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Protein

Syntaxin-17

Gene

Stx17

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

Functioni

SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane. May also play a role in the early secretory pathway where it may maintain the architecture of the endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi and/or regulate transport between the endoplasmic reticulum, the ERGIC and the Golgi (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Autophagy, ER-Golgi transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Syntaxin-171 Publication
Gene namesi
Name:Stx17Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1914977. Stx17.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini2 – 227226CytoplasmicSequence analysisAdd
BLAST
Transmembranei228 – 24821HelicalSequence analysisAdd
BLAST
Topological domaini249 – 2535LumenalSequence analysis
Transmembranei254 – 27421HelicalSequence analysisAdd
BLAST
Topological domaini275 – 30127CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 301300Syntaxin-17PRO_0000210229Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei41 – 411N6-acetyllysineBy similarity
Modified residuei156 – 1561Phosphotyrosine; by ABL1By similarity
Modified residuei288 – 2881PhosphoserineCombined sources

Post-translational modificationi

Dephosphorylation by PTPN2; regulates exit from the endoplasmic reticulum (By similarity). Phosphorylated at Tyr-156 probably by ABL1 (PubMed:23006999).By similarity1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9D0I4.
MaxQBiQ9D0I4.
PaxDbiQ9D0I4.
PRIDEiQ9D0I4.

PTM databases

iPTMnetiQ9D0I4.
PhosphoSiteiQ9D0I4.

Expressioni

Gene expression databases

BgeeiQ9D0I4.
CleanExiMM_STX17.
ExpressionAtlasiQ9D0I4. baseline and differential.
GenevisibleiQ9D0I4. MM.

Interactioni

Subunit structurei

Forms a SNARE complex composed of VAMP8, SNAP29 and STX17 involved in fusion of autophagosome with lysosome (By similarity). May interact with VTI1B (By similarity). Probably interacts with BET1, SCFD1 and SEC22B (By similarity). Interacts with PTPN2 and ABL1; involved in STX17 phosphorylation (By similarity). Interacts with COPB1 (By similarity). Interacts with TMED9 and TMED10; the interaction is direct (By similarity). Interact with VAMP7 (PubMed:23217709).By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ9D0I4. 2 interactions.
STRINGi10090.ENSMUSP00000068087.

Structurei

3D structure databases

ProteinModelPortaliQ9D0I4.
SMRiQ9D0I4. Positions 169-226.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini161 – 22363t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni228 – 27447Necessary and sufficient for localization to autophagosomeBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili49 – 12880Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi298 – 3014Endoplasmic reticulum retention signalSequence analysis

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

eggNOGiKOG0811. Eukaryota.
COG5325. LUCA.
GeneTreeiENSGT00390000013283.
HOGENOMiHOG000006905.
HOVERGENiHBG055257.
InParanoidiQ9D0I4.
KOiK08491.
OMAiANMREME.
PhylomeDBiQ9D0I4.
TreeFamiTF323947.

Family and domain databases

InterProiIPR028676. STX17.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF139. PTHR19957:SF139. 1 hit.
SMARTiSM00397. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9D0I4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSEDEEKVKL RRLEPAIQKF TKIVIPTDLE RLRKHQINIE KYQRCRIWDK
60 70 80 90 100
LHEEHINAGR TVQQLRSNIR EMEKLCLKVH KDDLVLLKRM IDPVKEAAAT
110 120 130 140 150
ATAEFLQLHL ESVEELKKQV NDEELLQPSL TRSTTVDGVL HTGEAEAASQ
160 170 180 190 200
SLTQIYALPE IPQDQNAAES WETLEADLIE LSHLVTDMSL LVSSQQEKID
210 220 230 240 250
SIADHVNSAA VNVEEGTKNL QKAAKYKLAA LPVAGALIGG VVGGPIGLLA
260 270 280 290 300
GFKVAGIAAA LGGGVLGFTG GKLIQRRKQK MMEKLTSSCP DLPSQSDKKR

S
Length:301
Mass (Da):33,221
Last modified:June 1, 2001 - v1
Checksum:i3715C8D747FF7FF6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti294 – 2941S → G in BAB31255 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011400 mRNA. Translation: BAB27592.1.
AK018526 mRNA. Translation: BAB31255.1.
AK034718 mRNA. Translation: BAC28806.1.
AK154503 mRNA. Translation: BAE32634.1.
AL683893 Genomic DNA. Translation: CAM14010.1.
BC028639 mRNA. Translation: AAH28639.1.
CCDSiCCDS18164.1.
RefSeqiNP_080619.2. NM_026343.2.
XP_006538271.1. XM_006538208.1.
UniGeneiMm.171334.

Genome annotation databases

EnsembliENSMUST00000064765; ENSMUSP00000068087; ENSMUSG00000061455.
ENSMUST00000107720; ENSMUSP00000103348; ENSMUSG00000061455.
GeneIDi67727.
KEGGimmu:67727.
UCSCiuc008sux.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK011400 mRNA. Translation: BAB27592.1.
AK018526 mRNA. Translation: BAB31255.1.
AK034718 mRNA. Translation: BAC28806.1.
AK154503 mRNA. Translation: BAE32634.1.
AL683893 Genomic DNA. Translation: CAM14010.1.
BC028639 mRNA. Translation: AAH28639.1.
CCDSiCCDS18164.1.
RefSeqiNP_080619.2. NM_026343.2.
XP_006538271.1. XM_006538208.1.
UniGeneiMm.171334.

3D structure databases

ProteinModelPortaliQ9D0I4.
SMRiQ9D0I4. Positions 169-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D0I4. 2 interactions.
STRINGi10090.ENSMUSP00000068087.

PTM databases

iPTMnetiQ9D0I4.
PhosphoSiteiQ9D0I4.

Proteomic databases

EPDiQ9D0I4.
MaxQBiQ9D0I4.
PaxDbiQ9D0I4.
PRIDEiQ9D0I4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000064765; ENSMUSP00000068087; ENSMUSG00000061455.
ENSMUST00000107720; ENSMUSP00000103348; ENSMUSG00000061455.
GeneIDi67727.
KEGGimmu:67727.
UCSCiuc008sux.1. mouse.

Organism-specific databases

CTDi55014.
MGIiMGI:1914977. Stx17.

Phylogenomic databases

eggNOGiKOG0811. Eukaryota.
COG5325. LUCA.
GeneTreeiENSGT00390000013283.
HOGENOMiHOG000006905.
HOVERGENiHBG055257.
InParanoidiQ9D0I4.
KOiK08491.
OMAiANMREME.
PhylomeDBiQ9D0I4.
TreeFamiTF323947.

Miscellaneous databases

PROiQ9D0I4.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D0I4.
CleanExiMM_STX17.
ExpressionAtlasiQ9D0I4. baseline and differential.
GenevisibleiQ9D0I4. MM.

Family and domain databases

InterProiIPR028676. STX17.
IPR006012. Syntaxin/epimorphin_CS.
IPR010989. t-SNARE.
IPR000727. T_SNARE_dom.
[Graphical view]
PANTHERiPTHR19957:SF139. PTHR19957:SF139. 1 hit.
SMARTiSM00397. 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. "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 and NOD.
    Tissue: Colon.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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/6J.
    Tissue: Thymus.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  5. "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway."
    Muppirala M., Gupta V., Swarup G.
    Biochim. Biophys. Acta 1823:2109-2119(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY ABL1.
  6. "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."
    Itakura E., Kishi-Itakura C., Mizushima N.
    Cell 151:1256-1269(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VAMP7.

Entry informationi

Entry nameiSTX17_MOUSE
AccessioniPrimary (citable) accession number: Q9D0I4
Secondary accession number(s): B1AVI3, Q9D330
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 109 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

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 one 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.