SC5A8_XENLA
ID SC5A8_XENLA Reviewed; 622 AA.
AC Q7SYH5; Q6PAX9; Q7SYH3; Q7SYH4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Sodium-coupled monocarboxylate transporter 1;
DE AltName: Full=Electrogenic sodium monocarboxylate cotransporter;
DE Short=xSMCTe;
DE AltName: Full=Sodium solute transporter Vito;
DE AltName: Full=Solute carrier family 5 member 8;
GN Name=slc5a8 {ECO:0000303|Ref.2};
GN Synonyms=smcte {ECO:0000312|EMBL:AAW55813.1},
GN vito {ECO:0000312|EMBL:AAP82285.1};
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAP82286.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Midgut {ECO:0000312|EMBL:AAP82286.1}, and
RC Tail bud {ECO:0000312|EMBL:AAP82286.1};
RX PubMed=12915320; DOI=10.1016/s1567-133x(03)00086-3;
RA Costa R.M.B., Mason J., Lee M., Amaya E., Zorn A.M.;
RT "Novel gene expression domains reveal early patterning of the Xenopus
RT endoderm.";
RL Gene Expr. Patterns 3:509-519(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAW55813.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Plata C.M., Romero M.F.;
RT "Cloning and expression of the Xenopus electrogenic sodium monocarboxylate
RT cotransporter, xSMCTe (Slc5A8).";
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:AAW55813.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH60005.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (OCT-2003) 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q8N695}; Multi-
CC pass membrane protein {ECO:0000250|UniProtKB:Q8N695}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:12915320}; Synonyms=vito-a
CC {ECO:0000269|PubMed:12915320}, vito-b {ECO:0000269|PubMed:12915320};
CC IsoId=Q7SYH5-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:12915320}; Synonyms=vito-c
CC {ECO:0000269|PubMed:12915320};
CC IsoId=Q7SYH5-2; Sequence=VSP_052791, VSP_052792;
CC -!- TISSUE SPECIFICITY: In the gastrula and neurula stages, expressed in
CC the gastrula anterior endoderm and in the entire circumference of the
CC blastopore lip superficial endoderm. At tailbud stages, abundant
CC expression observed in the ventral midgut region. As development
CC proceeds expression becomes restricted to the liver diverticulum and
CC ultimately to the presumptive gallbladder, by tadpole stage 35. Also
CC present in pronephros and the tip of the tail.
CC {ECO:0000269|PubMed:12915320}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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DR EMBL; AY260728; AAP82285.1; -; mRNA.
DR EMBL; AY260729; AAP82286.1; -; mRNA.
DR EMBL; AY260730; AAP82287.1; -; mRNA.
DR EMBL; AY727861; AAW55813.1; -; mRNA.
DR EMBL; BC060005; AAH60005.1; -; mRNA.
DR RefSeq; NP_001084454.1; NM_001090985.1. [Q7SYH5-1]
DR AlphaFoldDB; Q7SYH5; -.
DR SMR; Q7SYH5; -.
DR DNASU; 403396; -.
DR GeneID; 403396; -.
DR KEGG; xla:403396; -.
DR CTD; 403396; -.
DR Xenbase; XB-GENE-865289; slc5a8.1.L.
DR OrthoDB; 1180002at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 403396; Expressed in intestine and 9 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Alternative splicing; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..622
FT /note="Sodium-coupled monocarboxylate transporter 1"
FT /id="PRO_0000334502"
FT TOPO_DOM 1..15
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..51
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 73..83
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..128
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..161
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 183..184
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..283
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..336
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 358..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..415
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 437..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 460..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 591..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 596..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 389..402
FT /note="SLLYGAICIGMAGI -> TPPAGHFLTSLTTK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12915320"
FT /id="VSP_052791"
FT VAR_SEQ 403..622
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12915320"
FT /id="VSP_052792"
FT CONFLICT 285
FT /note="I -> V (in Ref. 1; AAP82286)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="A -> P (in Ref. 1; AAP82287)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="I -> L (in Ref. 1; AAP82286)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="Missing (in Ref. 2; AAW55813 and 3; AAH60005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 67556 MW; B5CC3D2F2065A2DF CRC64;
MVTPGNIGSF TVWDYLVFAL MLLISAVIGI YYAFAGGGQK TSKDFLMGGR SMTAVPVALS
LTASFMSAVT VLGTPAEVYR FGAMFIIFAF SYTIVVIISS EVFLPVFYRL GITSTYEYLE
LRFNKFVRLL GTILFIIQTV LYTGIVIYAP ALALNQVTGF DLWGAVVATG VVCTFYCTMG
GLKAVVWTDV FQVGIMVAGF TSVIIRAVVV QGGIGPILND SYYGDRLNFW DFDPNPLKRH
TFWTIVVGGT FTWTGIYGVN QAQVQRYIAC KTRFQAKMSL YVNLIGLWAI LACAVLSGLA
MYSIYKDCDP WTAKFVSAPD QLMPYLALDI LRDYPGLPGL FVSCAYSGTL STVSSSINAL
AAVTVEDLIK PYIRSLSEKK MSWISKGTSL LYGAICIGMA GIASLMGGLL QAALSIFGMV
GGPLLGLFSL GILFPFVNSL GAVIGLLSGF AISLWVGIGS QIYAPSPSSS LPKPLSLEGC
NFTSIESNWT STVMPMMTTL IPETQVSSRP ELADSWYSLS YLYFSTIGTI VAVLVGVIVS
LLSGGLKQNV NREFLLTSED FSYLNVLFSP CKEKGQEEKV EVLNWKARRT DNDMEQGTDN
PAFNNMEMTS TEKGEKTNGI TA
