S22A4_RAT
ID S22A4_RAT Reviewed; 553 AA.
AC Q9R141;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Solute carrier family 22 member 4;
DE AltName: Full=Organic cation/carnitine transporter 1;
GN Name=Slc22a4; Synonyms=Octn1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=10825452; DOI=10.1016/s0005-2736(00)00189-9;
RA Wu X., George R.L., Huang W., Wang H., Conway S.J., Leibach F.H.,
RA Ganapathy V.;
RT "Structural and functional characteristics and tissue distribution pattern
RT of OCTN1, an organic cation transporter, cloned from placenta.";
RL Biochim. Biophys. Acta 1466:315-327(2000).
CC -!- FUNCTION: Sodium-ion dependent, low affinity carnitine transporter.
CC Probably transports one sodium ion with one molecule of carnitine. Also
CC transports organic cations such as tetraethylammonium (TEA) without the
CC involvement of sodium. Relative uptake activity ratio of carnitine to
CC TEA is 1.78. {ECO:0000269|PubMed:10825452}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 8.0. At higher pH, transport activity decreases.
CC {ECO:0000269|PubMed:10825452};
CC -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in intestine, liver and kidney. Weakly
CC expressed in brain, thymus, lung, spleen, heart and skin. In brain, it
CC is expressed in cerebellum, especially in the granular layer, in
CC hippocampus and cortex. In kidney, it is expressed in cortex and
CC medulla with relatively more abundance in the cortical-medullary
CC junction. In heart, it is expressed in myocardium and valves. Expressed
CC labyrinthine zone of the placenta. {ECO:0000269|PubMed:10825452}.
CC -!- MISCELLANEOUS: Inhibited by desipramin > DMA > procainamide >
CC cimetidine.
CC -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC -!- CAUTION: It is unclear whether it transports carnitine in vivo.
CC {ECO:0000305}.
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DR EMBL; AF169831; AAD46922.1; -; mRNA.
DR RefSeq; NP_071606.1; NM_022270.1.
DR AlphaFoldDB; Q9R141; -.
DR SMR; Q9R141; -.
DR BindingDB; Q9R141; -.
DR ChEMBL; CHEMBL2073667; -.
DR GlyGen; Q9R141; 3 sites.
DR iPTMnet; Q9R141; -.
DR PhosphoSitePlus; Q9R141; -.
DR PaxDb; Q9R141; -.
DR Ensembl; ENSRNOT00000058907; ENSRNOP00000055693; ENSRNOG00000046195.
DR GeneID; 64037; -.
DR KEGG; rno:64037; -.
DR CTD; 6583; -.
DR RGD; 621149; Slc22a4.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154155; -.
DR InParanoid; Q9R141; -.
DR OrthoDB; 655566at2759; -.
DR PhylomeDB; Q9R141; -.
DR Reactome; R-RNO-549127; Organic cation transport.
DR PRO; PR:Q9R141; -.
DR Proteomes; UP000002494; Chromosome 10.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0015171; F:amino acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015226; F:carnitine transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015491; F:cation:cation antiporter activity; ISO:RGD.
DR GO; GO:0015101; F:organic cation transmembrane transporter activity; IDA:RGD.
DR GO; GO:0030165; F:PDZ domain binding; ISO:RGD.
DR GO; GO:0015651; F:quaternary ammonium group transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0089718; P:amino acid import across plasma membrane; ISO:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISO:RGD.
DR GO; GO:0015879; P:carnitine transport; ISO:RGD.
DR GO; GO:0015697; P:quaternary ammonium group transport; IDA:RGD.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006641; P:triglyceride metabolic process; ISO:RGD.
DR GO; GO:0042908; P:xenobiotic transport; ISO:RGD.
DR CDD; cd17376; MFS_SLC22A4_5_OCTN1_2; 1.
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; IPR045915; S22A4/5.
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 ATP-binding; Glycoprotein; Ion transport; Membrane; Nucleotide-binding;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..553
FT /note="Solute carrier family 22 member 4"
FT /id="PRO_0000220499"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..41
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 42..142
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..171
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 172..192
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 193..197
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 219..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..257
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 258..278
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..360
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..373
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..400
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 401..421
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 422..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..462
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 463..483
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 484..488
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 489..509
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 510..553
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 553 AA; 62362 MW; E26C8155768A14AD CRC64;
MRDYDEVIAF LGDWGPFQRL IFFLLSASII PNGFNGMSVV FLAGTPEHRC LVPHTVNLSS
AWRNHSIPLE TKDGRQVPQS CRRYRLATIA NFSALGLEPG LDVDLEQLEQ ESCLDGWEYS
KDVFLSTIVT EWNLVCEDDW KTPLTTSLFF VGVLCGSFVS GQLSDRFGRK KVLFATMAVQ
TGFSFVQIFS TNWEMFTVLF AIVGMGQISN YVVAFILGTE ILSKSVRILF STLGVCTFFA
IGYMVLPLFA YFIRDWRMLL LALTLPGLFC VPLWWFIPES PRWLISQRRF EEAEQIIQKA
AKMNGIMAPA VIFDPLELQE LNSLKQQKVF ILDLFKTRNI ATITVMSVML WMLTSVGYFA
LSLNVPNLHG DVYLNCFLSG LIEVPAYFTA WLLLRTLPRR YIIAGVLFWG GGVLLLVQVV
PEDYNFVSIG LVMLGKFGVT SAFSMLYVFT AELYPTLVRN MAVGITSMAS RVGSIIAPYF
VYLGAYNRLL PYILMGSLTV LIGIITLFFP ESFGVTLPEN LEQMQKVRGF RCGKKSTVSM
DREENPKVLI TAF
