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SNA29_CAEEL
ID   SNA29_CAEEL             Reviewed;         277 AA.
AC   P83351;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   06-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Soluble NSF attachment protein 29;
GN   Name=snap-29 {ECO:0000312|WormBase:K02D10.5};
GN   Synonyms=phi-28 {ECO:0000312|WormBase:K02D10.5};
GN   ORFNames=K02D10.5 {ECO:0000312|WormBase:K02D10.5};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=28581477; DOI=10.1038/ncb3539;
RA   Sinclair J., Pinter K., Samuel T., Beardsley S., Yuan X., Zhang J.,
RA   Meng K., Yun S., Krause M., Hamza I.;
RT   "Inter-organ signalling by HRG-7 promotes systemic haem homeostasis.";
RL   Nat. Cell Biol. 19:799-807(2017).
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. Plays a role in the processing and
CC       secretion of the aspartic protease hrg-7 from the intestine
CC       (PubMed:28581477). {ECO:0000250|UniProtKB:O95721,
CC       ECO:0000269|PubMed:28581477}.
CC   -!- SUBCELLULAR LOCATION: Synapse, synaptosome {ECO:0000250}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the aberrant
CC       secretion and processing of the aspartic protease hrg-7 with
CC       accumulation of hrg-7 in its immature uncleaved form and in the
CC       intestine. {ECO:0000269|PubMed:28581477}.
CC   -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR   EMBL; BX284603; CCD71830.1; -; Genomic_DNA.
DR   RefSeq; NP_498940.1; NM_066539.7.
DR   AlphaFoldDB; P83351; -.
DR   BioGRID; 41436; 9.
DR   DIP; DIP-61373N; -.
DR   IntAct; P83351; 1.
DR   STRING; 6239.K02D10.5; -.
DR   TCDB; 1.F.1.1.3; the synaptosomal vesicle fusion pore (svf-pore) family.
DR   EPD; P83351; -.
DR   PaxDb; P83351; -.
DR   PeptideAtlas; P83351; -.
DR   EnsemblMetazoa; K02D10.5.1; K02D10.5.1; WBGene00019305.
DR   GeneID; 176233; -.
DR   KEGG; cel:CELE_K02D10.5; -.
DR   UCSC; K02D10.5; c. elegans.
DR   CTD; 176233; -.
DR   WormBase; K02D10.5; CE17152; WBGene00019305; snap-29.
DR   eggNOG; KOG3065; Eukaryota.
DR   GeneTree; ENSGT00950000182843; -.
DR   HOGENOM; CLU_069907_0_0_1; -.
DR   InParanoid; P83351; -.
DR   OMA; NLDEMCD; -.
DR   OrthoDB; 1187770at2759; -.
DR   PhylomeDB; P83351; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   Reactome; R-CEL-6811438; Intra-Golgi traffic.
DR   PRO; PR:P83351; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00019305; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:WormBase.
DR   GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0098793; C:presynapse; IEA:GOC.
DR   GO; GO:0055037; C:recycling endosome; IDA:WormBase.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IMP:WormBase.
DR   GO; GO:0030728; P:ovulation; IMP:WormBase.
DR   GO; GO:0046903; P:secretion; IMP:WormBase.
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; 2.
PE   3: Inferred from homology;
KW   Coiled coil; Protein transport; Reference proteome; Repeat; Synapse;
KW   Synaptosome; Transport.
FT   CHAIN           1..277
FT                   /note="Soluble NSF attachment protein 29"
FT                   /id="PRO_0000213615"
FT   DOMAIN          44..106
FT                   /note="t-SNARE coiled-coil homology 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   DOMAIN          179..241
FT                   /note="t-SNARE coiled-coil homology 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          49..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          117..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   277 AA;  31115 MW;  EF33EBA0ED2574B5 CRC64;
     MSRNPFDDDY RPSAASSTMP VKSYTTMGHY SGEDEADYYE REIEKTLQES LDSTERSRRH
     LENSEKIGTS TAQQLLEQRE KLENTEKNLD EIHRTTQMTQ RNLNSLKSFF GGMFKNKFTK
     KPQEPTETPT VPQSKSASRL SETATNLSSG GGSATFSGPS GQRTLTESSR SAIKGTRWEA
     MDNQIDENLD MMSANLRNLQ RLGADLGKEV DSQNEMLDRI QYKAERNDGI VRDQDKQMQK
     ILGTGASTSQ TTAESLTPSM DTSTKMSLMM KATSLWK
 
 
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