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Protein

Syntaxin-8

Gene

Stx8

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

Functioni

Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.By similarity

GO - Molecular functioni

  1. chloride channel inhibitor activity Source: MGI
  2. SNAP receptor activity Source: GO_Central
  3. SNARE binding Source: MGI
  4. syntaxin binding Source: MGI
  5. ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

  1. early endosome to late endosome transport Source: MGI
  2. endosome to lysosome transport Source: Ensembl
  3. intracellular protein transport Source: GO_Central
  4. regulation of protein localization to plasma membrane Source: MGI
  5. vesicle fusion Source: GO_Central
Complete GO annotation...

Keywords - Biological processi

Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-8
Alternative name(s):
Syntaxin-like protein 3I35
Gene namesi
Name:Stx8
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1890156. Stx8.

Subcellular locationi

  1. Membrane By similarity; Single-pass type IV membrane protein By similarity

  2. Note: Preferentially associated with the early endosome. To lesser extends, also present in late endosome, the plasma membrane and coated pits (By similarity).By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 215215CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei216 – 23217Helical; Anchor for type IV membrane proteinSequence AnalysisAdd
BLAST
Topological domaini233 – 2364VesicularSequence Analysis

GO - Cellular componenti

  1. early endosome Source: MGI
  2. endosome Source: MGI
  3. integral component of membrane Source: GO_Central
  4. late endosome Source: MGI
  5. late endosome membrane Source: Ensembl
  6. lysosomal membrane Source: Ensembl
  7. perinuclear region of cytoplasm Source: MGI
  8. recycling endosome Source: MGI
  9. SNARE complex Source: GO_Central
  10. trans-Golgi network Source: MGI
  11. vesicle Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 236236Syntaxin-8PRO_0000210218Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601Phosphoserine1 Publication

Post-translational modificationi

Ubiquitinated by HECTD3.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO88983.
PaxDbiO88983.
PRIDEiO88983.

PTM databases

PhosphoSiteiO88983.

Expressioni

Gene expression databases

BgeeiO88983.
CleanExiMM_STX8.
ExpressionAtlasiO88983. baseline and differential.
GenevestigatoriO88983.

Interactioni

Subunit structurei

Forms a SNARE complex with STX7, VTI1B and VAMP8 which functions in the homotypic fusion of late endosomes. Part of the SNARE core complex containing STX7, VAMP8 and VTI1B. Interacts with VAMP8 (By similarity). Interacts with HECTD3.By similarity1 Publication

Protein-protein interaction databases

BioGridi207739. 5 interactions.

Structurei

3D structure databases

ProteinModelPortaliO88983.
SMRiO88983. Positions 152-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 20763t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili42 – 6524By similarityAdd
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

eggNOGiNOG259218.
GeneTreeiENSGT00390000007779.
HOGENOMiHOG000031515.
HOVERGENiHBG007572.
InParanoidiO88983.
KOiK08501.
OMAiNQYERNG.
OrthoDBiEOG7PS1GG.
PhylomeDBiO88983.
TreeFamiTF323262.

Family and domain databases

InterProiIPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O88983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPDPWFSTY DSTCQIAQEI AEKIQERNQC ERRGEKTPKL TLTIRTLLKN
60 70 80 90 100
LKVKIDLLKD LLLRAVSTRQ ITQLEGDRRQ NLLDDLVTRE RLLLASFKNE
110 120 130 140 150
GAEPDLIRSS LMSEEAKRGT PNPWLCEEPE ETRGLGFDEI RQQQQKIIQE
160 170 180 190 200
QDAGLDALSS IISRQKQMGQ EIGNELDEQN EIIDDLANLV ENTDEKLRTE
210 220 230
ARRVTLVDRK STSCGMIMVI LLLLVAIVVV AVWPTN
Length:236
Mass (Da):26,925
Last modified:November 1, 1998 - v1
Checksum:iEAE1D9D150C2EF2D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093064 mRNA. Translation: AAC64149.1.
AF036716 mRNA. Translation: AAC95286.1.
AB040054 mRNA. Translation: BAB20500.1.
AK003297 mRNA. Translation: BAB22698.1.
AL669842, AL663076 Genomic DNA. Translation: CAI24774.1.
BC048167 mRNA. Translation: AAH48167.1.
BC048479 mRNA. Translation: AAH48479.1.
CCDSiCCDS24863.1.
RefSeqiNP_061238.1. NM_018768.2.
UniGeneiMm.3973.

Genome annotation databases

EnsembliENSMUST00000021285; ENSMUSP00000021285; ENSMUSG00000020903.
GeneIDi55943.
KEGGimmu:55943.
UCSCiuc007jnj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF093064 mRNA. Translation: AAC64149.1.
AF036716 mRNA. Translation: AAC95286.1.
AB040054 mRNA. Translation: BAB20500.1.
AK003297 mRNA. Translation: BAB22698.1.
AL669842, AL663076 Genomic DNA. Translation: CAI24774.1.
BC048167 mRNA. Translation: AAH48167.1.
BC048479 mRNA. Translation: AAH48479.1.
CCDSiCCDS24863.1.
RefSeqiNP_061238.1. NM_018768.2.
UniGeneiMm.3973.

3D structure databases

ProteinModelPortaliO88983.
SMRiO88983. Positions 152-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207739. 5 interactions.

PTM databases

PhosphoSiteiO88983.

Proteomic databases

MaxQBiO88983.
PaxDbiO88983.
PRIDEiO88983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021285; ENSMUSP00000021285; ENSMUSG00000020903.
GeneIDi55943.
KEGGimmu:55943.
UCSCiuc007jnj.1. mouse.

Organism-specific databases

CTDi9482.
MGIiMGI:1890156. Stx8.

Phylogenomic databases

eggNOGiNOG259218.
GeneTreeiENSGT00390000007779.
HOGENOMiHOG000031515.
HOVERGENiHBG007572.
InParanoidiO88983.
KOiK08501.
OMAiNQYERNG.
OrthoDBiEOG7PS1GG.
PhylomeDBiO88983.
TreeFamiTF323262.

Miscellaneous databases

NextBioi311626.
PROiO88983.
SOURCEiSearch...

Gene expression databases

BgeeiO88983.
CleanExiMM_STX8.
ExpressionAtlasiO88983. baseline and differential.
GenevestigatoriO88983.

Family and domain databases

InterProiIPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 1 hit.
[Graphical view]
PROSITEiPS50192. T_SNARE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Thoreau V., Bilan F., Kitzis A., Chomel J.-C.
    Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Subramaniam V.N., Loh E., Hong W.
    Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Mouse syntaxin8."
    Nakamura N., Wada Y., Futai M.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H.
  4. "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: Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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.
    Tissue: Brain and Testis.
  7. "Interaction between syntaxin 8 and HECTd3, a HECT domain ligase."
    Zhang L., Kang L., Bond W., Zhang N.
    Cell. Mol. Neurobiol. 29:115-121(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HECTD3, UBIQUITINATION.
  8. "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-160, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSTX8_MOUSE
AccessioniPrimary (citable) accession number: O88983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: November 1, 1998
Last modified: February 4, 2015
This is version 108 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.