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Solute carrier family 22 member 2 (Organic cation transporter 2)

 S22A2_RABIT             Reviewed;         554 AA.
Q8MJI6;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-OCT-2002, sequence version 1.
25-OCT-2017, entry version 87.
RecName: Full=Solute carrier family 22 member 2;
AltName: Full=Organic cation transporter 2;
Name=SLC22A2; Synonyms=OCT2;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=12060594;
Zhang X., Evans K.K., Wright S.H.;
"Molecular cloning of rabbit organic cation transporter rbOCT2 and
functional comparisons with rbOCT1.";
Am. J. Physiol. 283:F124-F133(2002).
[2]
MUTAGENESIS OF ASN-71; ASN-96 AND ASN-112, GLYCOSYLATION, AND
SUBCELLULAR LOCATION.
PubMed=16368738; DOI=10.1152/ajprenal.00462.2005;
Pelis R.M., Suhre W.M., Wright S.H.;
"Functional influence of N-glycosylation in OCT2-mediated
tetraethylammonium transport.";
Am. J. Physiol. 290:F1118-F1126(2006).
-!- FUNCTION: Mediates tubular uptake of organic compounds from
circulation. Mediates the influx of agmatine, dopamine,
noradrenaline (norepinephrine), serotonin, choline, famotidine,
ranitidine, histamin, creatinine, amantadine, memantine,
acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP,
amiloride, metformin, N-1-methylnicotinamide (NMN), 1-methyl-4-
phenylpyridinium (MPP), cisplatin and oxaliplatin. Cisplatin may
develop a nephrotoxic action. Transport of creatinine is inhibited
by fluoroquinolones such as DX-619 and LVFX. This transporter is a
major determinant of the anticancer activity of oxaliplatin and
may contribute to antitumor specificity (By similarity). Mediates
tubular uptake of tetraethylammonium (TEA) and cimetidine.
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in kidney.
{ECO:0000269|PubMed:12060594}.
-!- INDUCTION: May be down-regulated in diabetic patients.
-!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
superfamily. Organic cation transporter (TC 2.A.1.19) family.
{ECO:0000305}.
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EMBL; AF458095; AAM83256.1; -; mRNA.
RefSeq; NP_001075584.1; NM_001082115.1.
UniGene; Ocu.2669; -.
ProteinModelPortal; Q8MJI6; -.
STRING; 9986.ENSOCUP00000002196; -.
GeneID; 100008831; -.
KEGG; ocu:100008831; -.
CTD; 6582; -.
eggNOG; ENOG410IRIE; Eukaryota.
eggNOG; ENOG410XSRI; LUCA.
HOGENOM; HOG000234568; -.
HOVERGEN; HBG061545; -.
InParanoid; Q8MJI6; -.
KO; K08199; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
CDD; cd06174; MFS; 1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR004749; Orgcat_transp/SVOP.
InterPro; IPR005829; Sugar_transporter_CS.
Pfam; PF00083; Sugar_tr; 1.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00898; 2A0119; 1.
PROSITE; PS50850; MFS; 1.
PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
1: Evidence at protein level;
Complete proteome; Glycoprotein; Ion transport; Membrane;
Reference proteome; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 554 Solute carrier family 22 member 2.
/FTId=PRO_0000320961.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 149 Extracellular. {ECO:0000255}.
TRANSMEM 150 170 Helical. {ECO:0000255}.
TOPO_DOM 171 176 Cytoplasmic. {ECO:0000255}.
TRANSMEM 177 197 Helical. {ECO:0000255}.
TOPO_DOM 198 209 Extracellular. {ECO:0000255}.
TRANSMEM 210 230 Helical. {ECO:0000255}.
TOPO_DOM 231 237 Cytoplasmic. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TOPO_DOM 259 262 Extracellular. {ECO:0000255}.
TRANSMEM 263 283 Helical. {ECO:0000255}.
TOPO_DOM 284 348 Cytoplasmic. {ECO:0000255}.
TRANSMEM 349 369 Helical. {ECO:0000255}.
TOPO_DOM 370 374 Extracellular. {ECO:0000255}.
TRANSMEM 375 395 Helical. {ECO:0000255}.
TOPO_DOM 396 403 Cytoplasmic. {ECO:0000255}.
TRANSMEM 404 424 Helical. {ECO:0000255}.
TOPO_DOM 425 427 Extracellular. {ECO:0000255}.
TRANSMEM 428 450 Helical. {ECO:0000255}.
TOPO_DOM 451 463 Cytoplasmic. {ECO:0000255}.
TRANSMEM 464 484 Helical. {ECO:0000255}.
TOPO_DOM 485 493 Extracellular. {ECO:0000255}.
TRANSMEM 494 514 Helical. {ECO:0000255}.
TOPO_DOM 515 554 Cytoplasmic. {ECO:0000255}.
SITE 450 450 Involved in recognition of organic
cations and participates in structural
changes that occur during translocation
of organic cations. {ECO:0000250}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 71 71 N->Q: Higher affinity for TEA. Loss of
plasma membrane localization; when
associated with Q-76. Loss of plasma
membrane localization; when associated
with Q-112. Loss of plasma membrane
localization; when associated with Q-76
and Q-112. {ECO:0000269|PubMed:16368738}.
MUTAGEN 96 96 N->Q: Higher affinity for TEA and lower
Vmax. {ECO:0000269|PubMed:16368738}.
MUTAGEN 112 112 N->Q: Higher affinity for TEA, lower Vmax
and loss of plasma membrane localization.
{ECO:0000269|PubMed:16368738}.
SEQUENCE 554 AA; 61576 MW; CFBD4525D6D1ABD4 CRC64;
MPTVDDILEQ VGHFHFFQKQ TFFLLALISA AFTPIYVGIV FLGFTPDHRC RSPGVAELSQ
RCGWSPGEEL NYTVPGLGAA DGAFARQCMR YEVDWNQSSP GCVDPLASLA PNRSHLPLGP
CQHGWVYDTP GSSIVTEFNL VCARSWMLDL FQSAVNIGFF IGSVGIGYLA DRFGRKLCLL
VTILINAAAG VLMAVSPNYT WMLIFRLIQG LVSKAGWLIG YILITEFVGL NYRRTVGILY
QVAFTVGLLV LAGVAYALPR WRWLQLTVTL PYFCFLLYYW CIPESPRWLI SQNKNAKAMR
IMEHIAKKNG KSLPVSLQSL RAAEDVGEKL NPSFLDLVRT PQIRKHTCIL MYNWFTSSVL
YQGLIMHLGL AGGDIYLDFF YSALVEFPAA FLIIATIDRV GRRYPWAVSN MVAGAACLAS
VFVPDDLQGL RITVACLGRM GITMAYEMVC LVNAELYPTF IRNLGVLVCS SLCDVGGIVT
PFLVYRLTAI WLQLPLVVFA VVGLVAGGLV LMLPETKGRT LPETIEEAEN LQRPRKNREK
VIYVHVRKAD GPLT


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