SNP29_BOVIN
ID SNP29_BOVIN Reviewed; 258 AA.
AC Q0II86;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Synaptosomal-associated protein 29 {ECO:0000250|UniProtKB:O95721};
DE Short=SNAP-29 {ECO:0000250|UniProtKB:O95721};
DE AltName: Full=Soluble 29 kDa NSF attachment protein {ECO:0000250|UniProtKB:O95721};
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=SNAP29 {ECO:0000250|UniProtKB:O95721};
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].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-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. SNAP29 is a SNARE involved in autophagy
CC through the direct control of autophagosome membrane fusion with the
CC lysososome membrane. Also plays a role in ciliogenesis by regulating
CC membrane fusions. {ECO:0000250|UniProtKB:O95721}.
CC -!- SUBUNIT: Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17,
CC involved in fusion of autophagosome with lysosome (By similarity).
CC Interacts with multiple syntaxins including STX6 (By similarity).
CC Interacts with EIPR1 (By similarity). Interacts with STX17; this
CC interaction is increased in the absence of TMEM39A (By similarity).
CC {ECO:0000250|UniProtKB:O95721, ECO:0000250|UniProtKB:Q9Z2P6}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O95721}. Golgi
CC apparatus membrane {ECO:0000250|UniProtKB:Q9Z2P6}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O95721}. Cytoplasmic vesicle,
CC autophagosome membrane {ECO:0000250|UniProtKB:O95721}; Peripheral
CC membrane protein {ECO:0000250|UniProtKB:O95721}. Cell projection,
CC cilium membrane {ECO:0000250|UniProtKB:O95721}; Peripheral membrane
CC protein {ECO:0000250|UniProtKB:O95721}. Note=Appears to be mostly
CC membrane-bound, probably via interaction with syntaxins, but a
CC significant portion is cytoplasmic. Localizes to the ciliary pocket
CC from where the cilium protrudes. {ECO:0000250|UniProtKB:O95721}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; BC122755; AAI22756.1; -; mRNA.
DR RefSeq; NP_001069427.1; NM_001075959.1.
DR AlphaFoldDB; Q0II86; -.
DR SMR; Q0II86; -.
DR STRING; 9913.ENSBTAP00000027666; -.
DR PaxDb; Q0II86; -.
DR PeptideAtlas; Q0II86; -.
DR PRIDE; Q0II86; -.
DR Ensembl; ENSBTAT00000027666; ENSBTAP00000027666; ENSBTAG00000020760.
DR GeneID; 532261; -.
DR KEGG; bta:532261; -.
DR CTD; 9342; -.
DR VEuPathDB; HostDB:ENSBTAG00000020760; -.
DR VGNC; VGNC:35052; SNAP29.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_069907_1_0_1; -.
DR InParanoid; Q0II86; -.
DR OMA; NLDEMCD; -.
DR OrthoDB; 1358184at2759; -.
DR TreeFam; TF320226; -.
DR Reactome; R-BTA-6798695; Neutrophil degranulation.
DR Reactome; R-BTA-6811438; Intra-Golgi traffic.
DR Proteomes; UP000009136; Chromosome 17.
DR Bgee; ENSBTAG00000020760; Expressed in spermatid and 109 other tissues.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IEA:Ensembl.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; IEA:Ensembl.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR InterPro; IPR000727; T_SNARE_dom.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..258
FT /note="Synaptosomal-associated protein 29"
FT /id="PRO_0000282874"
FT DOMAIN 196..258
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..107
FT /evidence="ECO:0000255"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ERB0"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 130
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 137
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 204
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 210
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
SQ SEQUENCE 258 AA; 28490 MW; 6F450322040BE683 CRC64;
MSAYPRSYNP FDEDAEDEDA RPAPWSDSRD LADGPGAPAD RQQALRQEVL RRAEATAAST
GRSLSLMYES ERIGVVSAEE LVRQRGALER TEKMVDKMEQ DLKTSQKHIN SIKSVFGGLV
NYFRSKPAET PSAQNGTLTP QPSGRLKDAI NSSKEQEAQY QASHPNLRKL QDSDSIPGGA
GSAVSSEAYP RNPHLRACHQ RIDSNLDELS VGLGRLKDIA LGIQTEIDEQ DDILDRLTSK
VDKLDVSITS TERKVRQL
