STX17_RAT
ID STX17_RAT Reviewed; 301 AA.
AC Q9Z158;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Syntaxin-17 {ECO:0000303|PubMed:10930465};
GN Name=Stx17 {ECO:0000250|UniProtKB:P56962};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
RA Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
RA Scheller R.H.;
RT "Three novel proteins of the syntaxin/SNAP-25 family.";
RL J. Biol. Chem. 273:34171-34179(1998).
RN [2]
RP SUBCELLULAR LOCATION, INTERACTION WITH BET1; SCFD1 AND SEC22B, AND TISSUE
RP SPECIFICITY.
RX PubMed=10930465; DOI=10.1091/mbc.11.8.2719;
RA Steegmaier M., Oorschot V., Klumperman J., Scheller R.H.;
RT "Syntaxin 17 is abundant in steroidogenic cells and implicated in smooth
RT endoplasmic reticulum membrane dynamics.";
RL Mol. Biol. Cell 11:2719-2731(2000).
RN [3]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-156, AND INTERACTION WITH COPB1;
RP 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 [4]
RP INTERACTION WITH ABL1, PHOSPHORYLATION AT TYR-156 BY ABL1,
RP DEPHOSPHORYLATION BY PTPN2, AND MUTAGENESIS OF TYR-156.
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).
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 VAMP7 (By similarity). May interact with VTI1B (By
CC similarity). Probably interacts with BET1, SCFD1 and SEC22B
CC (PubMed:10930465). Interacts with PTPN2 and ABL1; involved in STX17
CC phosphorylation (PubMed:23006999). Interacts with COPB1
CC (PubMed:21545355). Interacts with TMED9 and TMED10; the interaction is
CC direct (PubMed:21545355). Interacts with RUBCNL/PACER; promoting
CC targeting of RUBCNL/PACER to autophagosome (By similarity). Interacts
CC with VAMP8, SNAP29, VPS39 and VPS41; these interactions are increased
CC in the absence of TMEM39A (By similarity).
CC {ECO:0000250|UniProtKB:P56962, ECO:0000269|PubMed:10930465,
CC ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:23006999}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:21545355}; Multi-pass membrane protein
CC {ECO:0000255}. Smooth endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10930465}; Multi-pass membrane protein
CC {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment
CC membrane {ECO:0000269|PubMed:21545355}; 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:0000269|PubMed:10930465}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm, cytosol {ECO:0000269|PubMed:10930465}.
CC Mitochondrion membrane {ECO:0000250|UniProtKB:P56962}; Multi-pass
CC membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into
CC membranes. Localized into endoplasmic reticulum membranes, it also
CC localizes to the completed autophagosome membrane upon cell starvation
CC (By similarity). {ECO:0000250|UniProtKB:P56962}.
CC -!- TISSUE SPECIFICITY: Detected in all tissues examined with higher
CC expression in steroidogenic tissues including testis and adrenal gland
CC (at protein level). Highly expressed in liver and testis. Also found in
CC brain, heart, kidney, lung, placenta, skeletal muscle and spleen.
CC {ECO:0000269|PubMed:10930465, ECO:0000269|PubMed:9852078}.
CC -!- PTM: Phosphorylated at Tyr-156 probably by ABL1. Dephosphorylation by
CC PTPN2; regulates exit from the endoplasmic reticulum.
CC {ECO:0000269|PubMed:23006999}.
CC -!- SIMILARITY: Belongs to the syntaxin family. {ECO:0000305}.
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DR EMBL; AF115435; AAD11435.1; -; mRNA.
DR RefSeq; NP_663775.1; NM_145723.1.
DR RefSeq; XP_006238086.1; XM_006238024.2.
DR RefSeq; XP_017448641.1; XM_017593152.1.
DR AlphaFoldDB; Q9Z158; -.
DR SMR; Q9Z158; -.
DR BioGRID; 251633; 1.
DR STRING; 10116.ENSRNOP00000007641; -.
DR iPTMnet; Q9Z158; -.
DR PhosphoSitePlus; Q9Z158; -.
DR PaxDb; Q9Z158; -.
DR Ensembl; ENSRNOT00000007641; ENSRNOP00000007641; ENSRNOG00000005801.
DR GeneID; 252853; -.
DR KEGG; rno:252853; -.
DR UCSC; RGD:708499; rat.
DR CTD; 55014; -.
DR RGD; 708499; Stx17.
DR eggNOG; KOG0811; Eukaryota.
DR GeneTree; ENSGT01000000214440; -.
DR HOGENOM; CLU_058244_1_0_1; -.
DR InParanoid; Q9Z158; -.
DR OMA; YPVMGAL; -.
DR OrthoDB; 1493840at2759; -.
DR PhylomeDB; Q9Z158; -.
DR TreeFam; TF323947; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR PRO; PR:Q9Z158; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000005801; Expressed in liver and 18 other tissues.
DR Genevisible; Q9Z158; RN.
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; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS: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: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; ISO:RGD.
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; IDA:UniProtKB.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:RGD.
DR GO; GO:0005484; F:SNAP receptor activity; ISS:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:RGD.
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:RGD.
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_0000210230"
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 REGION 273..301
FT /note="Required for interaction with COPB1, TMED9 and
FT TMED10"
FT /evidence="ECO:0000269|PubMed:21545355"
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:0000269|PubMed:23006999"
FT MOD_RES 288
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P56962"
FT MUTAGEN 156
FT /note="Y->E: Alters interaction with COPB1 but not with
FT SEC24C."
FT /evidence="ECO:0000269|PubMed:21545355,
FT ECO:0000269|PubMed:23006999"
FT MUTAGEN 156
FT /note="Y->F: Prevents phosphorylation by ABL1 and impairs
FT transport from the endoplasmic reticulum to the endoplasmic
FT reticulum-Golgi intermediate compartment."
FT /evidence="ECO:0000269|PubMed:21545355,
FT ECO:0000269|PubMed:23006999"
SQ SEQUENCE 301 AA; 33182 MW; 7C64C38961C5B8DE CRC64;
MSEDEEKVKL RRLEPAIQKF TKIVIPTDLE RLKKHQINIE KYQRCRIWDK LHEEHINAGR
TVQQLRSNIR EMEKLCLKVH KDDLILLKRM IDPMKEAAAA ATAEFLQLHL ESVEELKKQV
KNEEALLQPS LTRSTTIDGV HTGEAEAASQ SLTQIYALPE IPRDQNAAES WETLEADLIE
LSHLVTDMSL LVNSQQEKID SIADHVNSAA VNVEEGTKNL QKAAKYKLAA LPVAGAVIGG
VVGGPIGLLA GFKVAGIAAA LGGGVLGFTG GKLIQRRKQK MMEKLTSSCP DLPSQSDKKC
S
