S22A5_RAT
ID S22A5_RAT Reviewed; 557 AA.
AC O70594; Q9QWL0;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Solute carrier family 22 member 5;
DE AltName: Full=CT1;
DE AltName: Full=High-affinity sodium-dependent carnitine cotransporter;
DE AltName: Full=Organic cation/carnitine transporter 2;
DE AltName: Full=UST2r;
GN Name=Slc22a5; Synonyms=Octn2;
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].
RC TISSUE=Kidney;
RX PubMed=9541011; DOI=10.1016/s0014-5793(98)00203-8;
RA Schoemig E., Spitzenberger F., Engelhardt M., Martel F., Oerding N.,
RA Gruendemann D.;
RT "Molecular cloning and characterization of two novel transport proteins
RT from rat kidney.";
RL FEBS Lett. 425:79-86(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Intestine;
RX PubMed=9792817; DOI=10.1006/bbrc.1998.9521;
RA Sekine T., Kusuhara H., Utsunomiya-Tate N., Tsuda M., Sugiyama Y.,
RA Kanai Y., Endou H.;
RT "Molecular cloning and characterization of high-affinity carnitine
RT transporter from rat intestine.";
RL Biochem. Biophys. Res. Commun. 251:586-591(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=10454528;
RA Wu X., Huang W., Prasad P.D., Seth P., Rajan D.P., Leibach F.H., Chen J.,
RA Conway S.J., Ganapathy V.;
RT "Functional characteristics and tissue distribution pattern of organic
RT cation transporter 2 (OCTN2), an organic cation/carnitine transporter.";
RL J. Pharmacol. Exp. Ther. 290:1482-1492(1999).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Sodium-ion dependent, high affinity carnitine transporter.
CC Involved in the active cellular uptake of carnitine. Transports one
CC sodium ion with one molecule of carnitine. Also transports organic
CC cations such as tetraethylammonium (TEA) without the involvement of
CC sodium. Also relative uptake activity ratio of carnitine to TEA is
CC 11.3.
CC -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Expressed in the proximal and distal tubules and in
CC the glomeruli in the kidney, in the myocardium, valves, and arterioles
CC in the heart, in the labyrinthine layer of the placenta, and in the
CC cortex, hippocampus, and cerebellum in the brain.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ001933; CAA05106.1; -; mRNA.
DR EMBL; AB017260; BAA34399.1; -; mRNA.
DR EMBL; AF110416; AAD54059.1; -; mRNA.
DR PIR; JE0346; JE0346.
DR RefSeq; NP_062142.1; NM_019269.1.
DR AlphaFoldDB; O70594; -.
DR SMR; O70594; -.
DR IntAct; O70594; 4.
DR STRING; 10116.ENSRNOP00000011340; -.
DR BindingDB; O70594; -.
DR ChEMBL; CHEMBL1075238; -.
DR GlyGen; O70594; 3 sites.
DR iPTMnet; O70594; -.
DR PhosphoSitePlus; O70594; -.
DR PaxDb; O70594; -.
DR Ensembl; ENSRNOT00000011340; ENSRNOP00000011340; ENSRNOG00000008432.
DR GeneID; 29726; -.
DR KEGG; rno:29726; -.
DR UCSC; RGD:3702; rat.
DR CTD; 6584; -.
DR RGD; 3702; Slc22a5.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000154155; -.
DR InParanoid; O70594; -.
DR OMA; MSWWLVP; -.
DR OrthoDB; 396963at2759; -.
DR PhylomeDB; O70594; -.
DR TreeFam; TF315847; -.
DR Reactome; R-RNO-200425; Carnitine metabolism.
DR Reactome; R-RNO-549127; Organic cation transport.
DR PRO; PR:O70594; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000008432; Expressed in adult mammalian kidney and 18 other tissues.
DR ExpressionAtlas; O70594; baseline and differential.
DR Genevisible; O70594; RN.
DR GO; GO:0016324; C:apical plasma membrane; ISO:RGD.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0031526; C:brush border membrane; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; NAS:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1901235; F:(R)-carnitine transmembrane transporter activity; IMP:ARUK-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0015226; F:carnitine 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:1902270; P:(R)-carnitine transmembrane transport; IMP:ARUK-UCL.
DR GO; GO:0007512; P:adult heart development; ISO:RGD.
DR GO; GO:0009437; P:carnitine metabolic process; ISO:RGD.
DR GO; GO:0015879; P:carnitine transport; IDA:RGD.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR GO; GO:0007626; P:locomotory behavior; ISO:RGD.
DR GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
DR GO; GO:0060731; P:positive regulation of intestinal epithelial structure maintenance; ISO:RGD.
DR GO; GO:0015697; P:quaternary ammonium group transport; IDA:RGD.
DR GO; GO:0048608; P:reproductive structure development; ISO:RGD.
DR GO; GO:0009609; P:response to symbiotic bacterium; ISO:RGD.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR GO; GO:0070715; P:sodium-dependent organic cation transport; ISO:RGD.
DR GO; GO:0150104; P:transport across blood-brain barrier; 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 Phosphoprotein; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Solute carrier family 22 member 5"
FT /id="PRO_0000220502"
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..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..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..341
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..362
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 363..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..406
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..430
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 452..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..557
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 537..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 486
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O76082"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 550
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O76082"
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"
FT CONFLICT 275
FT /note="W -> G (in Ref. 2; BAA34399)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 557 AA; 62567 MW; 172472E7B0A5F043 CRC64;
MRDYDEVTAF LGEWGPFQRL IFFLLSASII PNGFNGMSIV FLAGTPEHRC LVPHTVNLSS
AWRNHSIPLE TKDGRQVPQS CRRYRLATIA NFSALGLEPG RDVDLEQLEQ ENCLDGWEYN
KDVFLSTIVT EWDLVCKDDW KAPLTTSLFF VGVLMGSFIS GQLSDRFGRK NVLFLTMGMQ
TGFSFLQLFS VNFEMFTVLF VLVGMGQISN YVAAFVLGTE ILSKSIRIIF ATLGVCIFYA
FGFMVLPLFA YFIRDWRMLL LALTVPGVLC GALWWFIPES PRWLISQGRV KEAEVIIRKA
AKFNGIVAPS TIFDPSELQD LNSKKPQSHH IYDLVRTRNI RIITIMSIIL WLTISVGYFG
LSLDTPNLHG DIYVNCFLLA AVEVPAYVLA WLLLQHLPRR YSISAALFLG GSVLLFIQLV
PSELFYLSTA LVMVGKFGIT SAYSMVYVYT AELYPTVVRN MGVGVSSTAS RLGSILSPYF
VYLGAYDRFL PYILMGSLTI LTAILTLFFP ESFGAPLPDT IDQMLRVKGI KQWQIQSQTR
TQKDGGESPT VLKSTAF
