S22A2_PONAB
ID S22A2_PONAB Reviewed; 555 AA.
AC Q5R5H7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Solute carrier family 22 member 2;
DE AltName: Full=Organic cation transporter 2;
GN Name=SLC22A2; Synonyms=OCT2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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; CR860882; CAH92989.1; -; mRNA.
DR RefSeq; NP_001126767.1; NM_001133295.1.
DR AlphaFoldDB; Q5R5H7; -.
DR SMR; Q5R5H7; -.
DR STRING; 9601.ENSPPYP00000019208; -.
DR GeneID; 100173770; -.
DR KEGG; pon:100173770; -.
DR CTD; 6582; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q5R5H7; -.
DR OrthoDB; 326501at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0098590; C:plasma membrane region; IEA:UniProt.
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..555
FT /note="Solute carrier family 22 member 2"
FT /id="PRO_0000320960"
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..150
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..177
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..210
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 232..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 260..263
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..348
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 349..369
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 370..375
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 397..404
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..432
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 433..453
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 454..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..494
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..555
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 72
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 62424 MW; E0ED91B92445957B CRC64;
MPTTVDDVLE HGGEFHFFQK QMFFLLALLS ATFTPIYVGI VFLGFTPDHR CRSPGVAELS
LRCGWSPAEE LNYTVPGPGP AGEASPRQCG RYEVDWNQSA FGCVDPLASL DTNRSRLPLG
PCREGWVYET PGSSIVTEFN LVCANSWMLD LFQASVNVGF FFGSVSIGYI ADRFGRKLCL
LTTVLINAAA GVLMAISPTY TWMLIFRLIQ GLVSKAGWLI GYILITEFVG RRYRRTVGIF
YQVAYTVGLL VLAGVAYALP HWRWLQFTVT LPNFFFLLYY WCIPESPRWL ISQNKNAEAM
RIIKHIAKKN GKSLPASLQC LRLEEETGEK LNPSFLDLVR TPQIRKHTMI LMYNWFTSSV
LYQGLIMHMG LAGDNIYLDF FYSALVEFPA AFMIIVTIDR IGRRYPWAAS NMVAGAACLA
SVFIPGDLQW LKIIISCLGR MGITMAYEIV RLVNAELYPT FIRNLGVHIC SSMCDIGGII
TPFLVYRLTN IWLELPLMVF GVLGLVAGGL VLLLPETKGK ALPETIEEAE NMQRPRKNKE
KMIYLQVQKL DIPLN
