S22A1_RABIT
ID S22A1_RABIT Reviewed; 554 AA.
AC O77504;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Solute carrier family 22 member 1;
DE AltName: Full=Organic cation transporter 1;
DE AltName: Full=rbOCT1;
GN Name=SLC22A1; Synonyms=OCT1;
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], TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
RC STRAIN=New Zealand;
RX PubMed=9528667; DOI=10.1016/s0005-2736(97)00207-1;
RA Terashita S., Dresser M.J., Zhang L., Gray A.T., Yost S.C., Giacomini K.M.;
RT "Molecular cloning and functional expression of a rabbit renal organic
RT cation transporter.";
RL Biochim. Biophys. Acta 1369:1-6(1998).
RN [2]
RP FUNCTION.
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).
CC -!- FUNCTION: Translocates a broad array of organic cations with various
CC structures and molecular weights including the model compounds 1-
CC methyl-4-phenylpyridinium (MPP), tetraethylammonium (TEA), N-1-
CC methylnicotinamide (NMN), 4-(4-(dimethylamino)styryl)-N-
CC methylpyridinium (ASP), the endogenous compounds choline, guanidine,
CC histamine, epinephrine, adrenaline, noradrenaline and dopamine, and the
CC drugs quinine, and metformin. The transport of organic cations is
CC inhibited by a broad array of compounds like tetramethylammonium (TMA),
CC cocaine, lidocaine, NMDA receptor antagonists, atropine, prazosin,
CC cimetidine, TEA and NMN, guanidine, cimetidine, choline, procainamide,
CC quinine, tetrabutylammonium, and tetrapentylammonium. Translocates
CC organic cations in an electrogenic and pH-independent manner.
CC Translocates organic cations across the plasma membrane in both
CC directions. Transports the polyamines spermine and spermidine.
CC Transports pramipexole across the basolateral membrane of the proximal
CC tubular epithelial cells. The choline transport is activated by MMTS.
CC Regulated by various intracellular signaling pathways including
CC inhibition by protein kinase A activation, and endogenously activation
CC by the calmodulin complex, the calmodulin-dependent kinase II and LCK
CC tyrosine kinase. {ECO:0000269|PubMed:12060594,
CC ECO:0000269|PubMed:9528667}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=23 uM for MPP {ECO:0000269|PubMed:9528667};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein.
CC -!- TISSUE SPECIFICITY: Expressed in kidney, liver, and intestine.
CC {ECO:0000269|PubMed:9528667}.
CC -!- PTM: Phosphorylated. {ECO:0000250}.
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; AF015958; AAC23661.1; -; mRNA.
DR RefSeq; NP_001075491.1; NM_001082022.1.
DR AlphaFoldDB; O77504; -.
DR SMR; O77504; -.
DR STRING; 9986.ENSOCUP00000002189; -.
DR GeneID; 100008659; -.
DR KEGG; ocu:100008659; -.
DR CTD; 6580; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; O77504; -.
DR OrthoDB; 704438at2759; -.
DR TreeFam; TF315847; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
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; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Solute carrier family 22 member 1"
FT /id="PRO_0000333878"
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..206
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..229
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 230..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..374
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 375..395
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 396..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..431
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..464
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..492
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 450
FT /note="Involved in affinity and selectivity of cations as
FT well as in translocation"
FT /evidence="ECO:0000250"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08966"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 554 AA; 61288 MW; BE20D4E724D3C2A7 CRC64;
MPTVDDVLEQ VGEFGWFQKR TFLFLCLISA ILAPIYLGIV FLGFTPDHRC RSPGVDELSQ
RCGWSPEEEL NYTVPGLGAT DGAFVRQCMR YEVDWNQSSL GCVDPLASLA PNRSHLPLGP
CQHGWVYDTP GSSIVTEFNL VCADAWKVDL FQSCVNLGFF LGSLGVGYIA DRFGRKLCLL
LTTLINAVSG VLTAVAPDYT SMLLFRLLQG LVSKGSWMSG YTLITEFVGS GYRRTVAILY
QVAFSVGLVA LSGVAYAIPN WRWLQLTVSL PTFLCLFYYW CVPESPRWLL SQKRNTDAVK
IMDNIAQKNG KLPPADLKML SLDEDVTEKL SPSLADLFRT PNLRKHTFIL MFLWFTCSVL
YQGLILHMGA TGGNVYLDFF YSSLVEFPAA FVILVTIDRV GRIYPMAASN LAAGVASVIL
IFVPQDLHWL TIVLSCVGRM GATIVLQMIC LVNAELYPTF VRNLGVMVCS ALCDVGGIIT
PFMVFRLMEV WQPLPLIVFG VLGLLAGGMT LLLPETKGVA LPETIEDAEN LRRKAKPKES
KIYLQVQTSE LKGP
