S22A1_PIG
ID S22A1_PIG Reviewed; 554 AA.
AC Q863T6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Solute carrier family 22 member 1;
DE AltName: Full=Organic cation transporter 1;
DE AltName: Full=pOCT1;
GN Name=SLC22A1; Synonyms=OCT1;
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;
RA Honscha K.U., Aschenbach J.R., Gabel G.;
RT "Molecular and functional characterization of pig kidney OCT1.";
RL Submitted (FEB-2003) 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; AY238476; AAP13545.1; -; mRNA.
DR AlphaFoldDB; Q863T6; -.
DR SMR; Q863T6; -.
DR STRING; 9823.ENSSSCP00000004367; -.
DR PaxDb; Q863T6; -.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q863T6; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; 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; IBA:GO_Central.
DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
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 Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00898; 2A0119; 1.
DR PROSITE; PS50850; MFS; 1.
PE 2: Evidence at transcript 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_0000333877"
FT TOPO_DOM 1..24
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 46..234
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 256..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..347
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 348..368
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..431
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 453..464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 465..485
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..492
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 493..513
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 514..554
FT /note="Extracellular"
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; 61226 MW; 7E246BAED9DB4B83 CRC64;
MPSVDDVLEQ VGEFGWFQKQ AFLNLCLTSV AFAPIYVGIV FLGFTPDHRC RSPGVAELSQ
RCGWSLAEEL NYTVPGLGPA GQAFPRQCRR YEVDWNQSTL GCEDPLAGLA ANSSHLPLGP
CQYGWVYDTP GSSIVTEFNL VCEAAWKVDL FQSCVNVGFF VGSMGIGYIA DRLVGSSASW
PPPHQCRLGR PDAVAPDYVS LLVFRLLQGL VSKGSWMAGY TLITEFVGLG YRKTVAILYQ
TAFSVGLVLL SGLAYAVPHW RSLQLAVSLP IFLLLLCYWF VPESPRWLLS QKRNTQAIKI
MDRIAQKNGK LPPADLKMLS LEEEVVTERL SPSFLDLFRT QNLRKYTFIL MYLWFTSSVL
YQGLIMHVGA TGGSLYLDFL YSALVEFPAA FVILLIIDRF GRLYLLAGSN LLAGAACFFM
IFISHDLHWL SIVAACIGRM GITIVFQMVC LVSAELYPTF IRNLGVMVCS SLCDLGGVVA
PFLVFRLTEV WRGLPLVLFA ALGLVAGGMS LLLPETKGVA LPETIEEVER LGRKAKPRDN
MIYLQVKMPE PAGL
