GTR12_MOUSE
ID GTR12_MOUSE Reviewed; 622 AA.
AC Q8BFW9; Q14B60; Q3UPR6; Q8BZB7;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Solute carrier family 2, facilitated glucose transporter member 12 {ECO:0000305};
DE AltName: Full=Glucose transporter type 12 {ECO:0000303|PubMed:15465484};
DE Short=GLUT-12 {ECO:0000303|PubMed:15465484};
GN Name=Slc2a12 {ECO:0000312|MGI:MGI:3052471};
GN Synonyms=Glut12 {ECO:0000303|PubMed:15465484};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=CD-1; TISSUE=White adipose tissue;
RX PubMed=12890477; DOI=10.1016/s0006-291x(03)01322-6;
RA Wood I.S., Hunter L., Trayhurn P.;
RT "Expression of class III facilitative glucose transporter genes (GLUT-10
RT and GLUT-12) in mouse and human adipose tissues.";
RL Biochem. Biophys. Res. Commun. 308:43-49(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
RX PubMed=15465484; DOI=10.1016/j.modgep.2004.04.010;
RA Zhou Y., Kaye P.L., Pantaleon M.;
RT "Identification of the facilitative glucose transporter 12 gene Glut12 in
RT mouse preimplantation embryos.";
RL Gene Expr. Patterns 4:621-631(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Oviduct, Skin, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23041416; DOI=10.1016/j.bbadis.2012.09.013;
RA Waller A.P., George M., Kalyanasundaram A., Kang C., Periasamy M., Hu K.,
RA Lacombe V.A.;
RT "GLUT12 functions as a basal and insulin-independent glucose transporter in
RT the heart.";
RL Biochim. Biophys. Acta 1832:121-127(2013).
CC -!- FUNCTION: Insulin-independent facilitative glucose transporter.
CC {ECO:0000269|PubMed:23041416}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) = D-glucose(in); Xref=Rhea:RHEA:60376,
CC ChEBI:CHEBI:4167; Evidence={ECO:0000305|PubMed:23041416};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23041416};
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 skeletal muscle, heart, brain, kidney,
CC spleen, adipose tissues and to a lesser extent in small intestine and
CC lung. {ECO:0000269|PubMed:12890477}.
CC -!- DEVELOPMENTAL STAGE: Expression is clearly detected in ovulated oocytes
CC and 2-cells embryos but decline day 3 morulae. Remains at very low
CC levels between 2 dpc and 11 dpc. {ECO:0000269|PubMed:15465484}.
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; AJ549317; CAD70577.1; -; mRNA.
DR EMBL; AY230881; AAP45844.1; -; mRNA.
DR EMBL; AK028970; BAC26220.1; -; mRNA.
DR EMBL; AK031659; BAC27497.1; -; mRNA.
DR EMBL; AK035972; BAC29262.1; -; mRNA.
DR EMBL; AK143263; BAE25329.1; -; mRNA.
DR EMBL; BC096454; AAH96454.1; -; mRNA.
DR EMBL; BC116314; AAI16315.1; -; mRNA.
DR EMBL; BC116315; AAI16316.1; -; mRNA.
DR CCDS; CCDS23729.1; -.
DR RefSeq; NP_849265.2; NM_178934.4.
DR AlphaFoldDB; Q8BFW9; -.
DR SMR; Q8BFW9; -.
DR STRING; 10090.ENSMUSP00000043962; -.
DR GlyGen; Q8BFW9; 5 sites.
DR PhosphoSitePlus; Q8BFW9; -.
DR MaxQB; Q8BFW9; -.
DR PaxDb; Q8BFW9; -.
DR PRIDE; Q8BFW9; -.
DR ProteomicsDB; 271347; -.
DR Antibodypedia; 32959; 123 antibodies from 24 providers.
DR DNASU; 353169; -.
DR Ensembl; ENSMUST00000042261; ENSMUSP00000043962; ENSMUSG00000037490.
DR GeneID; 353169; -.
DR KEGG; mmu:353169; -.
DR UCSC; uc007epo.2; mouse.
DR CTD; 154091; -.
DR MGI; MGI:3052471; Slc2a12.
DR VEuPathDB; HostDB:ENSMUSG00000037490; -.
DR eggNOG; KOG0254; Eukaryota.
DR GeneTree; ENSGT00940000159614; -.
DR HOGENOM; CLU_001265_30_5_1; -.
DR InParanoid; Q8BFW9; -.
DR OMA; SCHEQEM; -.
DR OrthoDB; 430696at2759; -.
DR PhylomeDB; Q8BFW9; -.
DR TreeFam; TF332408; -.
DR Reactome; R-MMU-189200; Cellular hexose transport.
DR BioGRID-ORCS; 353169; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slc2a12; mouse.
DR PRO; PR:Q8BFW9; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8BFW9; protein.
DR Bgee; ENSMUSG00000037490; Expressed in choroid plexus epithelium and 166 other tissues.
DR ExpressionAtlas; Q8BFW9; baseline and differential.
DR Genevisible; Q8BFW9; MM.
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; IDA:MGI.
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:1904659; P:glucose transmembrane transport; IDA:MGI.
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 TIGRFAMs; TIGR00879; SP; 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..622
FT /note="Solute carrier family 2, facilitated glucose
FT transporter member 12"
FT /id="PRO_0000292016"
FT TOPO_DOM 1..44
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 66..84
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 106..111
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 133..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 190..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 223..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..471
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 493..503
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 504..524
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 525..533
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 534..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..622
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 195
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 387
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 405
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 159
FT /note="I -> L (in Ref. 3; BAE25329)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="A -> S (in Ref. 4; AAI16316)"
FT /evidence="ECO:0000305"
FT CONFLICT 290
FT /note="V -> I (in Ref. 3; BAC29262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 622 AA; 67336 MW; E308C83C3EA8267D CRC64;
MVPVENTEGP NLLNQKGREA ETEGSCGASG GGHPACAGGP SMFTFLTSVT AAISGLLVGY
ELGLISGALL QIRTLLALTC HEQEMVVSSL LIGAFLASLT GGVLIDRYGR RLAIILSSCL
LGLGSLVLIM SLSYTLLIMG RVAIGVSISL SSIATCVYIA EIAPQHRRGL LVSLNELMIV
TGILFAYISN YAFANISNGW KYMFGLVIPL GVLQAIAMYF LPPSPRFLVM KGQEESAGKV
LRKLRVISDT TEELTLIKSS LKDEYQYSFW DLFRSKDNMR TRILIGLTLV FFVQTTGQPN
ILFYASTVLK SVGFQSNEAA SLASTGVGVV KVVSTIPATL LVDHIGSKTF LCIGSSVMSA
SLLTMGIVNL NINMNFTNIC RSHSLLNQSL EEFVFYATGN LSISNSSLRE HFKRITPYSK
GSFMPMGNGM EPKGEMTFTS SLPNAGLSRT EHQGVTDTAV VPAAYKWLSL ASLLVYVAAF
SIGLGPMPWL VLSEIFPGGI RGRAMALTSS MNWGVNLLIS LTFLTVTDLI GLSWVCFIYT
IMSLASLAFV VLFIPETKGC SLEQISVELA KANYVKNNIC FMSHHQEELV PTQLQKRKPQ
EQLPECNHLC GRGQSQRPSP DT
