.”  Bottalico B.et.al.   17393420
[22] “Polymorphisms in a human kidney xenobiotic transporter, OCT2, exhibit altered function.”  Leabman M.K.et.al.   12142729
[23] “Human organic cation transporter (OCT1 and OCT2) gene polymorphisms and therapeutic effects of metformin.”  Shikata E.et.al.   17111267

External Searches:

Analyze:

Predict TMSs (Predict number of transmembrane segments)
Window Size: Angle:  
FASTA formatted sequence
1:	MPTTVDDVLE HGGEFHFFQK QMFFLLALLS ATFAPIYVGI VFLGFTPDHR CRSPGVAELS 
61:	LRCGWSPAEE LNYTVPGPGP AGEASPRQCR RYEVDWNQST FDCVDPLASL DTNRSRLPLG 
121:	PCRDGWVYET PGSSIVTEFN LVCANSWMLD LFQSSVNVGF FIGSMSIGYI ADRFGRKLCL 
181:	LTTVLINAAA GVLMAISPTY TWMLIFRLIQ GLVSKAGWLI GYILITEFVG RRYRRTVGIF 
241:	YQVAYTVGLL VLAGVAYALP HWRWLQFTVS LPNFFFLLYY WCIPESPRWL ISQNKNAEAM 
301:	RIIKHIAKKN GKSLPASLQR LRLEEETGKK LNPSFLDLVR TPQIRKHTMI LMYNWFTSSV 
361:	LYQGLIMHMG LAGDNIYLDF FYSALVEFPA AFMIILTIDR IGRRYPWAAS NMVAGAACLA 
421:	SVFIPGDLQW LKIIISCLGR MGITMAYEIV CLVNAELYPT FIRNLGVHIC SSMCDIGGII 
481:	TPFLVYRLTN IWLELPLMVF GVLGLVAGGL VLLLPETKGK ALPETIEEAE NMQRPRKNKE 
541:	KMIYLQVQKL DIPLN