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GTR12_DANRE
ID   GTR12_DANRE             Reviewed;         610 AA.
AC   Q6NWF1; Q6PHV4;
DT   26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Solute carrier family 2, facilitated glucose transporter member 12 {ECO:0000305};
DE   AltName: Full=Glucose transporter type 12 {ECO:0000303|PubMed:25326603};
DE            Short=GLUT-12 {ECO:0000303|PubMed:25326603};
GN   Name=slc2a12 {ECO:0000250|UniProtKB:Q8TD20};
GN   Synonyms=glut12 {ECO:0000303|PubMed:25326603};
GN   ORFNames=zgc:66027 {ECO:0000303|Ref.1}, zgc:85776 {ECO:0000303|Ref.1};
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 [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX   PubMed=25326603; DOI=10.1530/joe-14-0539;
RA   Jimenez-Amilburu V., Jong-Raadsen S., Bakkers J., Spaink H.P.,
RA   Marin-Juez R.;
RT   "GLUT12 deficiency during early development results in heart failure and a
RT   diabetic phenotype in zebrafish.";
RL   J. Endocrinol. 224:1-15(2015).
CC   -!- FUNCTION: Insulin-regulated facilitative glucose transporter.
CC       {ECO:0000269|PubMed:25326603}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC         ChEBI:CHEBI:4167; Evidence={ECO:0000305|PubMed:25326603};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9};
CC       Multi-pass membrane protein {ECO:0000255}. Endomembrane system
CC       {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein
CC       {ECO:0000255}. Cytoplasm, perinuclear region
CC       {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear
CC       region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
CC   -!- TISSUE SPECIFICITY: Expressed in the main insulin-sensitive tissues,
CC       such as cardiac muscle, skeletal muscle and adipose tissue.
CC       {ECO:0000269|PubMed:25326603}.
CC   -!- DISRUPTION PHENOTYPE: Morpholino knockdown of the protein impairs the
CC       development of the embryonic heart resulting in abnormal valve
CC       formation (PubMed:25326603). Embryos also show poor glycemic control
CC       (PubMed:25326603). {ECO:0000269|PubMed:25326603}.
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; BC056306; AAH56306.1; -; mRNA.
DR   EMBL; BC067616; AAH67616.2; -; mRNA.
DR   RefSeq; NP_956832.1; NM_200538.1.
DR   RefSeq; XP_005162361.1; XM_005162304.3.
DR   AlphaFoldDB; Q6NWF1; -.
DR   SMR; Q6NWF1; -.
DR   STRING; 7955.ENSDARP00000053530; -.
DR   PaxDb; Q6NWF1; -.
DR   Ensembl; ENSDART00000053531; ENSDARP00000053530; ENSDARG00000036865.
DR   GeneID; 393510; -.
DR   KEGG; dre:393510; -.
DR   CTD; 154091; -.
DR   ZFIN; ZDB-GENE-040426-1513; slc2a12.
DR   eggNOG; KOG0254; Eukaryota.
DR   GeneTree; ENSGT00940000159614; -.
DR   InParanoid; Q6NWF1; -.
DR   OMA; SCHEQEM; -.
DR   OrthoDB; 430696at2759; -.
DR   PhylomeDB; Q6NWF1; -.
DR   TreeFam; TF332408; -.
DR   Reactome; R-DRE-189200; Cellular hexose transport.
DR   PRO; PR:Q6NWF1; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 23.
DR   Bgee; ENSDARG00000036865; Expressed in bone element and 20 other tissues.
DR   ExpressionAtlas; Q6NWF1; baseline and differential.
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:0005886; C:plasma membrane; 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; IBA:GO_Central.
DR   GO; GO:0044381; P:glucose import in response to insulin stimulus; IMP:ZFIN.
DR   GO; GO:1904659; P:glucose transmembrane transport; IBA:GO_Central.
DR   GO; GO:0060047; P:heart contraction; IMP:ZFIN.
DR   GO; GO:0007507; P:heart development; IMP:ZFIN.
DR   GO; GO:0003179; P:heart valve morphogenesis; 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   Cell membrane; Cytoplasm; Glycoprotein; Membrane; Reference proteome;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..610
FT                   /note="Solute carrier family 2, facilitated glucose
FT                   transporter member 12"
FT                   /id="PRO_0000292017"
FT   TOPO_DOM        1..49
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..84
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        106..118
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        140..141
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        163..176
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        198..201
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        202..222
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        223..286
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        287..307
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        308..325
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        326..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        347..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..475
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        497..511
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        512..532
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        533..542
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        543..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        564..610
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        392
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        429
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        438
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        32
FT                   /note="G -> S (in Ref. 1; AAH56306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        423
FT                   /note="T -> A (in Ref. 1; AAH56306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        442
FT                   /note="N -> D (in Ref. 1; AAH56306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        448
FT                   /note="M -> I (in Ref. 1; AAH56306)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        597
FT                   /note="T -> I (in Ref. 1; AAH56306)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   610 AA;  65778 MW;  E5F794C4805E757C CRC64;
     MDAPEESIRM TSDPQSKIYV QNPDTHIHLE QGPSAKSGNG RALVLCSVSV ACLSGLLMGY
     EMSLISGALL QLRDVLTLSC PEQEQVVGSL LLGAFLLSLG GGTILDHYGR RFTIILTALL
     CVLGTLLSVC VVSFWALVVG RMLVGMSVAL SGTASCLYAA EVAPAAWRGR CVCVYELMVV
     LGMLLGFGLS WAFAGVPDGW RFTFGGALLP ALLQAGVMPL LPDSPRFLLA QQREKEAHAT
     LLRLRAGIKE VEPVEDELRA IRLAMGAERL HGFLDLFQSR DNMLQRLLVG AALVFLQQAT
     GQPNILAYAS TVLSSVGFHG NEAATLASTG FGVVKVGGTI PAIFLVDKVG PKALLCVGVV
     VMMLSTATLG AITMQSRTHV SSLCRGPGNT ANFTLFETGD ETDIQTNTPL GLYQPQNKLK
     TNTFLTSIND TREHWILNHT YNHRTALMET AELSKKDSAK IALQSLHEVS PSLKWISLVS
     LLVYVAGFSI SLGPMVHVVL SAIFPTGIRG KAVSVISAFN WATNLLISMT FLTLTERIGL
     PTVIFSYSAM SFLLVVFVIV FVPETKGRSL EQISKELAMK NHLRGTLLCH RRKHKATAQP
     SQEEKALATV
 
 
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