SC5A8_XENTR
ID SC5A8_XENTR Reviewed; 620 AA.
AC Q5BL81;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Sodium-coupled monocarboxylate transporter 1;
DE AltName: Full=Electrogenic sodium monocarboxylate cotransporter;
DE AltName: Full=Solute carrier family 5 member 8;
GN Name=slc5a8 {ECO:0000312|EMBL:AAH90570.1};
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:AAH90570.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH90570.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (FEB-2005) 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 -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000255}.
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DR EMBL; BC090570; AAH90570.1; -; mRNA.
DR RefSeq; NP_988910.2; NM_203579.2.
DR AlphaFoldDB; Q5BL81; -.
DR SMR; Q5BL81; -.
DR STRING; 8364.ENSXETP00000005409; -.
DR PaxDb; Q5BL81; -.
DR eggNOG; KOG2349; Eukaryota.
DR InParanoid; Q5BL81; -.
DR OrthoDB; 1180002at2759; -.
DR Proteomes; UP000008143; Genome assembly.
DR Proteomes; UP000790000; Unplaced.
DR Bgee; ENSXETG00000002542; Expressed in mesonephros and 21 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 Glycoprotein; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..620
FT /note="Sodium-coupled monocarboxylate transporter 1"
FT /id="PRO_0000334503"
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..86
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..107
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 108..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..239
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..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..519
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 520..540
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 541..620
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
SQ SEQUENCE 620 AA; 67371 MW; EE694E10CC09865A CRC64;
MVTPGNIGSF TVWDYVVFAL MLLISAVIGI YYAFAGGGQK TSKDFLMGGR SMTAVPVALS
LTASFMSAVT VLGTPAEVYR FGSMFSIFAF TYAIVVVISS EVFLPVFYRL GITSTYEYLE
LRFNKFVRLL GTILFIIQTV LYTGIVIYAP ALALNQVTGF DLWGAVVATG VVCTFYCTMG
GLKAVVWTDV FQVGIMVAGF SSVIIRAVVV QGGIGPILND SYYGDRLNFW DFTPNPLQRH
SFWTIVVGGT FTWTGIYGVN QSQVQRYIAC KTRFQAKLSL YINLLGLWAI LACAVLSGLA
MYSIYKDCDP WTAQFVSAPD QLMPYLSLDI LRDYPGLPGL FVSCAYSGTL STVSSSINAL
AAVTVEDLIK PYFRSLSETK MSWISKGTSL IYGAICIAMA GLASLMGGLL QAALSIFGMV
GGPLLGLFAL GIIFPFVNSL GAVIGLLSGF AISLWVGIGS QIYPPTASSS LPKPLSLEGC
NFTSFESNWT TTVMPMMTTL IPEVSSRPEL ADSWYSLSYL YFSTLGTIVA VVVGVIASLL
SGGLKQNVNR DFLLTSQDFS YLNVLFSNCK KKGQEEKVEV LNWKMRSTDT DMDQGTDNPA
FNHMEMSSTE KKEKMNGIIA
