P70452 (STX4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Syntaxin-4

Gene names

Name:	Stx4
Synonyms:	Stx4a

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	298 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Neurotransmitter transport Transport
Cellular component	Cell membrane Membrane
Domain	Coiled coil Transmembrane Transmembrane helix
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	intracellular protein transport Inferred from electronic annotation. Source: InterPro synaptic vesicle exocytosis Traceable author statement PubMed 12297296. Source: MGI
Cellular_component	SNARE complex Inferred from sequence or structural similarity. Source: UniProtKB basolateral plasma membrane Inferred from direct assay PubMed 18505797. Source: MGI cell surface Inferred from electronic annotation. Source: Compara integral to 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 specific granule Inferred from electronic annotation. Source: Compara trans-Golgi network Inferred from direct assay Ref.10. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cenpf	Q155P7	9	EBI-645716,EBI-2211248

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 298

298

Syntaxin-4

PRO_0000210203

Regions

Topological domain

1 – 274

274

Cytoplasmic Potential

Transmembrane

275 – 295

21

Helical; Anchor for type IV membrane protein; Potential

Topological domain

296 – 298

3

Extracellular Potential

Domain

200 – 262

63

t-SNARE coiled-coil homology

Region

154 – 298

145

Interaction with CENPF

Coiled coil

38 – 163

126

Potential

Amino acid modifications

Modified residue

15

1

Phosphoserine Ref.9 Ref.12

Modified residue

29

1

Phosphoserine Ref.12

Modified residue

117

1

Phosphoserine Ref.13

Experimental info

Sequence conflict

47

1

T → I in AAH52023. Ref.3

Sequence conflict

141

1

C → Y in BAE36660. Ref.2

Sequence conflict

281

1

S → Y in BAE26743. Ref.2

Secondary structure

1

.

.

.

.

.

.

298

Helix Strand Turn

Details...

Helix

5 – 8

4

Helix

12 – 15

4

Turn

16 – 18

3

Sequences

	Sequence		Length	Mass (Da)
	P70452 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: FCD1477E1126CEC1	FASTA	298	34,165
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15, MASS SPECTROMETRY. 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 AND SER-29, MASS SPECTROMETRY. Tissue: Macrophage.
[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, MASS SPECTROMETRY. 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.

IPI

IPI00109335.

RefSeq

NP_033320.1. NM_009294.3.

UniGene

Mm.24867.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2PJX	X-ray	3.15	C/D	1-29	[»]
3PUJ	X-ray	3.31	C/D	1-10	[»]
3PUK	X-ray	3.05	C/D	1-10	[»]

ProteinModelPortal

P70452.

SMR

P70452. Positions 39-292.

ModBase

Search...

Protein-protein interaction databases

IntAct

P70452. 3 interactions.

MINT

MINT-269272.

PTM databases

PhosphoSite

P70452.

Proteomic databases

PaxDb

P70452.

PRIDE

P70452.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000033075; ENSMUSP00000033075; ENSMUSG00000030805.
ENSMUST00000121705; ENSMUSP00000112927; ENSMUSG00000030805.

GeneID

20909.

KEGG

mmu:20909.

UCSC

uc009jwy.1. mouse.

Organism-specific databases

CTD

20909.

MGI

MGI:893577. Stx4a.

Phylogenomic databases

eggNOG

COG5074.

GeneTree

ENSGT00550000074334.

HOGENOM

HOG000286023.

HOVERGEN

HBG000497.

InParanoid

Q3TSL5.

KO

K13502.

OMA

LMQSEYR.

OrthoDB

EOG4Z62PD.

Enzyme and pathway databases

Reactome

REACT_147847. Translocation of Glut4 to the Plasma Membrane.
REACT_88307. Membrane Trafficking.

Gene expression databases

ArrayExpress

P70452.

Bgee

P70452.

CleanEx

MM_STX4A.

Genevestigator

P70452.

GermOnline

ENSMUSG00000030805. Mus musculus.

Family and domain databases

InterPro

IPR006012. Syntaxin/epimorphin_CS.
IPR006011. Syntaxin_N.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]

Pfam

PF05739. SNARE. 1 hit.
PF00804. Syntaxin. 1 hit.
[Graphical view]

SMART

SM00503. SynN. 1 hit.
SM00397. t_SNARE. 1 hit.
[Graphical view]

SUPFAM

SSF47661. t-snare. 1 hit.

PROSITE

PS00914. SYNTAXIN. 1 hit.
PS50192. T_SNARE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P70452.

NextBio

299793.

SOURCE

Search...

Entry information

Entry name

STX4_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 111 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program