| IED ID |
IndEnz0002001604 |
| Enzyme Type ID |
protease001604 |
| Protein Name |
Syntaxin-17
|
| Gene Name |
STX17 |
| Organism |
Homo sapiens (Human) |
| Taxonomic Lineage |
cellular organisms
Eukaryota
Opisthokonta
Metazoa
Eumetazoa
Bilateria
Deuterostomia
Chordata
Craniata
Vertebrata
Gnathostomata (jawed vertebrates)
Teleostomi
Euteleostomi
Sarcopterygii
Dipnotetrapodomorpha
Tetrapoda
Amniota
Mammalia
Theria
Eutheria
Boreoeutheria
Euarchontoglires
Primates
Haplorrhini
Simiiformes
Catarrhini
Hominoidea (apes)
Hominidae (great apes)
Homininae
Homo
Homo sapiens (Human)
|
| Enzyme Sequence |
MSEDEEKVKLRRLEPAIQKFIKIVIPTDLERLRKHQINIEKYQRCRIWDKLHEEHINAGRTVQQLRSNIREIEKLCLKVRKDDLVLLKRMIDPVKEEASAATAEFLQLHLESVEELKKQFNDEETLLQPPLTRSMTVGGAFHTTEAEASSQSLTQIYALPEIPQDQNAAESWETLEADLIELSQLVTDFSLLVNSQQEKIDSIADHVNSAAVNVEEGTKNLGKAAKYKLAALPVAGALIGGMVGGPIGLLAGFKVAGIAAALGGGVLGFTGGKLIQRKKQKMMEKLTSSCPDLPSQTDKKCS |
| Enzyme Length |
302 |
| Uniprot Accession Number |
P56962 |
| Absorption |
|
| Active Site |
|
| Activity Regulation |
|
| Binding Site |
|
| Calcium Binding |
|
| catalytic Activity |
|
| DNA Binding |
|
| EC Number |
|
| Enzyme Function |
FUNCTION: 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 (PubMed:23217709, PubMed:25686604, PubMed:28306502). STX17 is a SNARE of the autophagosome involved in autophagy through the direct control of autophagosome membrane fusion with the lysosome membrane (PubMed:23217709, PubMed:25686604, PubMed:28306502, PubMed:28504273). 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 (PubMed:21545355). {ECO:0000269|PubMed:21545355, ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:28306502, ECO:0000269|PubMed:28504273}. |
| Temperature Dependency |
|
| PH Dependency |
|
| Pathway |
|
| nucleotide Binding |
|
| Features |
Chain (1); Coiled coil (1); Domain (1); Helix (2); Initiator methionine (1); Modified residue (4); Motif (1); Mutagenesis (5); Region (1); Sequence conflict (3); Topological domain (3); Transmembrane (2) |
| Keywords |
3D-structure;Acetylation;Autophagy;Coiled coil;Cytoplasm;Cytoplasmic vesicle;ER-Golgi transport;Endoplasmic reticulum;Host-virus interaction;Membrane;Mitochondrion;Phosphoprotein;Reference proteome;Transmembrane;Transmembrane helix;Transport |
| Interact With |
O95573; O95721; Q9BV40; Q9H269; Q96AX1; Q96JC1; P49754; P70280 |
| Induction |
|
| Subcellular Location |
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23006999}; Multi-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:23006999}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604, ECO:0000269|PubMed:26416964, ECO:0000269|PubMed:28306502}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q9Z158}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z158}. Mitochondrion membrane {ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:28504273}; Multi-pass membrane protein {ECO:0000255}. Note=Has a hairpin-like insertion into membranes. Localizes to the completed autophagosome membrane upon cell starvation (PubMed:23217709). {ECO:0000269|PubMed:23217709}. |
| Modified Residue |
MOD_RES 2; /note=N-acetylserine; /evidence=ECO:0007744|PubMed:22814378; MOD_RES 41; /note=N6-acetyllysine; /evidence=ECO:0007744|PubMed:19608861; MOD_RES 157; /note=Phosphotyrosine; by ABL1; /evidence=ECO:0000250|UniProtKB:Q9Z158; MOD_RES 289; /note=Phosphoserine; /evidence=ECO:0007744|PubMed:23186163 |
| Post Translational Modification |
PTM: Phosphorylated at Tyr-157 probably by ABL1. Dephosphorylation by PTPN2; regulates exit from the endoplasmic reticulum (By similarity). {ECO:0000250|UniProtKB:Q9Z158}.; PTM: (Microbial infection) Cleaved by the L.pneumophila serine protease Lpg1137, impairing endoplasmic reticulum-mitochondria communication, leading to inhibit autophagy. {ECO:0000269|PubMed:28504273}. |
| Signal Peptide |
|
| Structure 3D |
X-ray crystallography (3) |
| Cross Reference PDB |
4WY4;
7BV4;
7BV6;
|
| Mapped Pubmed ID |
10445031;
10559959;
10747087;
12070132;
15037235;
16303754;
16912714;
17038314;
19164740;
19209086;
20596022;
20711500;
21689688;
22028648;
23378591;
23416715;
24119662;
24412244;
24554770;
25406594;
25492864;
25619926;
27099307;
28673965;
29073720;
29138318;
29420192;
29445155;
29549094;
29925525;
30237312;
30415939;
30655294;
30827897;
31053718;
31251111;
32264736;
32817423;
33155266;
33191543;
33336726;
8221884;
8620540;
8663406;
9094723;
9177194;
9307973;
9647643;
|
| Motif |
MOTIF 299..302; /note=Endoplasmic reticulum retention signal; /evidence=ECO:0000255 |
| Gene Encoded By |
|
| Mass |
33,403 |
| Kinetics |
|
| Metal Binding |
|
| Rhea ID |
|
| Cross Reference Brenda |
|