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P70452 (STX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Syntaxin-4
Gene names
Name:Stx4
Synonyms:Stx4a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length298 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones. Ref.1 Ref.4 Ref.10

Subunit structure

Interacts with STXBP6. Component of the SNARE complex composed of STX4, SNAP23 and VAMP7 that interacts with SYT7 during lysosomal exocytosis By similarity. Found in a complex with VAMP8 and SNAP23. Detected in a complex with SNAP23 and STXBP4. Interacts with VAMP2. Interacts with SNAP23 and SNAPIN. Interacts with LLGL1. Interacts (via C-terminus) with CENPF. Interacts with DOC2B. Interacts with STXBP3; excludes interaction with DOC2B and SNAP25. Interacts with STXBP4; excludes interaction with VAMP2. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.11

Subcellular location

Cell membrane; Single-pass type IV membrane protein Potential Ref.1 Ref.10.

Sequence similarities

Belongs to the syntaxin family.

Contains 1 t-SNARE coiled-coil homology domain.

Ontologies

Keywords
   Biological processNeurotransmitter transport
Transport
   Cellular componentCell membrane
Membrane
   DomainCoiled coil
Transmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processSNARE complex assembly

Inferred from direct assay PubMed 21151919. Source: BHF-UCL

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

synaptic vesicle exocytosis

Traceable author statement PubMed 12297296. Source: MGI

   Cellular_componentSNARE complex

Inferred from sequence or structural similarity. Source: UniProtKB

basolateral plasma membrane

Inferred from direct assay PubMed 18505797. Source: MGI

cell surface

Inferred from direct assay PubMed 21151919. Source: BHF-UCL

cytoplasm

Inferred from direct assay PubMed 12832401. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

lateral loop

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

myelin sheath adaxonal region

Inferred from direct assay PubMed 20237282. Source: BHF-UCL

perinuclear region of cytoplasm

Inferred from direct assay Ref.10. Source: UniProtKB

plasma membrane

Inferred from direct assay PubMed 12832401. Source: MGI

specific granule

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionSNARE binding

Inferred from physical interaction Ref.8. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.8Ref.10Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CenpfQ155P79EBI-645716,EBI-2211248

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 298298Syntaxin-4
PRO_0000210203

Regions

Topological domain1 – 274274Cytoplasmic Potential
Transmembrane275 – 29521Helical; Anchor for type IV membrane protein; Potential
Topological domain296 – 2983Extracellular Potential
Domain200 – 26263t-SNARE coiled-coil homology
Region154 – 298145Interaction with CENPF
Coiled coil38 – 163126 Potential

Amino acid modifications

Modified residue151Phosphoserine Ref.9 Ref.12
Modified residue291Phosphoserine Ref.12
Modified residue1171Phosphoserine Ref.13
Modified residue2481Phosphoserine Ref.12

Experimental info

Sequence conflict471T → I in AAH52023. Ref.3
Sequence conflict1411C → Y in BAE36660. Ref.2
Sequence conflict2811S → Y in BAE26743. Ref.2

Secondary structure

... 298
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70452 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: FCD1477E1126CEC1

FASTA29834,165
        10         20         30         40         50         60 
MRDRTHELRQ GDNISDDEDE VRVALVVHSG AARLGSPDDE FFQKVQTIRQ TMAKLESKVR 

        70         80         90        100        110        120 
ELEKQQVTIL ATPLPEESMK QGLQNLREEI KQLGREVRAQ LKAIEPQKEE ADENYNSVNT 

       130        140        150        160        170        180 
RMKKTQHGVL SQQFVELINK CNSMQSEYRE KNVERIRRQL KITNAGMVSD EELEQMLDSG 

       190        200        210        220        230        240 
QSEVFVSNIL KDTQVTRQAL NEISARHSEI QQLERSIREL HEIFTFLATE VEMQGEMINR 

       250        260        270        280        290 
IEKNILSSAD YVERGQEHVK IALENQKKAR KKKVMIAICV SVTVLILAVI IGITITVG 

« Hide

References

« Hide 'large scale' references
[1]"Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4."
Tellam J.T., Macaulay S.L., McIntosh S., Hewish D.R., Ward C.W., James D.E.
J. Biol. Chem. 272:6179-6186(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH STXB3, SUBCELLULAR LOCATION.
Tissue: Adipocyte.
[2]"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: Olfactory bulb and Placenta.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6, Czech II and FVB/N.
Tissue: Brain and Mammary gland.
[4]"Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes."
Min J., Okada S., Kanzaki M., Elmendorf J.S., Coker K.J., Ceresa B.P., Syu L.-J., Noda Y., Saltiel A.R., Pessin J.E.
Mol. Cell 3:751-760(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH STXBP4; SNAP23 AND VAMP2.
[5]"Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells."
Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I., Manickam E., Rowe T.
Biochem. J. 375:433-440(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNAP23 AND SNAPIN.
[6]"A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells."
Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.
Dev. Cell 7:359-371(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH VAMP8 AND SNAP23.
[7]"Mammalian homolog of Drosophila tumor suppressor lethal (2) giant larvae interacts with basolateral exocytic machinery in Madin-Darby canine kidney cells."
Musch A., Cohen D., Yeaman C., Nelson W.J., Rodriguez-Boulan E., Brennwald P.J.
Mol. Biol. Cell 13:158-168(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LLGL1.
[8]"Doc2beta is a novel Munc18c-interacting partner and positive effector of syntaxin 4-mediated exocytosis."
Ke B., Oh E., Thurmond D.C.
J. Biol. Chem. 282:21786-21797(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH STXBP3 AND VAMP2.
[9]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[10]"Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport."
Pooley R.D., Moynihan K.L., Soukoulis V., Reddy S., Francis R., Lo C., Ma L.-J., Bader D.M.
J. Cell Sci. 121:3413-3421(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CENPF, SUBCELLULAR LOCATION.
[11]"DOC2B: a novel syntaxin-4 binding protein mediating insulin-regulated GLUT4 vesicle fusion in adipocytes."
Fukuda N., Emoto M., Nakamori Y., Taguchi A., Miyamoto S., Uraki S., Oka Y., Tanizawa Y.
Diabetes 58:377-384(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DOC2B.
[12]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15; SER-29 AND SER-248, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U76832 mRNA. Translation: AAB18991.1.
AK145909 mRNA. Translation: BAE26743.1.
AK161971 mRNA. Translation: BAE36660.1.
BC005791 mRNA. Translation: AAH05791.1.
BC011491 mRNA. Translation: AAH11491.1.
BC052023 mRNA. Translation: AAH52023.1.
CCDSCCDS21880.1.
RefSeqNP_033320.1. NM_009294.3.
UniGeneMm.24867.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3PUJX-ray3.31C/D1-10[»]
3PUKX-ray3.05C/D1-10[»]
ProteinModelPortalP70452.
SMRP70452. Positions 39-292.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203563. 5 interactions.
DIPDIP-41399N.
IntActP70452. 6 interactions.
MINTMINT-269272.

PTM databases

PhosphoSiteP70452.

Proteomic databases

MaxQBP70452.
PaxDbP70452.
PRIDEP70452.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.
GeneID20909.
KEGGmmu:20909.
UCSCuc009jwy.1. mouse.

Organism-specific databases

CTD20909.
MGIMGI:893577. Stx4a.

Phylogenomic databases

eggNOGCOG5074.
GeneTreeENSGT00730000110677.
HOGENOMHOG000286023.
HOVERGENHBG000497.
InParanoidQ3TSL5.
KOK13502.
OMAINIRMQR.
OrthoDBEOG7X9G7R.
PhylomeDBP70452.
TreeFamTF313763.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_209837. Membrane Trafficking.

Gene expression databases

ArrayExpressP70452.
BgeeP70452.
CleanExMM_STX4A.
GenevestigatorP70452.

Family and domain databases

InterProIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMSSF47661. SSF47661. 1 hit.
PROSITEPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP70452.
NextBio299793.
PROP70452.
SOURCESearch...

Entry information

Entry nameSTX4_MOUSE
AccessionPrimary (citable) accession number: P70452
Secondary accession number(s): Q3TSL5, Q3UKQ8, Q80WT8
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 122 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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