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Solute carrier family 22 member 2 (Organic cation transporter 2) (rOCT2)

 S22A2_RAT               Reviewed;         555 AA.
Q9R0W2; P70485; P97558;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
22-NOV-2017, entry version 115.
RecName: Full=Solute carrier family 22 member 2;
AltName: Full=Organic cation transporter 2;
Short=rOCT2;
Name=Slc22a2; Synonyms=Oct2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=8702418; DOI=10.1006/bbrc.1996.1056;
Okuda M., Saito H., Urakami Y., Takano M., Inui K.;
"cDNA cloning and functional expression of a novel rat kidney organic
cation transporter, OCT2.";
Biochem. Biophys. Res. Commun. 224:500-507(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney cortex;
PubMed=9260930; DOI=10.1089/dna.1997.16.871;
Gorboulev V., Ulzheimer J.C., Akhoundova A., Ulzheimer-Teuber I.,
Karbach U., Quester S., Baumann C., Lang F., Busch A.E., Koepsell H.;
"Cloning and characterization of two human polyspecific organic cation
transporters.";
DNA Cell Biol. 16:871-881(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=10385678;
Gruendemann D., Liebich G., Kiefer N., Koster S., Schoemig E.;
"Selective substrates for non-neuronal monoamine transporters.";
Mol. Pharmacol. 56:1-10(1999).
[4]
BIOPHYSICAL PROPERTIES.
PubMed=9812985; DOI=10.1074/jbc.273.47.30915;
Grundemann D., Koster S., Kiefer N., Breidert T., Engelhardt M.,
Spitzenberger F., Obermuller N., Schomig E.;
"Transport of monoamine transmitters by the organic cation transporter
type 2, OCT2.";
J. Biol. Chem. 273:30915-30920(1998).
[5]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=10812069; DOI=10.1016/S0014-5793(00)01525-8;
Urakami Y., Okuda M., Saito H., Inui K.;
"Hormonal regulation of organic cation transporter OCT2 expression in
rat kidney.";
FEBS Lett. 473:173-176(2000).
[6]
TISSUE SPECIFICITY.
PubMed=11083459;
Sugawara-Yokoo M., Urakami Y., Koyama H., Fujikura K., Masuda S.,
Saito H., Naruse T., Inui K., Takata K.;
"Differential localization of organic cation transporters rOCT1 and
rOCT2 in the basolateral membrane of rat kidney proximal tubules.";
Histochem. Cell Biol. 114:175-180(2000).
[7]
FUNCTION.
PubMed=16242669; DOI=10.1016/j.bcp.2005.09.020;
Yonezawa A., Masuda S., Nishihara K., Yano I., Katsura T., Inui K.;
"Association between tubular toxicity of cisplatin and expression of
organic cation transporter rOCT2 (Slc22a2) in the rat.";
Biochem. Pharmacol. 70:1823-1831(2005).
[8]
FUNCTION, TISSUE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16272756; DOI=10.2133/dmpk.20.379;
Kimura N., Masuda S., Tanihara Y., Ueo H., Okuda M., Katsura T.,
Inui K.;
"Metformin is a superior substrate for renal organic cation
transporter OCT2 rather than hepatic OCT1.";
Drug Metab. Pharmacokinet. 20:379-386(2005).
[9]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=16006492; DOI=10.1124/jpet.105.088104;
Tahara H., Kusuhara H., Endou H., Koepsell H., Imaoka T., Fuse E.,
Sugiyama Y.;
"A species difference in the transport activities of H2 receptor
antagonists by rat and human renal organic anion and cation
transporters.";
J. Pharmacol. Exp. Ther. 315:337-345(2005).
[10]
MUTAGENESIS OF CYS-451.
PubMed=17567940; DOI=10.1152/ajprenal.00106.2007;
Sturm A., Gorboulev V., Gorbunov D., Keller T., Volk C., Schmitt B.M.,
Schlachtbauer P., Ciarimboli G., Koepsell H.;
"Identification of cysteines in rat organic cation transporters rOCT1
(C322, C451) and rOCT2 (C451) critical for transport activity and
substrate affinity.";
Am. J. Physiol. 293:F767-F779(2007).
[11]
FUNCTION.
PubMed=17582384; DOI=10.1016/j.bcp.2007.03.004;
Yokoo S., Yonezawa A., Masuda S., Fukatsu A., Katsura T., Inui K.;
"Differential contribution of organic cation transporters, OCT2 and
MATE1, in platinum agent-induced nephrotoxicity.";
Biochem. Pharmacol. 74:477-487(2007).
[12]
FUNCTION, AND INDUCTION BY ISCHEMIA.
PubMed=18180268; DOI=10.1124/dmd.107.019869;
Matsuzaki T., Morisaki T., Sugimoto W., Yokoo K., Sato D.,
Nonoguchi H., Tomita K., Terada T., Inui K., Hamada A., Saito H.;
"Altered pharmacokinetics of cationic drugs caused by down-regulation
of renal rat organic cation transporter 2 (slc22a2) and rat multidrug
and toxin extrusion 1 (slc47a1) in ischemia/reperfusion-induced acute
kidney injury.";
Drug Metab. Dispos. 36:649-654(2008).
-!- FUNCTION: Mediates tubular uptake of organic compounds from
circulation. Mediates the influx of agmatine, serotonin, choline,
ranitidine, histamin, creatinine, amantadine, memantine,
acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP
and amiloride (By similarity). Mediates the influx of adrenaline,
noradrenaline (norepinephrine), dopamine, cimetidine, famotidine,
metformin, N-1-methylnicotinamide (NMN), 1-methyl-4-
phenylpyridinium (MPP), tetraethylammonium (TEA), oxaliplatin and
cisplatin. 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. {ECO:0000250, ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16242669, ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:17582384, ECO:0000269|PubMed:18180268,
ECO:0000269|PubMed:8702418}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=68.8 uM for cimetidine (at pH 7.4 and 37 degrees Celsius)
{ECO:0000269|PubMed:16006492, ECO:0000269|PubMed:16272756};
KM=60.6 uM for famotidine {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
KM=0.63 mM for metformin {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
KM=4.4 mM for noradrenaline {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
KM=1.3 mM for histamine {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
KM=1.9 mM for dopamine {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
KM=3.6 mM for serotonin {ECO:0000269|PubMed:16006492,
ECO:0000269|PubMed:16272756};
Vmax=1490 pmol/min/mg enzyme for cimetidine uptake
{ECO:0000269|PubMed:16006492, ECO:0000269|PubMed:16272756};
Vmax=117 pmol/min/mg enzyme for famotidine uptake
{ECO:0000269|PubMed:16006492, ECO:0000269|PubMed:16272756};
Vmax=1.446 nmol/min/mg enzyme for metformin uptake
{ECO:0000269|PubMed:16006492, ECO:0000269|PubMed:16272756};
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
protein {ECO:0000305}.
-!- TISSUE SPECIFICITY: Expressed in the kidney; in the proximal
tubule of the outer medulla. Expression is greater in the kidney
of male than of female. {ECO:0000269|PubMed:10812069,
ECO:0000269|PubMed:11083459, ECO:0000269|PubMed:16272756,
ECO:0000269|PubMed:8702418}.
-!- INDUCTION: Down-regulated in ischemia/reperfusion (I/R) kidneys.
Up-regulated by testosterone and moderately down-regulated by
estradiol. {ECO:0000269|PubMed:10812069,
ECO:0000269|PubMed:18180268}.
-!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
superfamily. Organic cation transporter (TC 2.A.1.19) family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA11754.1; Type=Frameshift; Positions=539; Evidence={ECO:0000305};
Sequence=CAA66979.1; Type=Frameshift; Positions=539; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; D83044; BAA11754.1; ALT_FRAME; mRNA.
EMBL; X98334; CAA66979.1; ALT_FRAME; mRNA.
EMBL; Y13154; CAB52215.1; -; mRNA.
PIR; JC4884; JC4884.
RefSeq; NP_113772.1; NM_031584.2.
UniGene; Rn.10555; -.
ProteinModelPortal; Q9R0W2; -.
STRING; 10116.ENSRNOP00000023116; -.
BindingDB; Q9R0W2; -.
ChEMBL; CHEMBL1770032; -.
TCDB; 2.A.1.19.19; the major facilitator superfamily (mfs).
iPTMnet; Q9R0W2; -.
PhosphoSitePlus; Q9R0W2; -.
PaxDb; Q9R0W2; -.
PRIDE; Q9R0W2; -.
GeneID; 29503; -.
KEGG; rno:29503; -.
CTD; 6582; -.
RGD; 61936; Slc22a2.
eggNOG; KOG0255; Eukaryota.
eggNOG; COG0477; LUCA.
HOGENOM; HOG000234568; -.
HOVERGEN; HBG061545; -.
InParanoid; Q9R0W2; -.
KO; K08199; -.
PhylomeDB; Q9R0W2; -.
TreeFam; TF315847; -.
PRO; PR:Q9R0W2; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
GO; GO:0005277; F:acetylcholine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015220; F:choline transmembrane transporter activity; IDA:RGD.
GO; GO:0005329; F:dopamine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0005333; F:norepinephrine transmembrane transporter activity; IBA:GO_Central.
GO; GO:0008514; F:organic anion transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:RGD.
GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:RGD.
GO; GO:0008513; F:secondary active organic cation transmembrane transporter activity; IBA:GO_Central.
GO; GO:0005496; F:steroid binding; IDA:RGD.
GO; GO:0006812; P:cation transport; ISO:RGD.
GO; GO:0015872; P:dopamine transport; IBA:GO_Central.
GO; GO:0051608; P:histamine transport; IDA:RGD.
GO; GO:0006836; P:neurotransmitter transport; IBA:GO_Central.
GO; GO:0015874; P:norepinephrine transport; IBA:GO_Central.
GO; GO:0015695; P:organic cation transport; IDA:RGD.
GO; GO:0015697; P:quaternary ammonium group transport; IDA:RGD.
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 1 555 Solute carrier family 22 member 2.
/FTId=PRO_0000320962.
TOPO_DOM 1 21 Cytoplasmic. {ECO:0000255}.
TRANSMEM 22 42 Helical. {ECO:0000255}.
TOPO_DOM 43 150 Extracellular. {ECO:0000255}.
TRANSMEM 151 171 Helical. {ECO:0000255}.
TOPO_DOM 172 177 Cytoplasmic. {ECO:0000255}.
TRANSMEM 178 198 Helical. {ECO:0000255}.
TOPO_DOM 199 210 Extracellular. {ECO:0000255}.
TRANSMEM 211 231 Helical. {ECO:0000255}.
TOPO_DOM 232 238 Cytoplasmic. {ECO:0000255}.
TRANSMEM 239 259 Helical. {ECO:0000255}.
TOPO_DOM 260 263 Extracellular. {ECO:0000255}.
TRANSMEM 264 284 Helical. {ECO:0000255}.
TOPO_DOM 285 348 Cytoplasmic. {ECO:0000255}.
TRANSMEM 349 369 Helical. {ECO:0000255}.
TOPO_DOM 370 375 Extracellular. {ECO:0000255}.
TRANSMEM 376 396 Helical. {ECO:0000255}.
TOPO_DOM 397 404 Cytoplasmic. {ECO:0000255}.
TRANSMEM 405 425 Helical. {ECO:0000255}.
TOPO_DOM 426 432 Extracellular. {ECO:0000255}.
TRANSMEM 433 453 Helical. {ECO:0000255}.
TOPO_DOM 454 464 Cytoplasmic. {ECO:0000255}.
TRANSMEM 465 485 Helical. {ECO:0000255}.
TOPO_DOM 486 494 Extracellular. {ECO:0000255}.
TRANSMEM 495 515 Helical. {ECO:0000255}.
TOPO_DOM 516 555 Cytoplasmic. {ECO:0000255}.
SITE 451 451 Involved in recognition of organic
cations and participates in structural
changes that occur during translocation
of organic cations.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 451 451 C->M: Transport activity strongly
reduced. {ECO:0000269|PubMed:17567940}.
CONFLICT 332 332 N -> K (in Ref. 1; BAA11754).
{ECO:0000305}.
CONFLICT 335 335 F -> I (in Ref. 1; BAA11754).
{ECO:0000305}.
SEQUENCE 555 AA; 62343 MW; 29521969AE1AC206 CRC64;
MSTVDDILEH IGEFHLFQKQ TFFLLALLSG AFTPIYVGIV FLGFTPDHHC WSPGAAKLSQ
RCGWSQAEEL NYTVPGLGPS DEASFLSQCM RYEVDWNQST LDCVDPLSSL AADRNQLPLG
PCEHGWVYNT PGSSIVTEFN LVCAHSWMLD LFQSVVNVGF FIGAMMIGYL ADRFGRKFCL
LVTILINAIS GALMAISPNY AWMLVFRFLQ GLVSKAGWLI GYILITEFVG LGYRRMVGIC
YQIAFTVGLL ILAGVAYVIP NWRWLQFAVT LPNFCFLLYF WCIPESPRWL ISQNKIVKAM
KIIKHIAKKN GKSVPVSLQN LTPDEDAGKK LNPSFLDLVR TPQIRKHTLI LMYNWFTSSV
LYQGLIMHMG LAGDNIYLDF FYSALVEFPA AFIIILTIDR VGRRYPWAVS NMVAGAACLA
SVFIPDDLQW LKITIACLGR MGITMAYEMV CLVNAELYPT YIRNLGVLVC SSMCDIGGII
TPFLVYRLTD IWMEFPLVVF AVVGLVAGAL VLLLPETKGK ALPETIEDAE NMQRPRKKKE
KRIYLQVKQA DRPLS


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