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Q8BFW9 (GTR12_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 2, facilitated glucose transporter member 12
Alternative name(s):
Glucose transporter type 12
Short name=GLUT-12
Gene names
Name:Slc2a12
Synonyms:Glut12, Glut8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length622 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Facilitative glucose transporter By similarity.

Subcellular location

Endomembrane system; Multi-pass membrane protein By similarity.

Tissue specificity

Expressed in skeletal muscle, heart, brain, kidney, spleen, adipose tissues and to a lesser extend in small intestine and lung. Ref.1

Developmental stage

Expression is clearly detected in ovulated oocytes and 2-cells embryos but decline day 3 morulae. Remains at very low levels betwen E2 and E11. Ref.2

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 622622Solute carrier family 2, facilitated glucose transporter member 12
PRO_0000292016

Regions

Topological domain1 – 4444Cytoplasmic Potential
Transmembrane45 – 6521Helical; Potential
Topological domain66 – 8419Extracellular Potential
Transmembrane85 – 10521Helical; Potential
Topological domain106 – 1116Cytoplasmic Potential
Transmembrane112 – 13221Helical; Potential
Topological domain133 – 1419Extracellular Potential
Transmembrane142 – 16221Helical; Potential
Topological domain163 – 1686Cytoplasmic Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 20112Extracellular Potential
Transmembrane202 – 22221Helical; Potential
Topological domain223 – 28260Cytoplasmic Potential
Transmembrane283 – 30321Helical; Potential
Topological domain304 – 32118Extracellular Potential
Transmembrane322 – 34221Helical; Potential
Topological domain343 – 3497Cytoplasmic Potential
Transmembrane350 – 37021Helical; Potential
Topological domain371 – 471101Extracellular Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 50311Cytoplasmic Potential
Transmembrane504 – 52421Helical; Potential
Topological domain525 – 5339Extracellular Potential
Transmembrane534 – 55421Helical; Potential
Topological domain555 – 62268Cytoplasmic Potential

Amino acid modifications

Glycosylation1951N-linked (GlcNAc...) Potential
Glycosylation3751N-linked (GlcNAc...) Potential
Glycosylation3871N-linked (GlcNAc...) Potential
Glycosylation4001N-linked (GlcNAc...) Potential
Glycosylation4051N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict1591I → L in BAE25329. Ref.3
Sequence conflict1601A → S in AAI16316. Ref.4
Sequence conflict2901V → I in BAC29262. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q8BFW9 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: E308C83C3EA8267D

FASTA62267,336
        10         20         30         40         50         60 
MVPVENTEGP NLLNQKGREA ETEGSCGASG GGHPACAGGP SMFTFLTSVT AAISGLLVGY 

        70         80         90        100        110        120 
ELGLISGALL QIRTLLALTC HEQEMVVSSL LIGAFLASLT GGVLIDRYGR RLAIILSSCL 

       130        140        150        160        170        180 
LGLGSLVLIM SLSYTLLIMG RVAIGVSISL SSIATCVYIA EIAPQHRRGL LVSLNELMIV 

       190        200        210        220        230        240 
TGILFAYISN YAFANISNGW KYMFGLVIPL GVLQAIAMYF LPPSPRFLVM KGQEESAGKV 

       250        260        270        280        290        300 
LRKLRVISDT TEELTLIKSS LKDEYQYSFW DLFRSKDNMR TRILIGLTLV FFVQTTGQPN 

       310        320        330        340        350        360 
ILFYASTVLK SVGFQSNEAA SLASTGVGVV KVVSTIPATL LVDHIGSKTF LCIGSSVMSA 

       370        380        390        400        410        420 
SLLTMGIVNL NINMNFTNIC RSHSLLNQSL EEFVFYATGN LSISNSSLRE HFKRITPYSK 

       430        440        450        460        470        480 
GSFMPMGNGM EPKGEMTFTS SLPNAGLSRT EHQGVTDTAV VPAAYKWLSL ASLLVYVAAF 

       490        500        510        520        530        540 
SIGLGPMPWL VLSEIFPGGI RGRAMALTSS MNWGVNLLIS LTFLTVTDLI GLSWVCFIYT 

       550        560        570        580        590        600 
IMSLASLAFV VLFIPETKGC SLEQISVELA KANYVKNNIC FMSHHQEELV PTQLQKRKPQ 

       610        620 
EQLPECNHLC GRGQSQRPSP DT 

« Hide

References

« Hide 'large scale' references
[1]"Expression of class III facilitative glucose transporter genes (GLUT-10 and GLUT-12) in mouse and human adipose tissues."
Wood I.S., Hunter L., Trayhurn P.
Biochem. Biophys. Res. Commun. 308:43-49(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
Strain: CD-1.
Tissue: White adipose tissue.
[2]"Identification of the facilitative glucose transporter 12 gene Glut12 in mouse preimplantation embryos."
Zhou Y., Kaye P.L., Pantaleon M.
Gene Expr. Patterns 4:621-631(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Cerebellum, Oviduct, Skin and Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Kidney.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ549317 mRNA. Translation: CAD70577.1.
AY230881 mRNA. Translation: AAP45844.1.
AK028970 mRNA. Translation: BAC26220.1.
AK031659 mRNA. Translation: BAC27497.1.
AK035972 mRNA. Translation: BAC29262.1.
AK143263 mRNA. Translation: BAE25329.1.
BC096454 mRNA. Translation: AAH96454.1.
BC116314 mRNA. Translation: AAI16315.1.
BC116315 mRNA. Translation: AAI16316.1.
CCDSCCDS23729.1.
RefSeqNP_849265.2. NM_178934.4.
UniGeneMm.473705.

3D structure databases

ProteinModelPortalQ8BFW9.
SMRQ8BFW9. Positions 63-368, 458-565.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8BFW9.

Proteomic databases

PRIDEQ8BFW9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042261; ENSMUSP00000043962; ENSMUSG00000037490.
GeneID353169.
KEGGmmu:353169.
UCSCuc007epo.2. mouse.

Organism-specific databases

CTD154091.
MGIMGI:3052471. Slc2a12.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00590000083062.
HOGENOMHOG000202868.
HOVERGENHBG051858.
InParanoidQ8BFW9.
KOK08149.
OMAANISNGW.
OrthoDBEOG75B852.
PhylomeDBQ8BFW9.
TreeFamTF332408.

Gene expression databases

ArrayExpressQ8BFW9.
BgeeQ8BFW9.
GenevestigatorQ8BFW9.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR005828. Sub_transporter.
IPR003663. Sugar/inositol_transpt.
IPR005829. Sugar_transporter_CS.
[Graphical view]
PfamPF00083. Sugar_tr. 2 hits.
[Graphical view]
PRINTSPR00171. SUGRTRNSPORT.
SUPFAMSSF103473. SSF103473. 2 hits.
TIGRFAMsTIGR00879. SP. 1 hit.
PROSITEPS50850. MFS. 1 hit.
PS00216. SUGAR_TRANSPORT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio400315.
PROQ8BFW9.
SOURCESearch...

Entry information

Entry nameGTR12_MOUSE
AccessionPrimary (citable) accession number: Q8BFW9
Secondary accession number(s): Q14B60, Q3UPR6, Q8BZB7
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot