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Synaptosomal-associated protein 29 (SNAP-29) (Soluble 29 kDa NSF attachment protein) (Vesicle-membrane fusion protein SNAP-29)

 SNP29_HUMAN             Reviewed;         258 AA.
O95721;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
23-MAY-2018, entry version 167.
RecName: Full=Synaptosomal-associated protein 29 {ECO:0000312|HGNC:HGNC:11133};
Short=SNAP-29 {ECO:0000312|HGNC:HGNC:11133};
AltName: Full=Soluble 29 kDa NSF attachment protein {ECO:0000312|HGNC:HGNC:11133};
AltName: Full=Vesicle-membrane fusion protein SNAP-29;
Name=SNAP29 {ECO:0000312|HGNC:HGNC:11133};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=9852078; DOI=10.1074/jbc.273.51.34171;
Steegmaier M., Yang B., Yoo J.-S., Huang B., Shen M., Yu S., Luo Y.,
Scheller R.H.;
"Three novel proteins of the syntaxin/SNAP-25 family.";
J. Biol. Chem. 273:34171-34179(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Schardt A., Kraemer E.-M., Werner H., Nave K.-A.;
"Genomic organization of the human SNAP29 gene.";
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INVOLVEMENT IN CEDNIK.
PubMed=15968592; DOI=10.1086/432556;
Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D.,
Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H.,
O'brien T.J., Bercovich D., Shalev S., Geiger D., Bergman R.,
Horowitz M., Mandel H.;
"A mutation in SNAP29, coding for a SNARE protein involved in
intracellular trafficking, causes a novel neurocutaneous syndrome
characterized by cerebral dysgenesis, neuropathy, ichthyosis, and
palmoplantar keratoderma.";
Am. J. Hum. Genet. 77:242-251(2005).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[8]
FUNCTION IN AUTOPHAGY, AND INTERACTION WITH VAMP8 AND STX17.
PubMed=23217709; DOI=10.1016/j.cell.2012.11.001;
Itakura E., Kishi-Itakura C., Mizushima N.;
"The hairpin-type tail-anchored SNARE syntaxin 17 targets to
autophagosomes for fusion with endosomes/lysosomes.";
Cell 151:1256-1269(2012).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77; SER-78; SER-114;
THR-130; THR-137; SER-163; SER-182; SER-185; SER-204 AND SER-210, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[11]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=25686250; DOI=10.1038/ncb3109;
Lu Q., Insinna C., Ott C., Stauffer J., Pintado P.A., Rahajeng J.,
Baxa U., Walia V., Cuenca A., Hwang Y.S., Daar I.O., Lopes S.,
Lippincott-Schwartz J., Jackson P.K., Caplan S., Westlake C.J.;
"Early steps in primary cilium assembly require EHD1/EHD3-dependent
ciliary vesicle formation.";
Nat. Cell Biol. 17:228-240(2015).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[13]
X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 39-116 AND 194-258 IN COMPLEX
WITH STX17 AND VAMP8, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=25686604; DOI=10.1038/nature14147;
Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q.,
Wilz L.M., Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.;
"ATG14 promotes membrane tethering and fusion of autophagosomes to
endolysosomes.";
Nature 520:563-566(2015).
-!- 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. SNAP29 is a
SNARE involved in autophagy through the direct control of
autophagosome membrane fusion with the lysososome membrane. Plays
also a role in ciliogenesis by regulating membrane fusions.
{ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686250,
ECO:0000269|PubMed:25686604}.
-!- SUBUNIT: Forms a SNARE complex, composed of VAMP8, SNAP29 and
STX17, involved in fusion of autophagosome with lysosome
(PubMed:23217709, PubMed:25686604). Interacts with multiple
syntaxins including STX6 (By similarity). Interacts with EIPR1 (By
similarity). {ECO:0000250|UniProtKB:Q9Z2P6,
ECO:0000269|PubMed:23217709, ECO:0000269|PubMed:25686604}.
-!- INTERACTION:
Q8IZU0:FAM9B; NbExp=3; IntAct=EBI-490676, EBI-10175124;
Q9H115:NAPB; NbExp=4; IntAct=EBI-490676, EBI-3921185;
O15294:OGT; NbExp=2; IntAct=EBI-490676, EBI-539828;
Q86Y82:STX12; NbExp=4; IntAct=EBI-490676, EBI-2691717;
O14662-5:STX16; NbExp=4; IntAct=EBI-490676, EBI-9089968;
P56962:STX17; NbExp=9; IntAct=EBI-490676, EBI-2797775;
Q16623:STX1A; NbExp=3; IntAct=EBI-490676, EBI-712466;
O43752:STX6; NbExp=2; IntAct=EBI-490676, EBI-2695795;
P23763:VAMP1; NbExp=3; IntAct=EBI-490676, EBI-10201335;
P63027:VAMP2; NbExp=5; IntAct=EBI-490676, EBI-520113;
O75379-2:VAMP4; NbExp=3; IntAct=EBI-490676, EBI-10187996;
O95183:VAMP5; NbExp=5; IntAct=EBI-490676, EBI-10191195;
Q9BV40:VAMP8; NbExp=5; IntAct=EBI-490676, EBI-727028;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23217709}.
Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6};
Peripheral membrane protein {ECO:0000305}. Cytoplasmic vesicle,
autophagosome membrane {ECO:0000269|PubMed:25686604}; Peripheral
membrane protein {ECO:0000305}. Cell projection, cilium membrane
{ECO:0000269|PubMed:25686250}; Peripheral membrane protein
{ECO:0000305}. Note=Appears to be mostly membrane-bound, probably
via interaction with syntaxins, but a significant portion is
cytoplasmic. Localizes to the ciliary pocket from where the cilium
protrudes. {ECO:0000269|PubMed:23217709,
ECO:0000269|PubMed:25686250}.
-!- TISSUE SPECIFICITY: Found in brain, heart, kidney, liver, lung,
placenta, skeletal muscle, spleen and pancreas.
{ECO:0000269|PubMed:9852078}.
-!- DISEASE: Cerebral dysgenesis, neuropathy, ichthyosis, and
palmoplantar keratoderma syndrome (CEDNIK) [MIM:609528]: A
neurocutaneous syndrome characterized by cerebral dysgenesis,
neuropathy, ichthyosis and palmoplantar keratoderma.
{ECO:0000269|PubMed:15968592}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF115436; AAD11436.1; -; mRNA.
EMBL; AF278704; AAF91421.1; -; Genomic_DNA.
EMBL; CR456582; CAG30468.1; -; mRNA.
EMBL; BT007357; AAP36021.1; -; mRNA.
EMBL; BC009715; AAH09715.1; -; mRNA.
CCDS; CCDS13784.1; -.
RefSeq; NP_004773.1; NM_004782.3.
UniGene; Hs.108002; -.
PDB; 4WY4; X-ray; 1.40 A; C=39-116, D=194-258.
PDBsum; 4WY4; -.
ProteinModelPortal; O95721; -.
SMR; O95721; -.
BioGrid; 114748; 84.
CORUM; O95721; -.
DIP; DIP-56475N; -.
IntAct; O95721; 54.
MINT; O95721; -.
STRING; 9606.ENSP00000215730; -.
iPTMnet; O95721; -.
PhosphoSitePlus; O95721; -.
BioMuta; SNAP29; -.
EPD; O95721; -.
MaxQB; O95721; -.
PaxDb; O95721; -.
PeptideAtlas; O95721; -.
PRIDE; O95721; -.
DNASU; 9342; -.
Ensembl; ENST00000215730; ENSP00000215730; ENSG00000099940.
GeneID; 9342; -.
KEGG; hsa:9342; -.
UCSC; uc011ahw.3; human.
CTD; 9342; -.
DisGeNET; 9342; -.
EuPathDB; HostDB:ENSG00000099940.11; -.
GeneCards; SNAP29; -.
HGNC; HGNC:11133; SNAP29.
HPA; CAB037092; -.
HPA; HPA031823; -.
HPA; HPA056492; -.
MalaCards; SNAP29; -.
MIM; 604202; gene.
MIM; 609528; phenotype.
neXtProt; NX_O95721; -.
OpenTargets; ENSG00000099940; -.
Orphanet; 66631; CEDNIK syndrome.
PharmGKB; PA35981; -.
eggNOG; KOG3065; Eukaryota.
eggNOG; ENOG410Y3Y0; LUCA.
GeneTree; ENSGT00510000048053; -.
HOGENOM; HOG000046806; -.
HOVERGEN; HBG057045; -.
InParanoid; O95721; -.
KO; K08509; -.
OMA; QEAQYQA; -.
OrthoDB; EOG091G0GKH; -.
PhylomeDB; O95721; -.
TreeFam; TF320226; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-6811438; Intra-Golgi traffic.
ChiTaRS; SNAP29; human.
GeneWiki; SNAP29; -.
GenomeRNAi; 9342; -.
PRO; PR:O95721; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099940; -.
CleanEx; HS_SNAP29; -.
ExpressionAtlas; O95721; baseline and differential.
Genevisible; O95721; HS.
GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0020018; C:ciliary pocket membrane; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
GO; GO:0005484; F:SNAP receptor activity; TAS:ProtInc.
GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
GO; GO:0097352; P:autophagosome maturation; IMP:UniProtKB.
GO; GO:0016240; P:autophagosome membrane docking; IDA:GO_Central.
GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
GO; GO:0006887; P:exocytosis; TAS:ProtInc.
GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
InterPro; IPR000727; T_SNARE_dom.
SMART; SM00397; t_SNARE; 2.
PROSITE; PS50192; T_SNARE; 1.
1: Evidence at protein level;
3D-structure; Autophagy; Cell membrane; Cell projection; Cilium;
Cilium biogenesis/degradation; Coiled coil; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Golgi apparatus; Ichthyosis; Membrane;
Neuropathy; Palmoplantar keratoderma; Phosphoprotein;
Protein transport; Reference proteome; Transport.
CHAIN 1 258 Synaptosomal-associated protein 29.
/FTId=PRO_0000213601.
DOMAIN 196 258 t-SNARE coiled-coil homology.
{ECO:0000255|PROSITE-ProRule:PRU00202}.
COILED 76 107 {ECO:0000255}.
MOD_RES 77 77 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 78 78 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 114 114 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 130 130 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 137 137 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 185 185 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 204 204 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 210 210 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
HELIX 40 113 {ECO:0000244|PDB:4WY4}.
HELIX 195 255 {ECO:0000244|PDB:4WY4}.
SEQUENCE 258 AA; 28970 MW; 7E1CDBA22D6F5A3C CRC64;
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
NYFKSKPVET PPEQNGTLTS QPNNRLKEAI STSKEQEAKY QASHPNLRKL DDTDPVPRGA
GSAMSTDAYP KNPHLRAYHQ KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
VDKLDVNIKS TERKVRQL


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