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 03-AUG-2022, entry version 120.
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; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; 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 cation
RT 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, 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), tetraethylammonium (TEA), 1-methyl-4-
CC phenylpyridinium (MPP), cimetidine, cisplatin and oxaliplatin.
CC Cisplatin may develop a nephrotoxic action. Transport of creatinine is
CC inhibited by fluoroquinolones such as DX-619 and LVFX. This transporter
CC is a major determinant of the anticancer activity of oxaliplatin and
CC may contribute to antitumor specificity (By similarity). {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) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR EMBL; Y09400; CAA70567.1; -; mRNA.
DR RefSeq; NP_999067.1; NM_213902.1.
DR AlphaFoldDB; O02713; -.
DR SMR; O02713; -.
DR STRING; 9823.ENSSSCP00000004366; -.
DR TCDB; 2.A.1.19.5; the major facilitator superfamily (mfs).
DR PaxDb; O02713; -.
DR Ensembl; ENSSSCT00035082011; ENSSSCP00035033991; ENSSSCG00035061058.
DR Ensembl; ENSSSCT00040020681; ENSSSCP00040008685; ENSSSCG00040015330.
DR Ensembl; ENSSSCT00045028737; ENSSSCP00045019883; ENSSSCG00045016889.
DR Ensembl; ENSSSCT00055022315; ENSSSCP00055017684; ENSSSCG00055011340.
DR Ensembl; ENSSSCT00065065075; ENSSSCP00065028203; ENSSSCG00065047562.
DR Ensembl; ENSSSCT00070054098; ENSSSCP00070045864; ENSSSCG00070026975.
DR GeneID; 396936; -.
DR KEGG; ssc:396936; -.
DR CTD; 6582; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; O02713; -.
DR OrthoDB; 326501at2759; -.
DR ChiTaRS; SLC22A2; pig.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Chromosome 1.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015075; F:ion transmembrane transporter activity; 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 2: Evidence at transcript 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_0000320959"
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..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..376
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..403
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..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"
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
