STX17_BOVIN
ID STX17_BOVIN Reviewed; 302 AA.
AC Q5E9Y2;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Syntaxin-17 {ECO:0000250|UniProtKB:P56962};
GN Name=STX17 {ECO:0000250|UniProtKB:P56962};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal skin;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). Interacts
CC with RUBCNL/PACER; promoting targeting of RUBCNL/PACER to autophagosome
CC (By similarity). Interacts with VAMP8, SNAP29, VPS39 and VPS41; these
CC interactions are increased in the absence of TMEM39A (By similarity).
CC {ECO:0000250|UniProtKB:P56962, ECO:0000250|UniProtKB:Q9Z158}.
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:0000250|UniProtKB:P56962}; 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. {ECO:0000250|UniProtKB:P56962}.
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 -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; BT020788; AAX08805.1; -; mRNA.
DR EMBL; BC123853; AAI23854.1; -; mRNA.
DR RefSeq; NP_001029778.1; NM_001034606.1.
DR RefSeq; XP_005210267.1; XM_005210210.3.
DR RefSeq; XP_005210268.1; XM_005210211.3.
DR RefSeq; XP_005210269.1; XM_005210212.3.
DR AlphaFoldDB; Q5E9Y2; -.
DR SMR; Q5E9Y2; -.
DR STRING; 9913.ENSBTAP00000010541; -.
DR PaxDb; Q5E9Y2; -.
DR PRIDE; Q5E9Y2; -.
DR Ensembl; ENSBTAT00000010541; ENSBTAP00000010541; ENSBTAG00000008016.
DR GeneID; 534304; -.
DR KEGG; bta:534304; -.
DR CTD; 55014; -.
DR VEuPathDB; HostDB:ENSBTAG00000008016; -.
DR VGNC; VGNC:35433; STX17.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_058244_1_0_1; -.
DR InParanoid; Q5E9Y2; -.
DR OMA; YPVMGAL; -.
DR OrthoDB; 1493840at2759; -.
DR TreeFam; TF323947; -.
DR Reactome; R-BTA-204005; COPII-mediated vesicle transport.
DR Proteomes; UP000009136; Chromosome 8.
DR Bgee; ENSBTAG00000008016; Expressed in oocyte and 106 other tissues.
DR GO; GO:0005776; C:autophagosome; ISS: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: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; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0044233; C:mitochondria-associated endoplasmic reticulum membrane; IEA:Ensembl.
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:0019903; F:protein phosphatase binding; IEA:Ensembl.
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; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript 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..302
FT /note="Syntaxin-17"
FT /id="PRO_0000282600"
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:0000250|UniProtKB:P56962"
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:0000250|UniProtKB:P56962"
FT MOD_RES 41
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P56962"
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:0000250|UniProtKB:P56962"
SQ SEQUENCE 302 AA; 33559 MW; 10B11C865A691136 CRC64;
MSEDEEKVKL RRLEPAIQKF TKIVIPTDLE RLRKHQINIE KYQRCRVWDK LHEEHINAGR
TVQQLRSNIR EMEKLCLKVR KDDLGLLKRM IDPVKEEASA ATAEFLQLHL ESVEELKKQF
NDEETFLQPS LTRSMTVGGT FHSTEDEADP QSMTQIYALP EIPRDQNAAE SWETLEADLI
ELSQLVTDFS LLVNSQQEKI DSIEDHVNTA AVNVEEGTKN LGKAAKYKLA ALPVAGALIG
GVVGGPIGLL AGFKVAGIAA ALGGGVLGFT GGKLIQRRKQ KMMEKLASSC PDLPSQTDKK
CS
