SNP29_RAT
ID SNP29_RAT Reviewed; 257 AA.
AC Q9Z2P6;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Synaptosomal-associated protein 29 {ECO:0000250|UniProtKB:O95721};
DE Short=SNAP-29 {ECO:0000250|UniProtKB:O95721};
DE AltName: Full=Golgi SNARE of 32 kDa;
DE Short=Gs32;
DE AltName: Full=Soluble 29 kDa NSF attachment protein;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=Snap29 {ECO:0000250|UniProtKB:O95721};
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], SUBCELLULAR LOCATION, INTERACTION WITH STX6,
RP AND TISSUE SPECIFICITY.
RX PubMed=9880331; DOI=10.1091/mbc.10.1.119;
RA Wong S.H., Xu Y., Zhang T., Griffiths G., Lowe S.L., Subramaniam V.N.,
RA Seow K.T., Hong W.;
RT "GS32, a novel Golgi SNARE of 32 kDa, interacts preferentially with
RT syntaxin 6.";
RL Mol. Biol. Cell 10:119-134(1999).
RN [2]
RP PROTEIN SEQUENCE OF 170-190 AND 201-235, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA Lubec G., Diao W.;
RL Submitted (APR-2007) to UniProtKB.
RN [3]
RP INTERACTION WITH EIPR1.
RX PubMed=27191843; DOI=10.1371/journal.pgen.1006074;
RA Topalidou I., Cattin-Ortola J., Pappas A.L., Cooper K., Merrihew G.E.,
RA MacCoss M.J., Ailion M.;
RT "The EARP complex and its interactor eipr-1 are required for cargo sorting
RT to dense-core vesicles.";
RL PLoS Genet. 12:E1006074-E1006074(2016).
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 (PubMed:9880331).
CC Interacts with EIPR1 (PubMed:27191843). Interacts with STX17; this
CC interaction is increased in the absence of TMEM39A (By similarity).
CC {ECO:0000250|UniProtKB:O95721, ECO:0000269|PubMed:27191843,
CC ECO:0000269|PubMed:9880331}.
CC -!- INTERACTION:
CC Q9Z2P6; Q641Z6: Ehd1; NbExp=2; IntAct=EBI-492883, EBI-492911;
CC Q9Z2P6; Q9EQP2: Ehd4; Xeno; NbExp=2; IntAct=EBI-492883, EBI-491022;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9880331}. Golgi
CC apparatus membrane {ECO:0000269|PubMed:9880331}; Peripheral membrane
CC protein {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein
CC {ECO:0000305}. Cell projection, cilium membrane
CC {ECO:0000250|UniProtKB:O95721}; Peripheral membrane protein
CC {ECO:0000305}. Note=Appears to be mostly membrane-bound, probably via
CC interaction with syntaxins, but a significant portion is cytoplasmic.
CC Localizes to the ciliary pocket from where the cilium protrudes.
CC {ECO:0000250|UniProtKB:O95721}.
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9880331}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; AF035822; AAC72291.1; -; mRNA.
DR AlphaFoldDB; Q9Z2P6; -.
DR SMR; Q9Z2P6; -.
DR CORUM; Q9Z2P6; -.
DR ELM; Q9Z2P6; -.
DR IntAct; Q9Z2P6; 4.
DR STRING; 10116.ENSRNOP00000002550; -.
DR iPTMnet; Q9Z2P6; -.
DR PhosphoSitePlus; Q9Z2P6; -.
DR jPOST; Q9Z2P6; -.
DR PaxDb; Q9Z2P6; -.
DR PRIDE; Q9Z2P6; -.
DR RGD; 620225; Snap29.
DR eggNOG; KOG3065; Eukaryota.
DR InParanoid; Q9Z2P6; -.
DR PhylomeDB; Q9Z2P6; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR PRO; PR:Q9Z2P6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
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; ISO:RGD.
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:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
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 1: Evidence at protein level;
KW Autophagy; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Coiled coil; Cytoplasm; Cytoplasmic vesicle;
KW Direct protein sequencing; Golgi apparatus; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..257
FT /note="Synaptosomal-associated protein 29"
FT /id="PRO_0000213603"
FT DOMAIN 195..257
FT /note="t-SNARE coiled-coil homology"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..36
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 163
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
SQ SEQUENCE 257 AA; 29071 MW; 9B9BC1A351CB1A3C CRC64;
MSGYPKSYNP FDDDVEDEDT RPAPWKDARD LPDGPDPPID RQQYLRQEVL RGPSATAAST
SRSLFLMYES EKIGVASSEE LVRQRGVLEH TEKMVDKMDQ DLKMSQKHIN SIKSVFGGFI
NYFKSKPVEP PPEQNGSIVP QPSSRLKEAI NTSKDQESKY QASHPNLRRL HDAELDSVPA
STVNTEVYPK NSSLRAYHQK IDSNLDELSV GLGRLKDIAL GMQTEIEEQD DILDRLTTKV
DKLDVNIKST EKKVRQL
