Solute carrier family 2, facilitated glucose transporter member 4

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Reviewed, UniProtKB/Swiss-Prot P14142 (GTR4_MOUSE)

Last modified February 9, 2010. Version 106. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Solute carrier family 2, facilitated glucose transporter member 4
Alternative name(s):
    Glucose transporter type 4, insulin-responsive
      Short name=GLUT-4
    GT2

Gene names

Name:	Slc2a4
Synonyms:	Glut-4, Glut4

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	509 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Insulin-regulated facilitative glucose transporter.
Subunit structure	Binds to DAXX. Interacts via its N-terminus with SRFBP1 By similarity.
Subcellular location	Endomembrane system; Multi-pass membrane protein By similarity. Cytoplasm › perinuclear 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.
Tissue specificity	Skeletal and cardiac muscles; brown and white fat.
Involvement in disease	Defects in Slc2a4 may be the cause of certain post-receptor defects in non-insulin-dependent diabetes mellitus (NIDDM).
Miscellaneous	Insulin-stimulated phosphorylation of TBC1D4 is required for GLUT4 translocation.
Sequence similarities	Belongs to the major facilitator superfamily. Sugar transporter (TC 2.A.1.1) family. Glucose transporter subfamily. [View classification]

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Ontologies

Keywords
Biological process	Sugar transport Transport
Cellular component	Cytoplasm Membrane
Disease	Diabetes mellitus
Domain	Transmembrane
PTM	Glycoprotein Phosphoprotein
Gene Ontology (GO)
Biological process	brown fat cell differentiation Inferred from direct assay. Source: MGI glucose transport Inferred from direct assay. Source: MGI transmembrane transport Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasmic vesicle membrane Inferred from direct assay. Source: MGI integral to membrane of membrane fraction Inferred from direct assay. Source: MGI integral to plasma membrane Inferred from direct assay. Source: MGI microsome Inferred from direct assay. Source: MGI perinuclear region of cytoplasm Inferred from direct assay. Source: MGI trans-Golgi network transport vesicle Inferred from direct assay. Source: MGI
Molecular function	insulin-responsive hydrogen:glucose symporter activity Traceable author statement. Source: MGI
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 509

509

Solute carrier family 2, facilitated glucose transporter member 4

PRO_0000050364

Regions

Topological domain

1 – 23

Cytoplasmic Potential

Transmembrane

24 – 44

1 Potential

Topological domain

45 – 80

Extracellular Potential

Transmembrane

81 – 101

2 Potential

Topological domain

102 – 110

Cytoplasmic Potential

Transmembrane

111 – 131

3 Potential

Topological domain

132 – 141

Extracellular Potential

Transmembrane

142 – 162

4 Potential

Topological domain

163 – 170

Cytoplasmic Potential

Transmembrane

171 – 191

5 Potential

Topological domain

192 – 200

Extracellular Potential

Transmembrane

201 – 221

6 Potential

Topological domain

222 – 286

Cytoplasmic Potential

Transmembrane

287 – 307

7 Potential

Topological domain

308 – 322

Extracellular Potential

Transmembrane

323 – 343

8 Potential

Topological domain

344 – 352

Cytoplasmic Potential

Transmembrane

353 – 373

9 Potential

Topological domain

374 – 384

Extracellular Potential

Transmembrane

385 – 405

10 Potential

Topological domain

406 – 416

Cytoplasmic Potential

Transmembrane

417 – 437

11 Potential

Topological domain

438 – 444

Extracellular Potential

Transmembrane

445 – 465

12 Potential

Topological domain

466 – 508

Cytoplasmic Potential

Region

7 – 13

SRFBP1-binding By similarity

Region

294 – 296

Defines substrate specificity By similarity

Motif

489 – 490

Dileucine internalization motif Potential

Amino acid modifications

Modified residue

488

Phosphoserine Ref.5

Glycosylation

N-linked (GlcNAc...) Ref.6

Experimental info

Sequence conflict

D → DVK in AAA37753. Ref.1

Sequence conflict

132

V → A in BAB03251. Ref.2

Sequence conflict

177

Q → R in AAA37753. Ref.1

Sequence conflict

246

R → P in AAA37753. Ref.1

Sequence conflict

406

Missing in AAA37753. Ref.1

Sequence conflict

444

A → R in AAA37753. Ref.1

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Sequences

Sequence

Length

Mass (Da)

Tools

P14142-1 [UniParc].

Last modified November 16, 2001. Version 2.
Checksum: 6D260D7C45EB889D
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FASTA

509

54,783

        10         20         30         40         50         60 
MPSGFQQIGS DDGEPPRQRV TGTLVLAVFS AVLGSLQFGY NIGVINAPQK VIEQSYNATW 

        70         80         90        100        110        120 
LGRQGPGGPD SIPQGTLTTL WALSVAIFSV GGMISSFLIG IISQWLGRKR AMLANNVLAV 

       130        140        150        160        170        180 
LGGALMGLAN AVASYEILIL GRFLIGAYSG LTSGLVPMYV GEIAPTHLRG ALGTLNQLAI 

       190        200        210        220        230        240 
VIGILVAQVL GLESMLGTAT LWPLLLALTV LPALLQLILL PFCPESPRYL YIIRNLEGPA 

       250        260        270        280        290        300 
RKSLKRLTGW ADVSDALAEL KDEKRKLERE RPMSLLQLLG SRTHRQPLII AVVLQLSQQL 

       310        320        330        340        350        360 
SGINAVFYYS TSIFESAGVG QPAYATIGAG VVNTVFTLVS VLLVERAGRR TLHLLGLAGM 

       370        380        390        400        410        420 
CGCAILMTVA LLLLERVPAM SYVSIVAIFG FVAFFEIGPG PIPWFIVAEL FSQGPRPAAM 

       430        440        450        460        470        480 
AVAGFSNWTC NFIVGMGFQY VADAMGPYVF LLFAVLLLGF FIFTFLKVPE TRGRTFDQIS 

       490        500 
AAFRRTPSLL EQEVKPSTEL EYLGPDEND

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2654938] [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: 10952468] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C3H and NSY. Tissue: Muscle.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon.
[4]	"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: 12637568] [Abstract] Cited for: EFFECT OF TBC1D4 ON GLUT4 TRANSLOCATION.
[5]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 18973353] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-488, MASS SPECTROMETRY.
[6]	"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: 19349973] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-57, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
EMBL GenBank DDBJ	M23383 mRNA. Translation: AAA37753.1. AB008453 mRNA. Translation: BAB03251.1. BC014282 mRNA. Translation: AAH14282.1.
IPI	IPI00762242.
PIR	B30310.
RefSeq	NP_033230.2.
UniGene	Mm.10661
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P14142.
PTM databases
PhosphoSite	P14142.
Proteomic databases
PRIDE	P14142.
Genome annotation databases
Ensembl	ENSMUST00000018710; ENSMUSP00000018710; ENSMUSG00000018566; Mus musculus. [Genome view]
GeneID	20528.
KEGG	mmu:20528.
Organism-specific databases
CTD	20528.
MGI	MGI:95758. Slc2a4.
Phylogenomic databases
eggNOG	roNOG11437.
HOGENOM	HBG744444.
HOVERGEN	P14142.
InParanoid	P14142.
PhylomeDB	P14142.
Gene expression databases
ArrayExpress	P14142.
Bgee	P14142.
Genevestigator	P14142.
GermOnline	ENSMUSG00000018566. Mus musculus.
Family and domain databases
InterPro	IPR002441. Glc_transpt_4. IPR016196. MFS_general_subst_transpt. IPR003663. Sugar/inositol_transpt. IPR005829. Sugar_transporter_CS. [Graphical view]
PRINTS	PR01193. GLUCTRSPORT4. PR00171. SUGRTRNSPORT.
TIGRFAMs	TIGR00879. SP. 1 hit.
PROSITE	PS50850. MFS. 1 hit. PS00216. SUGAR_TRANSPORT_1. 1 hit. PS00217. SUGAR_TRANSPORT_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
SOURCE	Search...

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Entry information

Entry name

GTR4_MOUSE

Accession

Primary (citable) accession number: P14142
Secondary accession number(s): Q9JJN9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	November 16, 2001
Last modified:	February 9, 2010
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents