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Protein

Solute carrier family 2, facilitated glucose transporter member 4

Gene

Slc2a4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

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

Keywords - Biological processi

Sugar transport, Transport

Enzyme and pathway databases

ReactomeiREACT_297294. Glucose transport.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_346905. 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 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:95758. Slc2a4.

Subcellular locationi

  1. Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
  2. Endomembrane system By similarity; Multi-pass membrane protein By similarity
  3. Cytoplasmperinuclear region By similarity

  4. 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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2323CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei24 – 4421Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini45 – 8036ExtracellularSequence AnalysisAdd
BLAST
Transmembranei81 – 10121Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini102 – 1109CytoplasmicSequence Analysis
Transmembranei111 – 13121Helical; Name=3Sequence AnalysisAdd
BLAST
Topological domaini132 – 14110ExtracellularSequence Analysis
Transmembranei142 – 16221Helical; Name=4Sequence AnalysisAdd
BLAST
Topological domaini163 – 1708CytoplasmicSequence Analysis
Transmembranei171 – 19121Helical; Name=5Sequence AnalysisAdd
BLAST
Topological domaini192 – 2009ExtracellularSequence Analysis
Transmembranei201 – 22121Helical; Name=6Sequence AnalysisAdd
BLAST
Topological domaini222 – 28665CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei287 – 30721Helical; Name=7Sequence AnalysisAdd
BLAST
Topological domaini308 – 32215ExtracellularSequence AnalysisAdd
BLAST
Transmembranei323 – 34321Helical; Name=8Sequence AnalysisAdd
BLAST
Topological domaini344 – 3529CytoplasmicSequence Analysis
Transmembranei353 – 37321Helical; Name=9Sequence AnalysisAdd
BLAST
Topological domaini374 – 38411ExtracellularSequence AnalysisAdd
BLAST
Transmembranei385 – 40521Helical; Name=10Sequence AnalysisAdd
BLAST
Topological domaini406 – 41611CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei417 – 43721Helical; Name=11Sequence AnalysisAdd
BLAST
Topological domaini438 – 4447ExtracellularSequence Analysis
Transmembranei445 – 46521Helical; Name=12Sequence AnalysisAdd
BLAST
Topological domaini466 – 50843CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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

BgeeiP14142.
ExpressionAtlasiP14142. baseline and differential.
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 21-471.
ModBaseiSearch...
MobiDBiSearch...

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.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP14142.
KOiK07191.
OMAiAMLVNNI.
OrthoDBiEOG7QVM2R.
TreeFamiTF313762.

Family and domain databases

InterProiIPR002441. Glc_transpt_4.
IPR020846. MFS_dom.
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

        10         20         30         40         50
MPSGFQQIGS DDGEPPRQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK
60 70 80 90 100
VIEQSYNATW LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG
110 120 130 140 150
IISQWLGRKR AMLANNVLAV LGGALMGLAN AAASYEILIL GRFLIGAYSG
160 170 180 190 200
LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI VIGILVAQVL GLESMLGTAT
210 220 230 240 250
LWPLLLALTV LPALLQLILL PFCPESPRYL YIIRNLEGPA RKSLKRLTGW
260 270 280 290 300
ADVSDALAEL KDEKRKLERE RPMSLLQLLG SRTHRQPLII AVVLQLSQQL
310 320 330 340 350
SGINAVFYYS TSIFESAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR
360 370 380 390 400
TLHLLGLAGM CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG
410 420 430 440 450
PIPWFIVAEL FSQGPRPAAM AVAGFSNWTC NFIVGMGFQY VADAMGPYVF
460 470 480 490 500
LLFAVLLLGF FIFTFLKVPE TRGRTFDQIS AAFRRTPSLL EQEVKPSTEL

EYLGPDEND
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliP14142.
SMRiP14142. Positions 21-471.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Chemistry

ChEMBLiCHEMBL1250410.

PTM databases

PhosphoSiteiP14142.

Proteomic databases

MaxQBiP14142.
PaxDbiP14142.
PRIDEiP14142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi6517.
MGIiMGI:95758. Slc2a4.

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000119022.
HOGENOMiHOG000202871.
HOVERGENiHBG014816.
InParanoidiP14142.
KOiK07191.
OMAiAMLVNNI.
OrthoDBiEOG7QVM2R.
TreeFamiTF313762.

Enzyme and pathway databases

ReactomeiREACT_297294. Glucose transport.
REACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_346905. Facilitative Na+-independent glucose transporters.

Miscellaneous databases

NextBioi298775.
PROiP14142.
SOURCEiSearch...

Gene expression databases

BgeeiP14142.
ExpressionAtlasiP14142. baseline and differential.
GenevestigatoriP14142.

Family and domain databases

InterProiIPR002441. Glc_transpt_4.
IPR020846. MFS_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: April 1, 2015
This is version 154 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.