SNP29_MOUSE
ID SNP29_MOUSE Reviewed; 260 AA.
AC Q9ERB0; Q3UGN0; Q9DBC5;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Synaptosomal-associated protein 29 {ECO:0000312|MGI:MGI:1914724};
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 {ECO:0000250|UniProtKB:O95721};
DE AltName: Full=Vesicle-membrane fusion protein SNAP-29;
GN Name=Snap29 {ECO:0000312|MGI:MGI:1914724};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Bui T.D., Hong W.;
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, Liver, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=27628032; DOI=10.1242/bio.018648;
RA Hubert V., Peschel A., Langer B., Groeger M., Rees A., Kain R.;
RT "LAMP-2 is required for incorporating syntaxin-17 into autophagosomes and
RT for their fusion with lysosomes.";
RL Biol. Open 5:1516-1529(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 (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:0000305}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000269|PubMed:27628032}; 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 -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY008722; AAG32076.1; -; mRNA.
DR EMBL; AK005042; BAB23769.1; -; mRNA.
DR EMBL; AK007065; BAB24850.1; -; mRNA.
DR EMBL; AK039203; BAC30277.1; -; mRNA.
DR EMBL; AK147845; BAE28177.1; -; mRNA.
DR EMBL; BC030066; AAH30066.1; -; mRNA.
DR CCDS; CCDS28001.1; -.
DR RefSeq; NP_075837.3; NM_023348.4.
DR AlphaFoldDB; Q9ERB0; -.
DR SMR; Q9ERB0; -.
DR BioGRID; 212216; 33.
DR DIP; DIP-60853N; -.
DR IntAct; Q9ERB0; 22.
DR STRING; 10090.ENSMUSP00000023449; -.
DR iPTMnet; Q9ERB0; -.
DR PhosphoSitePlus; Q9ERB0; -.
DR EPD; Q9ERB0; -.
DR MaxQB; Q9ERB0; -.
DR PaxDb; Q9ERB0; -.
DR PeptideAtlas; Q9ERB0; -.
DR PRIDE; Q9ERB0; -.
DR ProteomicsDB; 261531; -.
DR Antibodypedia; 23352; 199 antibodies from 29 providers.
DR DNASU; 67474; -.
DR Ensembl; ENSMUST00000023449; ENSMUSP00000023449; ENSMUSG00000022765.
DR GeneID; 67474; -.
DR KEGG; mmu:67474; -.
DR UCSC; uc007yku.1; mouse.
DR CTD; 9342; -.
DR MGI; MGI:1914724; Snap29.
DR VEuPathDB; HostDB:ENSMUSG00000022765; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_069907_1_0_1; -.
DR InParanoid; Q9ERB0; -.
DR OMA; NLDEMCD; -.
DR OrthoDB; 1358184at2759; -.
DR PhylomeDB; Q9ERB0; -.
DR TreeFam; TF320226; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR BioGRID-ORCS; 67474; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Snap29; mouse.
DR PRO; PR:Q9ERB0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q9ERB0; protein.
DR Bgee; ENSMUSG00000022765; Expressed in animal zygote and 246 other tissues.
DR Genevisible; Q9ERB0; MM.
DR GO; GO:0005776; C:autophagosome; IDA:UniProtKB.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0020018; C:ciliary pocket membrane; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0016240; P:autophagosome membrane docking; ISO:MGI.
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; ISO:MGI.
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 Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transport.
FT CHAIN 1..260
FT /note="Synaptosomal-associated protein 29"
FT /id="PRO_0000213602"
FT DOMAIN 198..260
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 COILED 76..107
FT /evidence="ECO:0000255"
FT COMPBIAS 19..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 184
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 206
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT MOD_RES 212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95721"
FT CONFLICT 183..184
FT /note="SS -> FF (in Ref. 2; BAB23769)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 260 AA; 29572 MW; DD813A78C605576F CRC64;
MSGYPKSYNP FDDDVEEEDT RPAPWKDVRD LPDGPDAPID RQQYLRQEVL RRAEATAAST
SRSLSLMYES EKIGVASSEE LVRQRGVLEH TEKMVDKMDQ DLKMSQKHIN SIKSVFGGFI
NYFKSKPVEP PPEQNGSIVS QPNSRLKEAI NTSKDQENKY QASHPNLRRL QDAELDSVPK
EPSSTVNTEV YPKNSTLRTY HQKIDSNLDE LSVGLGHLKD IALGMQTEIE EQDDILDRLT
TKVDKLDVNI KSTEKKVRQL
