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Database: UniProt/SWISS-PROT
Entry: S22A2_PIG
LinkDB: S22A2_PIG
Original site: S22A2_PIG 
ID   S22A2_PIG               Reviewed;         554 AA.
AC   O02713;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   01-OCT-2014, entry version 88.
DE   RecName: Full=Solute carrier family 22 member 2;
DE   AltName: Full=Apical organic cation transporter;
DE   AltName: Full=Organic cation transporter 2;
GN   Name=SLC22A2; Synonyms=OCT2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
OC   Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=9099681; DOI=10.1074/jbc.272.16.10408;
RA   Grundemann D., Babin-Ebell J., Martel F., Ording N., Schmidt A.,
RA   Schoemig E.;
RT   "Primary structure and functional expression of the apical organic
RT   cation transporter from kidney epithelial LLC-PK1 cells.";
RL   J. Biol. Chem. 272:10408-10413(1997).
CC   -!- FUNCTION: Mediates tubular uptake of organic compounds from
CC       circulation. Mediates the influx of agmatine, dopamine,
CC       noradrenaline (norepinephrine), serotonin, choline, famotidine,
CC       ranitidine, histamin, creatinine, amantadine, memantine,
CC       acriflavine, 4-[4-(dimethylamino)-styryl]-N-methylpyridinium ASP,
CC       amiloride, metformin, N-1-methylnicotinamide (NMN),
CC       tetraethylammonium (TEA), 1-methyl-4-phenylpyridinium (MPP),
CC       cimetidine, cisplatin and oxaliplatin. Cisplatin may develop a
CC       nephrotoxic action. Transport of creatinine is inhibited by
CC       fluoroquinolones such as DX-619 and LVFX. This transporter is a
CC       major determinant of the anticancer activity of oxaliplatin and
CC       may contribute to antitumor specificity (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
CC       superfamily. Organic cation transporter (TC 2.A.1.19) family.
CC       {ECO:0000305}.
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DR   EMBL; Y09400; CAA70567.1; -; mRNA.
DR   RefSeq; NP_999067.1; NM_213902.1.
DR   UniGene; Ssc.14537; -.
DR   ProteinModelPortal; O02713; -.
DR   STRING; 9823.ENSSSCP00000004366; -.
DR   TCDB; 2.A.1.19.5; the major facilitator superfamily (mfs).
DR   GeneID; 396936; -.
DR   KEGG; ssc:396936; -.
DR   CTD; 6582; -.
DR   eggNOG; COG0477; -.
DR   HOGENOM; HOG000234568; -.
DR   HOVERGEN; HBG061545; -.
DR   KO; K08199; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015075; F:ion transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR016196; MFS_dom_general_subst_transpt.
DR   InterPro; IPR004749; Orgcat_transp.
DR   InterPro; IPR005828; Sub_transporter.
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   2: Evidence at transcript level;
KW   Complete proteome; Glycoprotein; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    554       Solute carrier family 22 member 2.
FT                                /FTId=PRO_0000320959.
FT   TOPO_DOM      1     21       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     22     42       Helical. {ECO:0000255}.
FT   TOPO_DOM     43    149       Extracellular. {ECO:0000255}.
FT   TRANSMEM    150    170       Helical. {ECO:0000255}.
FT   TOPO_DOM    171    176       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    177    197       Helical. {ECO:0000255}.
FT   TOPO_DOM    198    209       Extracellular. {ECO:0000255}.
FT   TRANSMEM    210    230       Helical. {ECO:0000255}.
FT   TOPO_DOM    231    237       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    238    258       Helical. {ECO:0000255}.
FT   TOPO_DOM    259    262       Extracellular. {ECO:0000255}.
FT   TRANSMEM    263    283       Helical. {ECO:0000255}.
FT   TOPO_DOM    284    347       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    348    368       Helical. {ECO:0000255}.
FT   TOPO_DOM    369    376       Extracellular. {ECO:0000255}.
FT   TRANSMEM    377    397       Helical. {ECO:0000255}.
FT   TOPO_DOM    398    403       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    404    424       Helical. {ECO:0000255}.
FT   TOPO_DOM    425    431       Extracellular. {ECO:0000255}.
FT   TRANSMEM    432    452       Helical. {ECO:0000255}.
FT   TOPO_DOM    453    463       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    464    484       Helical. {ECO:0000255}.
FT   TOPO_DOM    485    493       Extracellular. {ECO:0000255}.
FT   TRANSMEM    494    514       Helical. {ECO:0000255}.
FT   TOPO_DOM    515    554       Cytoplasmic. {ECO:0000255}.
FT   SITE        450    450       Involved in recognition of organic
FT                                cations and participates in structural
FT                                changes that occur during translocation
FT                                of organic cations. {ECO:0000250}.
FT   CARBOHYD     71     71       N-linked (GlcNAc...). {ECO:0000255}.
SQ   SEQUENCE   554 AA;  61990 MW;  E14B5565600C553B CRC64;
     MLTVDDILEH TGEFNFFQKQ TFFLLALLSA AFTPIYVGIV FLGFIPDHRC RSPGVAELSQ
     RCGWSLAEEL NYTVPGPGPA GQAFPRQCRR YEVDWNQSTL GCVDPLAGLA ANSSHLPLGP
     CRYGWVYDTP GSSIVTEFDL VCANSWLLDL FQSAVNVGFF IGSVGIGYIA DRFGRKLCLL
     LTILINAVSG VLMAISPTYT WMLVFRLIQG LVSKAGWMIG YILITEFVGL SYRRTVGIFY
     QVAFTFGLLV LAGVAYALPH WRWLQFTVTL PNFCFLFYYW CVPESPRWLI SQNKNAKAMS
     IIKHIAKKNG KSLPASLQSL RPDEEVGEKL KPSFLDLVRT PQIRKHTLIL MYNWFTSAVL
     YQGLVMHMGL AGSNLYLDFF YSALVEFPAA LLILLTIDRL GRRHPWAASN VVAGAACLAS
     VFIPEDPHWL RITVLCLGRM GITMAYEMVC LVNAELYPTF IRNLGVLVCS SMCDIGGIIT
     PFLVYRLTDI WHELPLVVFA VVGLIAGGLV LLLPETKGKT LPETIEEAET MRRPRKNKEK
     IIYLQVKKLD IPPN
//
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