SNP29_PONAB
ID SNP29_PONAB Reviewed; 258 AA.
AC Q5R5K4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860854; CAH92962.1; -; mRNA.
DR RefSeq; NP_001126747.1; NM_001133275.1.
DR AlphaFoldDB; Q5R5K4; -.
DR SMR; Q5R5K4; -.
DR STRING; 9601.ENSPPYP00000013412; -.
DR Ensembl; ENSPPYT00000052612; ENSPPYP00000032534; ENSPPYG00000032205.
DR GeneID; 100173749; -.
DR KEGG; pon:100173749; -.
DR CTD; 9342; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_069907_1_0_1; -.
DR InParanoid; Q5R5K4; -.
DR OMA; NLDEMCD; -.
DR OrthoDB; 1358184at2759; -.
DR TreeFam; TF320226; -.
DR Proteomes; UP000001595; Chromosome 22.
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:0031201; C:SNARE complex; ISS:UniProtKB.
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:0015031; P:protein transport; IEA:UniProtKB-KW.
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_0000230297"
FT DOMAIN 196..258
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 76..107
FT /evidence="ECO:0000255"
FT COMPBIAS 10..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 78
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; 28835 MW; D646D2F23BEEEB12 CRC64;
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL RRAEATAAST
SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ DLKISQKHIN SIKSVFGGLV
NYFKSKPVET PPEQNGTLAS QPNSRLKEAI SSSKEQEAKY QASHPNLRRL DDTDPVPRGA
GSAVSTDAYP KNPHLQAYHQ KIDSNLDELS VGLGRLKDIA LGMQTEIEEQ DDILDRLTTK
VDKLDVNIKS TERKVRQL
