GTR10_DANRE
ID GTR10_DANRE Reviewed; 513 AA.
AC F1R0H0; A8KB28; I1SV80;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 10 {ECO:0000305};
DE AltName: Full=Glucose transporter type 10 {ECO:0000303|PubMed:22116938};
DE Short=GLUT-10 {ECO:0000303|PubMed:22116938};
GN Name=slc2a10 {ECO:0000303|PubMed:21553381,
GN ECO:0000312|ZFIN:ZDB-GENE-080204-6};
GN Synonyms=glut10 {ECO:0000303|PubMed:22116938};
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]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RC STRAIN=AB;
RX PubMed=21553381; DOI=10.1387/ijdb.103179nc;
RA Chiarelli N., Ritelli M., Zoppi N., Benini A., Borsani G., Barlati S.,
RA Colombi M.;
RT "Characterization and expression pattern analysis of the facilitative
RT glucose transporter 10 gene (slc2a10) in Danio rerio.";
RL Int. J. Dev. Biol. 55:229-236(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
RA Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA Clee C., Oliver K., Clark R., Riddle C., Elliot D., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., Rogers J., Stemple D.L.;
RT "The zebrafish reference genome sequence and its relationship to the human
RT genome.";
RL Nature 496:498-503(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22116938; DOI=10.1093/hmg/ddr555;
RA Willaert A., Khatri S., Callewaert B.L., Coucke P.J., Crosby S.D.,
RA Lee J.G., Davis E.C., Shiva S., Tsang M., De Paepe A., Urban Z.;
RT "GLUT10 is required for the development of the cardiovascular system and
RT the notochord and connects mitochondrial function to TGFbeta signaling.";
RL Hum. Mol. Genet. 21:1248-1259(2012).
CC -!- FUNCTION: Facilitative glucose transporter required for the development
CC of the cardiovascular system. {ECO:0000269|PubMed:22116938}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000250|UniProtKB:O95528};
CC -!- SUBCELLULAR LOCATION: Endomembrane system
CC {ECO:0000250|UniProtKB:O95528}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:O95528}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically
CC (PubMed:21553381). Ubiquitous expression until the early somitogenesis
CC stage (PubMed:21553381). In later embryonic stages, detected in the
CC otic vesicles, hatching gland cells, pectoral fin, posterior tectum and
CC swim bladder (PubMed:21553381). {ECO:0000269|PubMed:21553381}.
CC -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein causes
CC notochord and cardiovascular abnormalities (PubMed:22116938). Fishes
CC display a reduced heart rate and blood flow, coupled with an incomplete
CC and irregular vascular patterning (PubMed:22116938).
CC {ECO:0000269|PubMed:22116938}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sugar
CC transporter (TC 2.A.1.1) family. Glucose transporter subfamily.
CC {ECO:0000305}.
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DR EMBL; HM560591; AEF56581.1; -; mRNA.
DR EMBL; HM560592; AEF56582.1; -; mRNA.
DR EMBL; CU928126; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC153938; AAI53939.1; -; mRNA.
DR RefSeq; NP_001104633.1; NM_001111163.1.
DR RefSeq; XP_005172836.1; XM_005172779.3.
DR AlphaFoldDB; F1R0H0; -.
DR SMR; F1R0H0; -.
DR STRING; 7955.ENSDARP00000104821; -.
DR TCDB; 2.A.1.1.85; the major facilitator superfamily (mfs).
DR PaxDb; F1R0H0; -.
DR Ensembl; ENSDART00000167938; ENSDARP00000130266; ENSDARG00000090820.
DR Ensembl; ENSDART00000171219; ENSDARP00000135785; ENSDARG00000090820.
DR GeneID; 560546; -.
DR KEGG; dre:560546; -.
DR CTD; 81031; -.
DR ZFIN; ZDB-GENE-080204-6; slc2a10.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000159430; -.
DR InParanoid; F1R0H0; -.
DR OMA; GCIWLPE; -.
DR OrthoDB; 326501at2759; -.
DR PhylomeDB; F1R0H0; -.
DR TreeFam; TF332408; -.
DR Reactome; R-DRE-189200; Cellular hexose transport.
DR PRO; PR:F1R0H0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 11.
DR Bgee; ENSDARG00000090820; Expressed in mature ovarian follicle and 33 other tissues.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005355; F:glucose transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015293; F:symporter activity; IBA:GO_Central.
DR GO; GO:0072359; P:circulatory system development; IMP:ZFIN.
DR GO; GO:1904659; P:glucose transmembrane transport; IBA:GO_Central.
DR GO; GO:0030903; P:notochord development; IMP:ZFIN.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR003663; Sugar/inositol_transpt.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF00083; Sugar_tr; 2.
DR PRINTS; PR00171; SUGRTRNSPORT.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Glycoprotein; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..513
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 10"
FT /id="PRO_0000447627"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 7..27
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..46
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 47..67
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..80
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 81..101
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..104
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 105..125
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 126..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 131..151
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 152..164
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 165..185
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..236
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 237..257
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 258..272
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 273..293
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 294..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 302..322
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 423..443
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..513
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT BINDING 246..247
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT BINDING 399
FT /ligand="D-glucose"
FT /ligand_id="ChEBI:CHEBI:4167"
FT /evidence="ECO:0000250|UniProtKB:P11169"
FT CARBOHYD 270
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 85
FT /note="A -> T (in Ref. 3; AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="I -> V (in Ref. 3; AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="I -> F (in Ref. 1; AEF56581/AEF56582 and 3;
FT AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="P -> Q (in Ref. 1; AEF56581/AEF56582 and 3;
FT AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="H -> R (in Ref. 1; AEF56581/AEF56582)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="R -> T (in Ref. 3; AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="D -> E (in Ref. 1; AEF56581/AEF56582 and 3;
FT AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 425
FT /note="A -> T (in Ref. 3; AAI53939)"
FT /evidence="ECO:0000305"
FT CONFLICT 430
FT /note="S -> T (in Ref. 1; AEF56581/AEF56582 and 3;
FT AAI53939)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 55944 MW; 053133F21B2E8033 CRC64;
MGCSVLLLTI TVSTLGGLVF GYELGIISGA LPQLQTHFSL GCVQQEAVVS ALLIGSLFAS
IIGGWLIDRH GRRTSILLSN LLILAGSVIL TTGTSFFALV IGRAVIGFAM TVSSMSCCIF
VSEMVTPERR GLMVTLYEVG ITVGILIAYA VNYIFNNVPL TGWRYMFGFA IIPSLIQLAS
IVLLPKQAEV FVIHDDDSRQ ADRLTEETET SNQHQQSEKY GVSDLFKSKD NMRRRTVIGV
GLVLSQQFTG QPNVLFYAST ILFSVGFQSN ASAILASVGF GIVKVIATLL AMLCSDRAGR
RSLLIGGCSM LAVGLILTGF LCRQSVIDTT KRCTSVGPHS NLTLSAEHDE GVGFSSQTLD
VHEHLRSFSQ SEDIYKWIIF TCLMAVVSAF SVSFGPMTWV VLSEIFPKDI RGRAFSFINC
FNVGANLIVS FSFLSIIDVI GLSGVFLMYG VVGIAGVVFI YLVLPETKGK SLQDIDRELS
QTRMIHRQEL CSIFQRRRFS PGYQRVQLTS TAT
