S22A2_RABIT
ID S22A2_RABIT Reviewed; 554 AA.
AC Q8MJI6;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Solute carrier family 22 member 2;
DE AltName: Full=Organic cation transporter 2;
GN Name=SLC22A2; Synonyms=OCT2;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12060594; DOI=10.1152/ajprenal.00367.2001;
RA Zhang X., Evans K.K., Wright S.H.;
RT "Molecular cloning of rabbit organic cation transporter rbOCT2 and
RT functional comparisons with rbOCT1.";
RL Am. J. Physiol. 283:F124-F133(2002).
RN [2]
RP MUTAGENESIS OF ASN-71; ASN-96 AND ASN-112, GLYCOSYLATION, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16368738; DOI=10.1152/ajprenal.00462.2005;
RA Pelis R.M., Suhre W.M., Wright S.H.;
RT "Functional influence of N-glycosylation in OCT2-mediated
RT tetraethylammonium transport.";
RL Am. J. Physiol. 290:F1118-F1126(2006).
CC -!- FUNCTION: Mediates tubular uptake of organic compounds from
CC circulation. Mediates the influx of agmatine, dopamine, noradrenaline
CC (norepinephrine), serotonin, choline, famotidine, ranitidine,
CC histamine, creatinine, amantadine, memantine, acriflavine, 4-[4-
CC (dimethylamino)-styryl]-N-methylpyridinium ASP, amiloride, metformin,
CC N-1-methylnicotinamide (NMN), 1-methyl-4-phenylpyridinium (MPP),
CC cisplatin and oxaliplatin. Cisplatin may develop a nephrotoxic action.
CC Transport of creatinine is inhibited by fluoroquinolones such as DX-619
CC and LVFX. This transporter is a major determinant of the anticancer
CC activity of oxaliplatin and may contribute to antitumor specificity (By
CC similarity). Mediates tubular uptake of tetraethylammonium (TEA) and
CC cimetidine. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in kidney. {ECO:0000269|PubMed:12060594}.
CC -!- INDUCTION: May be down-regulated in diabetic patients.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF458095; AAM83256.1; -; mRNA.
DR RefSeq; NP_001075584.1; NM_001082115.1.
DR AlphaFoldDB; Q8MJI6; -.
DR SMR; Q8MJI6; -.
DR STRING; 9986.ENSOCUP00000002196; -.
DR GeneID; 100008831; -.
DR KEGG; ocu:100008831; -.
DR CTD; 6582; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q8MJI6; -.
DR OrthoDB; 326501at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IEA:UniProt.
DR GO; GO:0071705; P:nitrogen compound transport; IEA:UniProt.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004749; Orgcat_transp/SVOP.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00898; 2A0119; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 2.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Solute carrier family 22 member 2"
FT /id="PRO_0000320961"
FT TOPO_DOM 1..21
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 22..42
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 43..149
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 171..176
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..209
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 210..230
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 231..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 428..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..463
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..493
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 494..514
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 515..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 450
FT /note="Involved in recognition of organic cations and
FT participates in structural changes that occur during
FT translocation of organic cations"
FT /evidence="ECO:0000250"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 71
FT /note="N->Q: Higher affinity for TEA. Loss of plasma
FT membrane localization; when associated with Q-76. Loss of
FT plasma membrane localization; when associated with Q-112.
FT Loss of plasma membrane localization; when associated with
FT Q-76 and Q-112."
FT /evidence="ECO:0000269|PubMed:16368738"
FT MUTAGEN 96
FT /note="N->Q: Higher affinity for TEA and lower Vmax."
FT /evidence="ECO:0000269|PubMed:16368738"
FT MUTAGEN 112
FT /note="N->Q: Higher affinity for TEA, lower Vmax and loss
FT of plasma membrane localization."
FT /evidence="ECO:0000269|PubMed:16368738"
SQ 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
