Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Syntaxin-4

Gene

Stx4

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

Functioni

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.3 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Neurotransmitter transport, Transport

Enzyme and pathway databases

ReactomeiREACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_342156. Disinhibition of SNARE formation.
REACT_347655. Clathrin derived vesicle budding.

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-4
Gene namesi
Name:Stx4
Synonyms:Stx4a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:893577. Stx4a.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 274274CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei275 – 29521Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini296 – 2983ExtracellularSequence Analysis

GO - Cellular componenti

  • basolateral plasma membrane Source: MGI
  • cell surface Source: BHF-UCL
  • cytoplasm Source: MGI
  • dendritic spine Source: MGI
  • endomembrane system Source: GO_Central
  • endosome Source: MGI
  • extracellular exosome Source: MGI
  • extracellular space Source: MGI
  • integral component of membrane Source: GO_Central
  • intracellular Source: MGI
  • lamellipodium Source: MGI
  • lateral loop Source: BHF-UCL
  • membrane Source: MGI
  • myelin sheath adaxonal region Source: BHF-UCL
  • perinuclear region of cytoplasm Source: UniProtKB
  • plasma membrane Source: MGI
  • SNARE complex Source: UniProtKB
  • somatodendritic compartment Source: MGI
  • specific granule Source: MGI
  • storage vacuole Source: MGI
  • synapse Source: MGI
  • synaptic vesicle Source: GO_Central
  • trans-Golgi network Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 298298Syntaxin-4PRO_0000210203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine2 Publications
Modified residuei29 – 291Phosphoserine1 Publication
Modified residuei117 – 1171Phosphoserine1 Publication
Modified residuei248 – 2481Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP70452.
PaxDbiP70452.
PRIDEiP70452.

PTM databases

PhosphoSiteiP70452.

Expressioni

Gene expression databases

BgeeiP70452.
CleanExiMM_STX4A.
ExpressionAtlasiP70452. baseline and differential.
GenevisibleiP70452. MM.

Interactioni

Subunit structurei

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.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CenpfQ155P79EBI-645716,EBI-2211248
Snap23O090442EBI-645716,EBI-1812522

Protein-protein interaction databases

BioGridi203563. 5 interactions.
DIPiDIP-41399N.
IntActiP70452. 8 interactions.
MINTiMINT-269272.
STRINGi10090.ENSMUSP00000033075.

Structurei

Secondary structure

1
298
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 84Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PUJX-ray3.31C/D1-10[»]
3PUKX-ray3.05C/D1-10[»]
ProteinModelPortaliP70452.
SMRiP70452. Positions 39-292.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP70452.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini200 – 26263t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni154 – 298145Interaction with CENPFAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili38 – 163126Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the syntaxin family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5074.
GeneTreeiENSGT00760000119200.
HOGENOMiHOG000286023.
HOVERGENiHBG000497.
InParanoidiP70452.
KOiK13502.
OMAiQKVQTIR.
OrthoDBiEOG7X9G7R.
PhylomeDBiP70452.
TreeFamiTF313763.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70452-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRDRTHELRQ GDNISDDEDE VRVALVVHSG AARLGSPDDE FFQKVQTIRQ
60 70 80 90 100
TMAKLESKVR ELEKQQVTIL ATPLPEESMK QGLQNLREEI KQLGREVRAQ
110 120 130 140 150
LKAIEPQKEE ADENYNSVNT RMKKTQHGVL SQQFVELINK CNSMQSEYRE
160 170 180 190 200
KNVERIRRQL KITNAGMVSD EELEQMLDSG QSEVFVSNIL KDTQVTRQAL
210 220 230 240 250
NEISARHSEI QQLERSIREL HEIFTFLATE VEMQGEMINR IEKNILSSAD
260 270 280 290
YVERGQEHVK IALENQKKAR KKKVMIAICV SVTVLILAVI IGITITVG
Length:298
Mass (Da):34,165
Last modified:February 1, 1997 - v1
Checksum:iFCD1477E1126CEC1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471T → I in AAH52023 (PubMed:15489334).Curated
Sequence conflicti141 – 1411C → Y in BAE36660 (PubMed:16141072).Curated
Sequence conflicti281 – 2811S → Y in BAE26743 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21880.1.
RefSeqiNP_033320.1. NM_009294.3.
UniGeneiMm.24867.

Genome annotation databases

EnsembliENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.
GeneIDi20909.
KEGGimmu:20909.
UCSCiuc009jwy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS21880.1.
RefSeqiNP_033320.1. NM_009294.3.
UniGeneiMm.24867.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PUJX-ray3.31C/D1-10[»]
3PUKX-ray3.05C/D1-10[»]
ProteinModelPortaliP70452.
SMRiP70452. Positions 39-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203563. 5 interactions.
DIPiDIP-41399N.
IntActiP70452. 8 interactions.
MINTiMINT-269272.
STRINGi10090.ENSMUSP00000033075.

PTM databases

PhosphoSiteiP70452.

Proteomic databases

MaxQBiP70452.
PaxDbiP70452.
PRIDEiP70452.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.
GeneIDi20909.
KEGGimmu:20909.
UCSCiuc009jwy.1. mouse.

Organism-specific databases

CTDi20909.
MGIiMGI:893577. Stx4a.

Phylogenomic databases

eggNOGiCOG5074.
GeneTreeiENSGT00760000119200.
HOGENOMiHOG000286023.
HOVERGENiHBG000497.
InParanoidiP70452.
KOiK13502.
OMAiQKVQTIR.
OrthoDBiEOG7X9G7R.
PhylomeDBiP70452.
TreeFamiTF313763.

Enzyme and pathway databases

ReactomeiREACT_302653. Translocation of GLUT4 to the plasma membrane.
REACT_342156. Disinhibition of SNARE formation.
REACT_347655. Clathrin derived vesicle budding.

Miscellaneous databases

EvolutionaryTraceiP70452.
NextBioi299793.
PROiP70452.
SOURCEiSearch...

Gene expression databases

BgeeiP70452.
CleanExiMM_STX4A.
ExpressionAtlasiP70452. baseline and differential.
GenevisibleiP70452. MM.

Family and domain databases

InterProiIPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]
SMARTiSM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]
SUPFAMiSSF47661. SSF47661. 1 hit.
PROSITEiPS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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.

Entry informationi

Entry nameiSTX4_MOUSE
AccessioniPrimary (citable) accession number: P70452
Secondary accession number(s): Q3TSL5, Q3UKQ8, Q80WT8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: June 24, 2015
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.