SC5A8_DANRE
ID SC5A8_DANRE Reviewed; 610 AA.
AC Q3ZMH1; A0AUP7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Sodium-coupled monocarboxylate transporter 1;
DE AltName: Full=Electrogenic sodium monocarboxylate cotransporter;
DE Short=zSMCTe;
DE AltName: Full=Sodium solute symporter family 5 member 8 protein;
DE AltName: Full=Solute carrier family 5 member 8;
GN Name=slc5a8 {ECO:0000250|UniProtKB:Q8N695};
GN Synonyms=slc5a8l {ECO:0000312|ZFIN:ZDB-GENE-061110-98},
GN smcte {ECO:0000312|EMBL:AAW55811.1}; ORFNames=zgc:152716;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAW55811.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP TISSUE SPECIFICITY.
RX PubMed=17255103; DOI=10.1074/jbc.m609313200;
RA Plata C., Sussman C.R., Sindic A., Liang J.O., Mount D.B., Josephs Z.M.,
RA Chang M.-H., Romero M.F.;
RT "Zebrafish Slc5a12 encodes an electroneutral sodium monocarboxylate
RT transporter (SMCTn). A comparison with the electrogenic SMCT
RT (SMCTe/Slc5a8).";
RL J. Biol. Chem. 282:11996-12009(2007).
RN [2] {ECO:0000312|EMBL:AAI24586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=AB; TISSUE=Intestine;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-
CC dependent sodium-coupled solute transporter, including transport of
CC monocarboxylates (short-chain fatty acids including L-lactate, D-
CC lactate, pyruvate, acetate, propionate, valerate and butyrate),
CC lactate, mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-
CC aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate,
CC acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate
CC stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier
CC mediated diffusion of iodide. Mediates iodide transport from the
CC thyrocyte into the colloid lumen through the apical membrane.
CC {ECO:0000269|PubMed:17255103}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=169 uM for L-lactate {ECO:0000269|PubMed:17255103};
CC KM=535 uM for nicotinate {ECO:0000269|PubMed:17255103};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N695}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q8N695}.
CC -!- TISSUE SPECIFICITY: Expressed in brain and eye 24 hours post-
CC fertilization. In the 5 day old embryo, detected in swim bladder,
CC pronephros (embryonic kidney), pronephric tube, and pronephric ducts,
CC brain, trabecular bar, eyes, otic capsule, stomach, gall bladder, and
CC gut. {ECO:0000269|PubMed:17255103}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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; AY727859; AAW55811.1; -; mRNA.
DR EMBL; BC124585; AAI24586.1; -; mRNA.
DR RefSeq; NP_001030141.1; NM_001034969.1.
DR AlphaFoldDB; Q3ZMH1; -.
DR SMR; Q3ZMH1; -.
DR STRING; 7955.ENSDARP00000030637; -.
DR TCDB; 2.A.21.5.5; the solute:sodium symporter (sss) family.
DR PaxDb; Q3ZMH1; -.
DR GeneID; 556156; -.
DR KEGG; dre:556156; -.
DR CTD; 556156; -.
DR ZFIN; ZDB-GENE-061110-98; slc5a8l.
DR eggNOG; KOG2349; Eukaryota.
DR InParanoid; Q3ZMH1; -.
DR OrthoDB; 1180002at2759; -.
DR PhylomeDB; Q3ZMH1; -.
DR PRO; PR:Q3ZMH1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015355; F:secondary active monocarboxylate transmembrane transporter activity; IDA:ZFIN.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0006814; P:sodium ion transport; IBA:GO_Central.
DR CDD; cd11519; SLC5sbd_SMCT1; 1.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR001734; Na/solute_symporter.
DR InterPro; IPR041992; SLC5sbd_SMCT1.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..610
FT /note="Sodium-coupled monocarboxylate transporter 1"
FT /id="PRO_0000334501"
FT TOPO_DOM 1..10
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..52
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..87
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 109..134
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 135..155
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 156..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..193
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..240
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..261
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 262..284
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..340
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..414
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..440
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 462..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 485
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 453
FT /note="I -> V (in Ref. 2; AAI24586)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="V -> I (in Ref. 2; AAI24586)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 610 AA; 66359 MW; F6A6E706A1DB2321 CRC64;
MPGSGGPVAT FSVWDYVVFA GLILVAAGIG LFQSFRGRKE ASSDEFLLGG RQMTAVPVAL
SLTASFMSGI TVIGTPAEAY LYGTPFWLFF ISYAIMSTIS AEIFVPLFYR LNITSTYEYL
EMRYNKLIRV IGTSMYIIQT ALYTGMVIFA PALALNQITG LDLWGVLVAT GAVCIIYCTL
GGLKAVIWTD VFQMIIMLGG FVAVIARGAV LQGGLGRVWN DSFYGGRLET FSFDPDPLRR
HSFWTIVVGG SLMWASMYSI NQSQVQRYIS CRTMTHAKLS LYVNMVGLWV TVSLAMMSGL
TMYSIYKDCD PFTNKDVGAT DQLLPYLVMD ILADFPGLPG LFVAAAYSGT LSTVSSSINA
LVAVTVEDFM KPAWPSLTER QLSWINMGMS VFYGAVCIGM AGVASMMGNI LQAALSIFGM
ISGPLLGLYM LGMFFRCANS TGGLAGLASG LAITLWVGIG AQLYPPLPEK TLRLPLSVEG
CVALNTSETT TMTPFSTVLQ TTTPQPRPAL ADNWYSLSYL YFSPVGIVVT MIIALIVSAI
SGGCKQKKVR PELFISKSDL ICFRCKKSDS EVSDLIETKP KDNQGLDSPV FYDNEIVLKE
KDQQEKITKL