STX17_MOUSE
ID STX17_MOUSE Reviewed; 301 AA.
AC Q9D0I4; B1AVI3; Q9D330;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Syntaxin-17 {ECO:0000303|PubMed:23006999};
GN Name=Stx17 {ECO:0000312|MGI:MGI:1914977};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Colon;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP PHOSPHORYLATION BY ABL1.
RX PubMed=23006999; DOI=10.1016/j.bbamcr.2012.09.003;
RA Muppirala M., Gupta V., Swarup G.;
RT "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for
RT membrane trafficking in the early secretory pathway.";
RL Biochim. Biophys. Acta 1823:2109-2119(2012).
RN [6]
RP INTERACTION WITH VAMP7.
RX PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
RA Itakura E., Kishi-Itakura C., Mizushima N.;
RT "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes
RT for fusion with endosomes/lysosomes.";
RL Cell 151:1256-1269(2012).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=27628032; DOI=10.1242/bio.018648;
RA Hubert V., Peschel A., Langer B., Groeger M., Rees A., Kain R.;
RT "LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and
RT for their fusion with lysosomes.";
RL Biol. Open 5:1516-1529(2016).
CC -!- FUNCTION: SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment
CC protein receptors, are essential proteins for fusion of cellular
CC membranes. SNAREs localized on opposing membranes assemble to form a
CC trans-SNARE complex, an extended, parallel four alpha-helical bundle
CC that drives membrane fusion. STX17 is a SNARE of the autophagosome
CC involved in autophagy through the direct control of autophagosome
CC membrane fusion with the lysosome membrane. May also play a role in the
CC early secretory pathway where it may maintain the architecture of the
CC endoplasmic reticulum-Golgi intermediate compartment/ERGIC and Golgi
CC and/or regulate transport between the endoplasmic reticulum, the ERGIC
CC and the Golgi (By similarity). {ECO:0000250|UniProtKB:P56962}.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome (By similarity). May
CC interact with VTI1B (By similarity). Probably interacts with BET1,
CC SCFD1 and SEC22B (By similarity). Interacts with PTPN2 and ABL1;
CC involved in STX17 phosphorylation (By similarity). Interacts with COPB1
CC (By similarity). Interacts with TMED9 and TMED10; the interaction is
CC direct (By similarity). Interacts with VAMP7 (PubMed:23217709).
CC Interacts with RUBCNL/PACER; promoting targeting of RUBCNL/PACER to
CC autophagosome (By similarity). Interacts with VAMP8, SNAP29, VPS39 and
CC VPS41; these interactions are increased in the absence of TMEM39A (By
CC similarity). {ECO:0000250|UniProtKB:P56962,
CC ECO:0000250|UniProtKB:Q9Z158, ECO:0000269|PubMed:23217709}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein
CC {ECO:0000255}. Smooth endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:27628032}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane
CC {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z158}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into
CC membranes. Localizes to the completed autophagosome membrane upon cell
CC starvation (By similarity). {ECO:0000250|UniProtKB:P56962}.
CC -!- PTM: Dephosphorylation by PTPN2; regulates exit from the endoplasmic
CC reticulum (By similarity). Phosphorylated at Tyr-156 probably by ABL1
CC (PubMed:23006999). {ECO:0000250|UniProtKB:Q9Z158,
CC ECO:0000269|PubMed:23006999}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AK011400; BAB27592.1; -; mRNA.
DR EMBL; AK018526; BAB31255.1; -; mRNA.
DR EMBL; AK034718; BAC28806.1; -; mRNA.
DR EMBL; AK154503; BAE32634.1; -; mRNA.
DR EMBL; AL683893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028639; AAH28639.1; -; mRNA.
DR CCDS; CCDS18164.1; -.
DR RefSeq; NP_080619.2; NM_026343.2.
DR RefSeq; XP_006538271.1; XM_006538208.1.
DR AlphaFoldDB; Q9D0I4; -.
DR SMR; Q9D0I4; -.
DR BioGRID; 212398; 4.
DR IntAct; Q9D0I4; 3.
DR MINT; Q9D0I4; -.
DR STRING; 10090.ENSMUSP00000103348; -.
DR iPTMnet; Q9D0I4; -.
DR PhosphoSitePlus; Q9D0I4; -.
DR EPD; Q9D0I4; -.
DR jPOST; Q9D0I4; -.
DR MaxQB; Q9D0I4; -.
DR PaxDb; Q9D0I4; -.
DR PeptideAtlas; Q9D0I4; -.
DR PRIDE; Q9D0I4; -.
DR ProteomicsDB; 254765; -.
DR Antibodypedia; 752; 151 antibodies from 25 providers.
DR DNASU; 67727; -.
DR Ensembl; ENSMUST00000064765; ENSMUSP00000068087; ENSMUSG00000061455.
DR Ensembl; ENSMUST00000107720; ENSMUSP00000103348; ENSMUSG00000061455.
DR GeneID; 67727; -.
DR KEGG; mmu:67727; -.
DR UCSC; uc008sux.1; mouse.
DR CTD; 55014; -.
DR MGI; MGI:1914977; Stx17.
DR VEuPathDB; HostDB:ENSMUSG00000061455; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_058244_1_0_1; -.
DR InParanoid; Q9D0I4; -.
DR OMA; YPVMGAL; -.
DR OrthoDB; 1493840at2759; -.
DR PhylomeDB; Q9D0I4; -.
DR TreeFam; TF323947; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR BioGRID-ORCS; 67727; 5 hits in 71 CRISPR screens.
DR ChiTaRS; Stx17; mouse.
DR PRO; PR:Q9D0I4; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9D0I4; protein.
DR Bgee; ENSMUSG00000061455; Expressed in parotid gland and 250 other tissues.
DR ExpressionAtlas; Q9D0I4; baseline and differential.
DR Genevisible; Q9D0I4; MM.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0030134; C:COPII-coated ER to Golgi transport vesicle; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; ISS:UniProtKB.
DR GO; GO:0033116; C:endoplasmic reticulum-Golgi intermediate compartment membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0012507; C:ER to Golgi transport vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030868; C:smooth endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0005484; F:SNAP receptor activity; ISS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:MGI.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; ISS:UniProtKB.
DR GO; GO:0097111; P:endoplasmic reticulum-Golgi intermediate compartment organization; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISO:MGI.
DR GO; GO:0048278; P:vesicle docking; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR010989; SNARE.
DR InterPro; IPR028676; STX17.
DR InterPro; IPR045242; Syntaxin.
DR InterPro; IPR006012; Syntaxin/epimorphin_CS.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19957; PTHR19957; 1.
DR PANTHER; PTHR19957:SF139; PTHR19957:SF139; 1.
DR SMART; SM00397; t_SNARE; 1.
DR SUPFAM; SSF47661; SSF47661; 1.
DR PROSITE; PS00914; SYNTAXIN; 1.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Endoplasmic reticulum; ER-Golgi transport; Membrane; Mitochondrion;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P56962"
FT CHAIN 2..301
FT /note="Syntaxin-17"
FT /id="PRO_0000210229"
FT TOPO_DOM 2..227
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..253
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..274
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 275..301
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 161..223
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 228..274
FT /note="Necessary and sufficient for localization to
FT autophagosome"
FT /evidence="ECO:0000250|UniProtKB:P56962"
FT COILED 49..128
FT /evidence="ECO:0000255"
FT MOTIF 298..301
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P56962"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56962"
FT MOD_RES 156
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z158"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 294
FT /note="S -> G (in Ref. 1; BAB31255)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 33221 MW; 3715C8D747FF7FF6 CRC64;
MSEDEEKVKL RRLEPAIQKF TKIVIPTDLE RLRKHQINIE KYQRCRIWDK LHEEHINAGR
TVQQLRSNIR EMEKLCLKVH KDDLVLLKRM IDPVKEAAAT ATAEFLQLHL ESVEELKKQV
NDEELLQPSL TRSTTVDGVL HTGEAEAASQ SLTQIYALPE IPQDQNAAES WETLEADLIE
LSHLVTDMSL LVSSQQEKID SIADHVNSAA VNVEEGTKNL QKAAKYKLAA LPVAGALIGG
VVGGPIGLLA GFKVAGIAAA LGGGVLGFTG GKLIQRRKQK MMEKLTSSCP DLPSQSDKKR
S
