[1]	NUCLEOTIDE SEQUENCE [MRNA]. TISSUE=Adipocyte; Tellam J., Piper R.C., Smith C., James D.E.; Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]	IDENTIFICATION IN A COMPLEX WITH VAMP8 AND VTI1B. DOI=10.1016/j.devcel.2004.08.002; PubMed=15363411 [NCBI, ExPASy, EBI, Israel, Japan] Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.; "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells."; Dev. Cell 7:359-371(2004).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS SPECTROMETRY. TISSUE=Brain; DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan] Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; "Phosphoproteomic analysis of the developing mouse brain."; Mol. Cell. Proteomics 3:1093-1101(2004).
[4]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-79, AND MASS SPECTROMETRY. TISSUE=Brain cortex; DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan] Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."; Mol. Cell. Proteomics 6:283-293(2007).
[5]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-126 AND SER-129, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan] Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; "Large-scale phosphorylation analysis of mouse liver."; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-45; SER-129 AND SER-205, AND MASS SPECTROMETRY. TISSUE=Macrophage; DOI=10.1016/j.immuni.2008.11.006; PubMed=19144319 [NCBI, ExPASy, EBI, Israel, Japan] Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.; "The phagosomal proteome in interferon-gamma-activated macrophages."; Immunity 30:143-154(2009).
[7]	X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 169-229 IN COMPLEX WITH VAMP8; STX8 AND VTI1B. DOI=10.1038/nsb746; PubMed=11786915 [NCBI, ExPASy, EBI, Israel, Japan] Antonin W., Fasshauer D., Becker S., Jahn R., Schneider T.R.; "Crystal structure of the endosomal SNARE complex reveals common structural principles of all SNAREs."; Nat. Struct. Biol. 9:107-111(2002).

Comments

FUNCTION: May be involved in protein trafficking from the plasma membrane to the early endosome (EE) as well as in homotypic fusion of endocytic organelles. Mediates the endocytic trafficking from early endosomes to late endosomes and lysosomes (By similarity).
SUBUNIT: Part of the SNARE core complex containing VAMP8, STX8 and VTI1B. Found in a complex with VAMP8 and VTI1B in the liver. Forms a SNARE complex with VTI1B, STX8 and VAMP8 which functions in the homotypic fusion of late endosomes. Interacts with VPS11, VPS16, VPS18 and VPS33A (By similarity).
SUBCELLULAR LOCATION: Early endosome membrane; Single-pass type IV membrane protein (By similarity).
SIMILARITY: Belongs to the syntaxin family.
SIMILARITY: Contains 1 t-SNARE coiled-coil homology domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF056323; AAC15971.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00118217; -.

UniGene

Mm.248042

3D structure databases

PDB

1GL2; X-ray; 1.90 A; B=169-228.

[ExPASy / RCSB / EBI]

PDBsum

1GL2; -.

ModBase

O70439.

Protein-protein interaction databases

IntAct

O70439; 2.

PTM databases

PhosphoSite

O70439; -.

Organism-specific databases

MGI

MGI:1858210; Stx7.

Gene expression databases

O70439; -.

O70439; -.

MM_STX7; -.

ENSMUSG00000019998; Mus musculus.

Ontologies

GO:0031901;	Cellular component: early endosome membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005484;	Molecular function: SNAP receptor activity (inferred from electronic annotation from InterPro).
GO:0006886;	Biological process: intracellular protein transport (inferred from electronic annotation from InterPro).
GO:0016192;	Biological process: vesicle-mediated transport (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006012; Syntaxin/epimorphin_CS.
IPR006011; Syntaxin_N.
IPR000727; T_SNARE.
Graphical view of domain structure.

Pfam

PF05739; SNARE; 1.
PF00804; Syntaxin; 1.
Pfam graphical view of domain structure.

SMART

SM00503; SynN; 1.
SM00397; t_SNARE; 1.
SMART graphical view of domain structure.

PROSITE

PS00914; SYNTAXIN; 1.
PS50192; T_SNARE; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O70439; -.

Genome annotation databases

Ensembl

ENSMUSG00000019998; Mus musculus. [Contig view]

Phylogenomic databases

HOGENOM

O70439; -.

HOVERGEN

O70439; -.

Other

Stx7; Mus musculus.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Acetylation; Coiled coil; Endosome; Iron; Membrane; Phosphoprotein; Transmembrane.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 261`	`260`	`Syntaxin-7.`	`PRO_0000210214`
`TOPO_DOM`	`2 238`	`237`	`Cytoplasmic (Potential).`
`TRANSMEM`	`239 259`	`21`	`Anchor for type IV membrane protein (Potential).`
`TOPO_DOM`	`260 261`	`2`	`Vesicular (Potential).`
`DOMAIN`	`165 227`	`63`	`t-SNARE coiled-coil homology.`
`COILED`	`47 68`	`22`	`Potential.`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`MOD_RES`	`45 45`		`Phosphoserine.`
`MOD_RES`	`79 79`		`Phosphothreonine.`
`MOD_RES`	`125 125`		`Phosphoserine.`
`MOD_RES`	`126 126`		`Phosphoserine.`
`MOD_RES`	`129 129`		`Phosphoserine.`
`MOD_RES`	`205 205`		`Phosphoserine.`
`HELIX`	`170 226`	`57`

Sequence information

Length: 261 AA [This is the length of the unprocessed precursor]

Molecular weight: 29821 Da [This is the MW of the unprocessed precursor]

CRC64: 62F4E4B33F247ADB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSYTPGIGGD SAQLAQRISS NIQKITQCSV EIQRTLNQLG TPQDSPELRQ LLQQKQQYTN 

        70         80         90        100        110        120 
QLAKETDKYI KEFGSLPTTP SEQRQRKIQK DRLVAEFTTS LTNFQKAQRQ AAEREKEFVA 

       130        140        150        160        170        180 
RVRASSRVSG GFPEDSSKEK NLVSWESQTQ PQVQVQDEEI TEDDLRLIHE RESSIRQLEA 

       190        200        210        220        230        240 
DIMDINEIFK DLGMMIHEQG DMIDSIEANV ESAEVHVQQA NQQLSRAADY QRKSRKTLCI 

       250        260 
IIFILVVRIV IICLIVWGLK G

O70439 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools