STX17_HUMAN
ID STX17_HUMAN Reviewed; 302 AA.
AC P56962; Q4VXC2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 2.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Syntaxin-17 {ECO:0000303|PubMed:21545355};
GN Name=STX17 {ECO:0000303|PubMed:21545355, ECO:0000312|HGNC:HGNC:11432};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-41, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP FUNCTION, AND INTERACTION WITH TMED9 AND TMED10.
RX PubMed=21545355; DOI=10.1042/bc20110006;
RA Muppirala M., Gupta V., Swarup G.;
RT "Syntaxin 17 cycles between the ER and ERGIC and is required to maintain
RT the architecture of ERGIC and Golgi.";
RL Biol. Cell 103:333-350(2011).
RN [9]
RP INTERACTION WITH ABL1 AND PTPN2, AND SUBCELLULAR LOCATION.
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 [10]
RP FUNCTION IN AUTOPHAGY, SUBCELLULAR LOCATION, TOPOLOGY, INTERACTION WITH
RP SNAP29; VAMP7; VAMP8 AND VTI1B, AND MUTAGENESIS OF GLY-244; GLY-248;
RP GLY-264; GLY-268 AND 299-LYS-LYS-300.
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=26416964; DOI=10.1083/jcb.201501059;
RA Terawaki S., Camosseto V., Prete F., Wenger T., Papadopoulos A.,
RA Rondeau C., Combes A., Rodriguez Rodrigues C., Vu Manh T.P., Fallet M.,
RA English L., Santamaria R., Soares A.R., Weil T., Hammad H., Desjardins M.,
RA Gorvel J.P., Santos M.A., Gatti E., Pierre P.;
RT "RUN and FYVE domain-containing protein 4 enhances autophagy and lysosome
RT tethering in response to Interleukin-4.";
RL J. Cell Biol. 210:1133-1152(2015).
RN [15]
RP FUNCTION, INTERACTION WITH RUBCNL/PACER, AND SUBCELLULAR LOCATION.
RX PubMed=28306502; DOI=10.1016/j.molcel.2017.02.010;
RA Cheng X., Ma X., Ding X., Li L., Jiang X., Shen Z., Chen S., Liu W.,
RA Gong W., Sun Q.;
RT "Pacer mediates the function of class III PI3K and HOPS complexes in
RT autophagosome maturation by engaging Stx17.";
RL Mol. Cell 65:1029-1043(2017).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE (MICROBIAL
RP INFECTION).
RX PubMed=28504273; DOI=10.1038/ncomms15406;
RA Arasaki K., Mikami Y., Shames S.R., Inoue H., Wakana Y., Tagaya M.;
RT "Legionella effector Lpg1137 shuts down ER-mitochondria communication
RT through cleavage of syntaxin 17.";
RL Nat. Commun. 8:15406-15406(2017).
RN [17]
RP INTERACTION WITH VPS39; VPS41; VAMP8 AND SNAP29.
RX PubMed=31806350; DOI=10.1016/j.molcel.2019.10.035;
RA Miao G., Zhang Y., Chen D., Zhang H.;
RT "The ER-Localized Transmembrane Protein TMEM39A/SUSR2 Regulates Autophagy
RT by Controlling the Trafficking of the PtdIns(4)P Phosphatase SAC1.";
RL Mol. Cell 0:0-0(2019).
RN [18]
RP INTERACTION WITH RUBCNL/PACER.
RX PubMed=30704899; DOI=10.1016/j.molcel.2018.12.017;
RA Cheng X., Ma X., Zhu Q., Song D., Ding X., Li L., Jiang X., Wang X.,
RA Tian R., Su H., Shen Z., Chen S., Liu T., Gong W., Liu W., Sun Q.;
RT "Pacer is a mediator of mTORC1 and GSK3-TIP60 signaling in regulation of
RT autophagosome maturation and lipid metabolism.";
RL Mol. Cell 73:1-15(2019).
RN [19]
RP INTERACTION WITH VAMP8; SNAP29 AND VPS41.
RX PubMed=33422265; DOI=10.1016/j.devcel.2020.12.010;
RA Miao G., Zhao H., Li Y., Ji M., Chen Y., Shi Y., Bi Y., Wang P., Zhang H.;
RT "ORF3a of the COVID-19 virus SARS-CoV-2 blocks HOPS complex-mediated
RT assembly of the SNARE complex required for autolysosome formation.";
RL Dev. Cell 56:427-442(2020).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 170-227 IN COMPLEX WITH SNAP29 AND
RP VAMP8, INTERACTION WITH ATG14, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25686604; DOI=10.1038/nature14147;
RA Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M.,
RA Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.;
RT "ATG14 promotes membrane tethering and fusion of autophagosomes to
RT endolysosomes.";
RL Nature 520:563-566(2015).
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 (PubMed:23217709, PubMed:25686604,
CC PubMed:28306502). STX17 is a SNARE of the autophagosome involved in
CC autophagy through the direct control of autophagosome membrane fusion
CC with the lysosome membrane (PubMed:23217709, PubMed:25686604,
CC PubMed:28306502, PubMed:28504273). May also play a role in the early
CC 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 (PubMed:21545355). {ECO:0000269|PubMed:21545355,
CC ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604,
CC ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:28504273}.
CC -!- SUBUNIT: Forms a SNARE complex composed of VAMP8, SNAP29 and STX17
CC involved in fusion of autophagosome with lysosome (PubMed:23217709,
CC PubMed:25686604). Interacts with VAMP7 and VTI1B (PubMed:23217709).
CC Probably interacts with BET1, SCFD1 and SEC22B (By similarity).
CC Interacts with PTPN2 and ABL1; involved in STX17 phosphorylation
CC (PubMed:23006999). Interacts with COPB1 (By similarity). Interacts with
CC TMED9 and TMED10; the interaction is direct (PubMed:21545355).
CC Interacts with ATG14 (PubMed:25686604). Interacts with RUBCNL/PACER;
CC promoting targeting of RUBCNL/PACER to autophagosome (PubMed:28306502,
CC PubMed:30704899). Interacts with VAMP8, SNAP29, VPS39 and VPS41; these
CC interactions are increased in the absence of TMEM39A (PubMed:31806350,
CC PubMed:33422265). {ECO:0000250|UniProtKB:Q9Z158,
CC ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:23006999,
CC ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604,
CC ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:30704899,
CC ECO:0000269|PubMed:31806350, ECO:0000269|PubMed:33422265}.
CC -!- SUBUNIT: (Microbial infection) The interactions with VAMP8, SNAP29 and
CC VPS41 are decreased in presence of SARS coronavirus-2/SARS-CoV-2 ORF3A
CC protein. {ECO:0000269|PubMed:33422265}.
CC -!- INTERACTION:
CC P56962; O95573: ACSL3; NbExp=5; IntAct=EBI-2797775, EBI-1190822;
CC P56962; O95721: SNAP29; NbExp=10; IntAct=EBI-2797775, EBI-490676;
CC P56962; Q9BV40: VAMP8; NbExp=11; IntAct=EBI-2797775, EBI-727028;
CC P56962; Q9H269: VPS16; NbExp=3; IntAct=EBI-2797775, EBI-2655929;
CC P56962; Q96AX1: VPS33A; NbExp=4; IntAct=EBI-2797775, EBI-2527283;
CC P56962; Q96JC1: VPS39; NbExp=2; IntAct=EBI-2797775, EBI-1050197;
CC P56962; P49754: VPS41; NbExp=2; IntAct=EBI-2797775, EBI-2130459;
CC P56962; P70280: Vamp7; Xeno; NbExp=2; IntAct=EBI-2797775, EBI-6555653;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:23006999}; 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:0000269|PubMed:23006999}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604,
CC ECO:0000269|PubMed:26416964, ECO:0000269|PubMed:28306502}; Multi-pass
CC membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated
CC vesicle membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Z158}. Mitochondrion membrane
CC {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:28504273}; 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 (PubMed:23217709). {ECO:0000269|PubMed:23217709}.
CC -!- PTM: Phosphorylated at Tyr-157 probably by ABL1. Dephosphorylation by
CC PTPN2; regulates exit from the endoplasmic reticulum (By similarity).
CC {ECO:0000250|UniProtKB:Q9Z158}.
CC -!- PTM: (Microbial infection) Cleaved by the L.pneumophila serine protease
CC Lpg1137, impairing endoplasmic reticulum-mitochondria communication,
CC leading to inhibit autophagy. {ECO:0000269|PubMed:28504273}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AK000658; BAA91311.1; -; mRNA.
DR EMBL; AL358937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471105; EAW58920.1; -; Genomic_DNA.
DR EMBL; BC101564; AAI01565.1; -; mRNA.
DR EMBL; BC101566; AAI01567.1; -; mRNA.
DR CCDS; CCDS6745.1; -.
DR RefSeq; NP_060389.2; NM_017919.2.
DR RefSeq; XP_011517122.1; XM_011518820.2.
DR RefSeq; XP_011517123.1; XM_011518821.2.
DR PDB; 4WY4; X-ray; 1.40 A; B=170-227.
DR PDB; 7BV4; X-ray; 2.00 A; C/D/F/H=167-188.
DR PDB; 7BV6; X-ray; 3.05 A; B/F/J/N/R/V=142-228.
DR PDBsum; 4WY4; -.
DR PDBsum; 7BV4; -.
DR PDBsum; 7BV6; -.
DR AlphaFoldDB; P56962; -.
DR SMR; P56962; -.
DR BioGRID; 120346; 273.
DR DIP; DIP-47297N; -.
DR IntAct; P56962; 40.
DR MINT; P56962; -.
DR STRING; 9606.ENSP00000259400; -.
DR TCDB; 8.A.91.1.11; the syntaxin (syntaxin) family.
DR GlyGen; P56962; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P56962; -.
DR PhosphoSitePlus; P56962; -.
DR BioMuta; STX17; -.
DR DMDM; 212286190; -.
DR EPD; P56962; -.
DR jPOST; P56962; -.
DR MassIVE; P56962; -.
DR MaxQB; P56962; -.
DR PaxDb; P56962; -.
DR PeptideAtlas; P56962; -.
DR PRIDE; P56962; -.
DR ProteomicsDB; 56962; -.
DR Antibodypedia; 752; 151 antibodies from 25 providers.
DR DNASU; 55014; -.
DR Ensembl; ENST00000259400.11; ENSP00000259400.6; ENSG00000136874.11.
DR Ensembl; ENST00000525640.5; ENSP00000435981.1; ENSG00000136874.11.
DR Ensembl; ENST00000534052.1; ENSP00000433484.1; ENSG00000136874.11.
DR GeneID; 55014; -.
DR KEGG; hsa:55014; -.
DR MANE-Select; ENST00000259400.11; ENSP00000259400.6; NM_017919.3; NP_060389.2.
DR UCSC; uc004bal.5; human.
DR CTD; 55014; -.
DR DisGeNET; 55014; -.
DR GeneCards; STX17; -.
DR HGNC; HGNC:11432; STX17.
DR HPA; ENSG00000136874; Low tissue specificity.
DR MIM; 604204; gene.
DR neXtProt; NX_P56962; -.
DR OpenTargets; ENSG00000136874; -.
DR PharmGKB; PA36232; -.
DR VEuPathDB; HostDB:ENSG00000136874; -.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_058244_1_0_1; -.
DR InParanoid; P56962; -.
DR OMA; YPVMGAL; -.
DR OrthoDB; 1493840at2759; -.
DR PhylomeDB; P56962; -.
DR TreeFam; TF323947; -.
DR PathwayCommons; P56962; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR SignaLink; P56962; -.
DR BioGRID-ORCS; 55014; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; STX17; human.
DR GenomeRNAi; 55014; -.
DR Pharos; P56962; Tbio.
DR PRO; PR:P56962; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P56962; protein.
DR Bgee; ENSG00000136874; Expressed in nipple and 189 other tissues.
DR ExpressionAtlas; P56962; baseline and differential.
DR Genevisible; P56962; HS.
DR GO; GO:0005776; C:autophagosome; IDA:GO_Central.
DR GO; GO:0000421; C:autophagosome membrane; IDA: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:0005789; C:endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IDA: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:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; IDA: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; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IMP:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IDA:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:UniProtKB.
DR GO; GO:0097111; P:endoplasmic reticulum-Golgi intermediate compartment organization; IMP:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IDA: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 3D-structure; Acetylation; Autophagy; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Endoplasmic reticulum; ER-Golgi transport;
KW Host-virus interaction; Membrane; Mitochondrion; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..302
FT /note="Syntaxin-17"
FT /id="PRO_0000210228"
FT TOPO_DOM 2..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..254
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 276..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 162..224
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 229..275
FT /note="Necessary and sufficient for localization to
FT autophagosome"
FT /evidence="ECO:0000269|PubMed:23217709"
FT COILED 53..123
FT /evidence="ECO:0000255"
FT MOTIF 299..302
FT /note="Endoplasmic reticulum retention signal"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 157
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:Q9Z158"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MUTAGEN 244
FT /note="G->L: Alters localization to the autophagosome; when
FT associated with Leu-248."
FT /evidence="ECO:0000269|PubMed:23217709"
FT MUTAGEN 248
FT /note="G->L: Alters localization to the autophagosome; when
FT associated with Leu-244."
FT /evidence="ECO:0000269|PubMed:23217709"
FT MUTAGEN 264
FT /note="G->L: Alters localization to the autophagosome; when
FT associated with Leu-268."
FT /evidence="ECO:0000269|PubMed:23217709"
FT MUTAGEN 268
FT /note="G->L: Alters localization to the autophagosome; when
FT associated with Leu-264."
FT /evidence="ECO:0000269|PubMed:23217709"
FT MUTAGEN 299..300
FT /note="KK->AA: Localizes to the Golgi instead of the
FT endoplasmic reticulum."
FT /evidence="ECO:0000269|PubMed:23217709"
FT CONFLICT 28
FT /note="D -> N (in Ref. 1; BAA91311)"
FT /evidence="ECO:0000305"
FT CONFLICT 172
FT /note="W -> R (in Ref. 1; BAA91311)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="G -> C (in Ref. 1; BAA91311)"
FT /evidence="ECO:0000305"
FT HELIX 173..195
FT /evidence="ECO:0007829|PDB:4WY4"
FT HELIX 197..226
FT /evidence="ECO:0007829|PDB:4WY4"
SQ SEQUENCE 302 AA; 33403 MW; 51AD5427EFBAC541 CRC64;
MSEDEEKVKL RRLEPAIQKF IKIVIPTDLE RLRKHQINIE KYQRCRIWDK LHEEHINAGR
TVQQLRSNIR EIEKLCLKVR KDDLVLLKRM IDPVKEEASA ATAEFLQLHL ESVEELKKQF
NDEETLLQPP LTRSMTVGGA FHTTEAEASS QSLTQIYALP EIPQDQNAAE SWETLEADLI
ELSQLVTDFS LLVNSQQEKI DSIADHVNSA AVNVEEGTKN LGKAAKYKLA ALPVAGALIG
GMVGGPIGLL AGFKVAGIAA ALGGGVLGFT GGKLIQRKKQ KMMEKLTSSC PDLPSQTDKK
CS
