S22A1_BOVIN
ID S22A1_BOVIN Reviewed; 563 AA.
AC A7MBE0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Solute carrier family 22 member 1;
DE AltName: Full=Organic cation transporter 1;
GN Name=SLC22A1; Synonyms=OCT1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Kidney;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane; Multi-pass membrane
CC protein.
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; BC151505; AAI51506.1; -; mRNA.
DR RefSeq; NP_001094568.1; NM_001101098.2.
DR AlphaFoldDB; A7MBE0; -.
DR SMR; A7MBE0; -.
DR STRING; 9913.ENSBTAP00000004059; -.
DR BindingDB; A7MBE0; -.
DR PaxDb; A7MBE0; -.
DR PRIDE; A7MBE0; -.
DR Ensembl; ENSBTAT00000004059; ENSBTAP00000004059; ENSBTAG00000008540.
DR GeneID; 519461; -.
DR KEGG; bta:519461; -.
DR CTD; 6580; -.
DR VEuPathDB; HostDB:ENSBTAG00000008540; -.
DR VGNC; VGNC:34719; SLC22A1.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000162065; -.
DR HOGENOM; CLU_001265_33_5_1; -.
DR InParanoid; A7MBE0; -.
DR OMA; YLWFSCA; -.
DR OrthoDB; 704438at2759; -.
DR TreeFam; TF315847; -.
DR Reactome; R-BTA-112311; Neurotransmitter clearance.
DR Reactome; R-BTA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-BTA-2161517; Abacavir transmembrane transport.
DR Reactome; R-BTA-442660; Na+/Cl- dependent neurotransmitter transporters.
DR Reactome; R-BTA-549127; Organic cation transport.
DR Proteomes; UP000009136; Chromosome 9.
DR Bgee; ENSBTAG00000008540; Expressed in cortex of kidney and 30 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
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:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0008504; F:monoamine transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015214; F:pyrimidine nucleoside transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0019534; F:toxin transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0090494; P:dopamine uptake; IEA:Ensembl.
DR GO; GO:0015874; P:norepinephrine transport; IEA:Ensembl.
DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
DR GO; GO:0051610; P:serotonin uptake; IEA:Ensembl.
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 Cell membrane; Glycoprotein; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..563
FT /note="Solute carrier family 22 member 1"
FT /id="PRO_0000333874"
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..144
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 145..165
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..196
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..342
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..371
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 372..392
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 393..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..423
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..459
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 460..480
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 481..487
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 488..508
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 509..563
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 445
FT /note="Involved in affinity and selectivity of cations as
FT well as in translocation"
FT /evidence="ECO:0000250"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08966"
FT CARBOHYD 71
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 563 AA; 62502 MW; 36AAF99750A912F3 CRC64;
MLTVDDVLEQ VGEFGWFQKQ TFLILCLLSA AFAPIYVGIV FLAFTPDHRC RSPGVAELSR
RCGWSLAEEL NYTVPGPGPE SQCLRYEVDW NQSTLGCLDP LASLATNGSP LPLGPCEQGW
VYDTPGSSIV TEFNLVCDDS WKVDLFQSCV NLGFFLGSLG VGYIADRFGR KVCLLATTLT
CASLGVLTAV APDYTSLLIF RLLQGLVSKG SWTAGYTLIT EFVGLGYRRT VAILYQMAFT
VGLVLLSGLA YILPHWRWLQ LAVSLPIFLL LFRFWFVPES PRWLLSQKRN TEAIKIMDHI
AQKNGKLPPA DLKMLSLEED VTEKLSPSFI DLFRTPNLRK YTFILMYLWF TSSVVYQGLI
MHVGATGGNL YLDFLYSALV EFPAGFIILV TIDRFGRRYP LATSNLAAGL ACFLMIFIPH
DLPWLNIMVA CVGRMGITIV FQMVCLVNAE LFPTFIRNLG MMVCSSLCDL GGVLTPFLVF
RLMEVWQGSP LILFAALGLV AGGMTLLLPE TKGVTLPETI EDAENLQRKA KPKENKIYLQ
VQTSELNTQA AERDASQGTA QQK
