S13A5_RAT
ID S13A5_RAT Reviewed; 572 AA.
AC Q8CJ44;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Solute carrier family 13 member 5;
DE AltName: Full=Na(+)/citrate cotransporter;
DE Short=NaCT;
DE AltName: Full=Sodium-coupled citrate transporter;
DE AltName: Full=Sodium-dependent citrate transporter;
GN Name=Slc13a5; Synonyms=Nact;
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, TISSUE SPECIFICITY, TRANSPORTER
RP ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=12177002; DOI=10.1074/jbc.m207072200;
RA Inoue K., Zhuang L., Maddox D.M., Smith S.B., Ganapathy V.;
RT "Structure, function, and expression pattern of a novel sodium-coupled
RT citrate transporter (NaCT) cloned from mammalian brain.";
RL J. Biol. Chem. 277:39469-39476(2002).
CC -!- FUNCTION: High-affinity sodium/citrate cotransporter that mediates
CC citrate entry into cells (PubMed:12177002). Transports citrate in a
CC Na(+)-dependent manner, transport process is electrogenic and
CC recognizes the trivalent form of citrate rather than the divalent form
CC (PubMed:12177002). Although citrate is its main substrate, other
CC intermediates of the citric acid cycle, such as succinate, fumarate,
CC malate, oxaloacetate and alpha-ketoglutarate can serve as substrates
CC but with a much lower affinity compared to citrate (By similarity).
CC Shows a substrate sensitivity in the order of citrate > succinate ~
CC fumarate ~ oxaloacetate ~ malate > alpha-ketoglutarate ~ isocitrate (By
CC similarity). Citrate transporter activity is lost when sodium ions are
CC replaced by either potassium or choline ions (By similarity). Transport
CC activity is potentiated by lithium ions in the presence of low
CC concentrations of citrate but this potentiating effect disappears in
CC the presence of high concentrations of citrate (By similarity).
CC Involved in the regulation of citrate levels in the brain (By
CC similarity). {ECO:0000250|UniProtKB:Q67BT3,
CC ECO:0000269|PubMed:12177002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate(out) + 4 Na(+)(out) = citrate(in) + 4 Na(+)(in);
CC Xref=Rhea:RHEA:65664, ChEBI:CHEBI:16947, ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:12177002};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 uM for citrate {ECO:0000269|PubMed:12177002};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:12177002};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q86YT5}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q86YT5};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in liver, testis and brain.
CC {ECO:0000269|PubMed:12177002}.
CC -!- SIMILARITY: Belongs to the SLC13A/DASS transporter (TC 2.A.47) family.
CC NADC subfamily. {ECO:0000305}.
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DR EMBL; AF522186; AAN52081.1; -; mRNA.
DR RefSeq; NP_733768.1; NM_170668.1.
DR AlphaFoldDB; Q8CJ44; -.
DR SMR; Q8CJ44; -.
DR STRING; 10116.ENSRNOP00000020043; -.
DR BindingDB; Q8CJ44; -.
DR ChEMBL; CHEMBL3769295; -.
DR GlyGen; Q8CJ44; 2 sites.
DR PaxDb; Q8CJ44; -.
DR GeneID; 266998; -.
DR KEGG; rno:266998; -.
DR CTD; 284111; -.
DR RGD; 631374; Slc13a5.
DR eggNOG; KOG1281; Eukaryota.
DR HOGENOM; CLU_005170_9_1_1; -.
DR InParanoid; Q8CJ44; -.
DR PhylomeDB; Q8CJ44; -.
DR TreeFam; TF312913; -.
DR Reactome; R-RNO-433137; Sodium-coupled sulphate, di- and tri-carboxylate transporters.
DR PRO; PR:Q8CJ44; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; Q8CJ44; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0015137; F:citrate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0005343; F:organic acid:sodium symporter activity; IDA:RGD.
DR GO; GO:0017153; F:sodium:dicarboxylate symporter activity; IDA:RGD.
DR GO; GO:0015141; F:succinate transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015142; F:tricarboxylic acid transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central.
DR GO; GO:0071285; P:cellular response to lithium ion; ISS:UniProtKB.
DR GO; GO:0015746; P:citrate transport; IDA:RGD.
DR GO; GO:0015741; P:fumarate transport; ISS:UniProtKB.
DR GO; GO:0015729; P:oxaloacetate transport; ISS:UniProtKB.
DR GO; GO:0015744; P:succinate transport; IDA:RGD.
DR GO; GO:0006842; P:tricarboxylic acid transport; ISO:RGD.
DR InterPro; IPR031312; Na/sul_symport_CS.
DR InterPro; IPR001898; SLC13A/DASS.
DR Pfam; PF00939; Na_sulph_symp; 1.
DR PROSITE; PS01271; NA_SULFATE; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..572
FT /note="Solute carrier family 13 member 5"
FT /id="PRO_0000260103"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 532..552
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 382
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 566
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 572 AA; 63878 MW; 9CD35A72FC50D374 CRC64;
MASAKTYVTK FKSFVILFFA PILLLPLIIL VPDKFARCAY VIILMAIYWC TDVIPVAITS
LLPVLLFPLL KVLDSKQVCV QYMTDTNMLF LGSLIVATAV ERWELHKRIA LRMLLFVGTK
PSRLMLGFMF VTAFLSMWIS NTATTAMMIP IVEAMLEQMV ATNVAVDASQ RTMELLDKNK
ASELPGSQVV FEDPSVQKQE DEETKNMYKA MNLCVCYAAS IGGTATLTGT GPNVVLLGQM
QELFPDSKDV MNFASWFAFA LPNMLLMLVM AWLWLLCFYM RPNLKKTCIC CGRKKKDTEK
IASKVLYEEY RKLGPLSYAE CNVLFCFGLL IILWFSRDPG FMPGWLSIAW IEGNTKHVTD
ATVAIFVAIL LFIVPSQKPK FNFSRQTEEE RKTPFYPPPL LNWKVTQEKV PWGIVLLLGG
GFAMAKGCET SGLSEWMARQ MEPLSSVRPA IITLILSCIV AMTTECTSNV ATTTLFLPIF
ASMARSIGIH PLYVMIPCTL SASLAFMLPV ATPPNAIVFA YGHLKVIDMV KTGLVMNILG
IASVFLSVNT WGRAVFNLDK FPDWANLTHI NT
