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P14142

- GTR4_MOUSE

UniProt

P14142 - GTR4_MOUSE

Protein

Solute carrier family 2, facilitated glucose transporter member 4

Gene

Slc2a4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Insulin-regulated facilitative glucose transporter.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei333 – 3331MonosaccharideBy similarity
    Binding sitei404 – 4041MonosaccharideBy similarity

    GO - Molecular functioni

    1. D-glucose transmembrane transporter activity Source: Ensembl
    2. glucose transmembrane transporter activity Source: MGI
    3. insulin-responsive hydrogen:glucose symporter activity Source: MGI
    4. protein binding Source: MGI

    GO - Biological processi

    1. amylopectin biosynthetic process Source: MGI
    2. brown fat cell differentiation Source: MGI
    3. cellular response to insulin stimulus Source: UniProtKB
    4. cellular response to osmotic stress Source: MGI
    5. glucose homeostasis Source: Ensembl
    6. glucose transport Source: MGI
    7. response to ethanol Source: Ensembl

    Keywords - Biological processi

    Sugar transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_206357. Facilitative Na+-independent glucose transporters.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Solute carrier family 2, facilitated glucose transporter member 4
    Alternative name(s):
    GT2
    Glucose transporter type 4, insulin-responsive
    Short name:
    GLUT-4
    Gene namesi
    Name:Slc2a4
    Synonyms:Glut-4, Glut4
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:95758. Slc2a4.

    Subcellular locationi

    Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication. Endomembrane system By similarity; Multi-pass membrane protein By similarity. Cytoplasmperinuclear region By similarity
    Note: Localizes primarily to the perinuclear region, undergoing continued recycling to the plasma membrane where it is rapidly reinternalized. The dileucine internalization motif is critical for intracellular sequestration By similarity.By similarity

    GO - Cellular componenti

    1. coated pit Source: Ensembl
    2. cytoplasmic vesicle membrane Source: MGI
    3. endomembrane system Source: UniProtKB
    4. endosome Source: MGI
    5. external side of plasma membrane Source: Ensembl
    6. extracellular vesicular exosome Source: MGI
    7. insulin-responsive compartment Source: UniProtKB
    8. integral component of membrane Source: MGI
    9. integral component of plasma membrane Source: MGI
    10. membrane Source: MGI
    11. multivesicular body Source: Ensembl
    12. perinuclear region of cytoplasm Source: MGI
    13. plasma membrane Source: UniProtKB
    14. sarcolemma Source: MGI
    15. trans-Golgi network transport vesicle Source: MGI

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Defects in Slc2a4 may be the cause of certain post-receptor defects in non-insulin-dependent diabetes mellitus (NIDDM).

    Keywords - Diseasei

    Diabetes mellitus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 509509Solute carrier family 2, facilitated glucose transporter member 4PRO_0000050364Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi57 – 571N-linked (GlcNAc...)1 Publication
    Modified residuei274 – 2741Phosphoserine; by SGK1By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP14142.
    PaxDbiP14142.
    PRIDEiP14142.

    PTM databases

    PhosphoSiteiP14142.

    Expressioni

    Tissue specificityi

    Skeletal and cardiac muscles; brown and white fat.

    Gene expression databases

    ArrayExpressiP14142.
    BgeeiP14142.
    GenevestigatoriP14142.

    Interactioni

    Subunit structurei

    Binds to DAXX. Interacts via its N-terminus with SRFBP1. Interacts with NDUFA9 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi203307. 4 interactions.
    DIPiDIP-42440N.
    IntActiP14142. 1 interaction.
    MINTiMINT-1342290.

    Structurei

    3D structure databases

    ProteinModelPortaliP14142.
    SMRiP14142. Positions 31-481.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 2323CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini45 – 8036ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini102 – 1109CytoplasmicSequence Analysis
    Topological domaini132 – 14110ExtracellularSequence Analysis
    Topological domaini163 – 1708CytoplasmicSequence Analysis
    Topological domaini192 – 2009ExtracellularSequence Analysis
    Topological domaini222 – 28665CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini308 – 32215ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini344 – 3529CytoplasmicSequence Analysis
    Topological domaini374 – 38411ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini406 – 41611CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini438 – 4447ExtracellularSequence Analysis
    Topological domaini466 – 50843CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei24 – 4421Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei81 – 10121Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei111 – 13121Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei142 – 16221Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei171 – 19121Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei201 – 22121Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei287 – 30721Helical; Name=7Sequence AnalysisAdd
    BLAST
    Transmembranei323 – 34321Helical; Name=8Sequence AnalysisAdd
    BLAST
    Transmembranei353 – 37321Helical; Name=9Sequence AnalysisAdd
    BLAST
    Transmembranei385 – 40521Helical; Name=10Sequence AnalysisAdd
    BLAST
    Transmembranei417 – 43721Helical; Name=11Sequence AnalysisAdd
    BLAST
    Transmembranei445 – 46521Helical; Name=12Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 137SRFBP1-bindingBy similarity
    Regioni298 – 3047Monosaccharide bindingBy similarity

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi489 – 4902Dileucine internalization motifSequence Analysis

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0477.
    GeneTreeiENSGT00720000108560.
    HOGENOMiHOG000202871.
    HOVERGENiHBG014816.
    InParanoidiQ3TPK6.
    KOiK07191.
    OMAiAMLVNNI.
    OrthoDBiEOG7QVM2R.
    TreeFamiTF313762.

    Family and domain databases

    InterProiIPR002441. Glc_transpt_4.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR003663. Sugar/inositol_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view]
    PfamiPF00083. Sugar_tr. 1 hit.
    [Graphical view]
    PRINTSiPR01193. GLUCTRSPORT4.
    PR00171. SUGRTRNSPORT.
    SUPFAMiSSF103473. SSF103473. 1 hit.
    TIGRFAMsiTIGR00879. SP. 1 hit.
    PROSITEiPS50850. MFS. 1 hit.
    PS00216. SUGAR_TRANSPORT_1. 1 hit.
    PS00217. SUGAR_TRANSPORT_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P14142-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSGFQQIGS DDGEPPRQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK    50
    VIEQSYNATW LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG 100
    IISQWLGRKR AMLANNVLAV LGGALMGLAN AAASYEILIL GRFLIGAYSG 150
    LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI VIGILVAQVL GLESMLGTAT 200
    LWPLLLALTV LPALLQLILL PFCPESPRYL YIIRNLEGPA RKSLKRLTGW 250
    ADVSDALAEL KDEKRKLERE RPMSLLQLLG SRTHRQPLII AVVLQLSQQL 300
    SGINAVFYYS TSIFESAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR 350
    TLHLLGLAGM CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG 400
    PIPWFIVAEL FSQGPRPAAM AVAGFSNWTC NFIVGMGFQY VADAMGPYVF 450
    LLFAVLLLGF FIFTFLKVPE TRGRTFDQIS AAFRRTPSLL EQEVKPSTEL 500
    EYLGPDEND 509
    Length:509
    Mass (Da):54,755
    Last modified:July 27, 2011 - v3
    Checksum:iA174212455EE0390
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111D → DVK in AAA37753. (PubMed:2654938)Curated
    Sequence conflicti132 – 1321A → V in AAA37753. (PubMed:2654938)Curated
    Sequence conflicti177 – 1771Q → R in AAA37753. (PubMed:2654938)Curated
    Sequence conflicti246 – 2461R → P in AAA37753. (PubMed:2654938)Curated
    Sequence conflicti406 – 4061Missing in AAA37753. (PubMed:2654938)Curated
    Sequence conflicti444 – 4441A → R in AAA37753. (PubMed:2654938)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23383 mRNA. Translation: AAA37753.1.
    AB008453 mRNA. Translation: BAB03251.1.
    AY902342 Genomic DNA. Translation: AAX90627.1.
    AK137607 mRNA. Translation: BAE23429.1.
    AK164310 mRNA. Translation: BAE37730.1.
    AL596185 Genomic DNA. Translation: CAI35157.1.
    CH466596 Genomic DNA. Translation: EDL12494.1.
    CH466596 Genomic DNA. Translation: EDL12496.1.
    BC014282 mRNA. Translation: AAH14282.1.
    CCDSiCCDS36201.1.
    PIRiB30310.
    RefSeqiNP_033230.2. NM_009204.2.
    UniGeneiMm.10661.

    Genome annotation databases

    EnsembliENSMUST00000018710; ENSMUSP00000018710; ENSMUSG00000018566.
    GeneIDi20528.
    KEGGimmu:20528.
    UCSCiuc007jsy.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M23383 mRNA. Translation: AAA37753.1 .
    AB008453 mRNA. Translation: BAB03251.1 .
    AY902342 Genomic DNA. Translation: AAX90627.1 .
    AK137607 mRNA. Translation: BAE23429.1 .
    AK164310 mRNA. Translation: BAE37730.1 .
    AL596185 Genomic DNA. Translation: CAI35157.1 .
    CH466596 Genomic DNA. Translation: EDL12494.1 .
    CH466596 Genomic DNA. Translation: EDL12496.1 .
    BC014282 mRNA. Translation: AAH14282.1 .
    CCDSi CCDS36201.1.
    PIRi B30310.
    RefSeqi NP_033230.2. NM_009204.2.
    UniGenei Mm.10661.

    3D structure databases

    ProteinModelPortali P14142.
    SMRi P14142. Positions 31-481.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203307. 4 interactions.
    DIPi DIP-42440N.
    IntActi P14142. 1 interaction.
    MINTi MINT-1342290.

    Chemistry

    ChEMBLi CHEMBL1250410.

    PTM databases

    PhosphoSitei P14142.

    Proteomic databases

    MaxQBi P14142.
    PaxDbi P14142.
    PRIDEi P14142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018710 ; ENSMUSP00000018710 ; ENSMUSG00000018566 .
    GeneIDi 20528.
    KEGGi mmu:20528.
    UCSCi uc007jsy.1. mouse.

    Organism-specific databases

    CTDi 6517.
    MGIi MGI:95758. Slc2a4.

    Phylogenomic databases

    eggNOGi COG0477.
    GeneTreei ENSGT00720000108560.
    HOGENOMi HOG000202871.
    HOVERGENi HBG014816.
    InParanoidi Q3TPK6.
    KOi K07191.
    OMAi AMLVNNI.
    OrthoDBi EOG7QVM2R.
    TreeFami TF313762.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_206357. Facilitative Na+-independent glucose transporters.

    Miscellaneous databases

    NextBioi 298775.
    PROi P14142.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14142.
    Bgeei P14142.
    Genevestigatori P14142.

    Family and domain databases

    InterProi IPR002441. Glc_transpt_4.
    IPR020846. MFS_dom.
    IPR016196. MFS_dom_general_subst_transpt.
    IPR005828. Sub_transporter.
    IPR003663. Sugar/inositol_transpt.
    IPR005829. Sugar_transporter_CS.
    [Graphical view ]
    Pfami PF00083. Sugar_tr. 1 hit.
    [Graphical view ]
    PRINTSi PR01193. GLUCTRSPORT4.
    PR00171. SUGRTRNSPORT.
    SUPFAMi SSF103473. SSF103473. 1 hit.
    TIGRFAMsi TIGR00879. SP. 1 hit.
    PROSITEi PS50850. MFS. 1 hit.
    PS00216. SUGAR_TRANSPORT_1. 1 hit.
    PS00217. SUGAR_TRANSPORT_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence, tissue distribution, and differential expression of mRNA for a putative insulin-responsive glucose transporter in mouse 3T3-L1 adipocytes."
      Kaestner K.H., Christy R.J., McLenithan J.C., Braiterman L.T., Cornelius P., Pekala P.H., Lane M.D.
      Proc. Natl. Acad. Sci. U.S.A. 86:3150-3154(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Age-dependent changes in phenotypes and candidate gene analysis in a polygenic animal model of type II diabetes; NSY mouse."
      Ueda H., Ikegami H., Kawaguchi Y., Fujisawa T., Nojima K., Babaya N., Yamada K., Shibata M., Yamato E., Ogihara T.
      Diabetologia 43:932-938(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C3H and NSY.
      Tissue: Muscle.
    3. "Characterization of quantitative trait loci influencing growth and adiposity using congenic mouse strains."
      Farber C.R., Corva P.M., Medrano J.F.
      Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: CAST/EiJ.
      Tissue: Brain.
    4. "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.
      , 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: Bone and Spinal ganglion.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    6. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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].
      Tissue: Colon.
    8. "Insulin-stimulated phosphorylation of a Rab GTPase-activating protein regulates GLUT4 translocation."
      Sano H., Kane S., Sano E., Miinea C.P., Asara J.M., Lane W.S., Garner C.W., Lienhard G.E.
      J. Biol. Chem. 278:14599-14602(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: EFFECT OF TBC1D4 ON GLUT4 TRANSLOCATION.
    9. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57.
    10. "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
      Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
      Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiGTR4_MOUSE
    AccessioniPrimary (citable) accession number: P14142
    Secondary accession number(s): Q3TPK6, Q9JJN9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Insulin-stimulated phosphorylation of TBC1D4 is required for GLUT4 translocation.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3