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 24-JAN-2024, entry version 160. 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 RC 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; 35. DR DIP; DIP-60853N; -. DR IntAct; Q9ERB0; 22. DR STRING; 10090.ENSMUSP00000023449; -. DR GlyGen; Q9ERB0; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9ERB0; -. DR PhosphoSitePlus; Q9ERB0; -. DR EPD; Q9ERB0; -. DR MaxQB; Q9ERB0; -. DR PaxDb; 10090-ENSMUSP00000023449; -. DR PeptideAtlas; Q9ERB0; -. DR ProteomicsDB; 261531; -. DR Pumba; Q9ERB0; -. DR Antibodypedia; 23352; 223 antibodies from 29 providers. DR DNASU; 67474; -. DR Ensembl; ENSMUST00000023449.11; ENSMUSP00000023449.9; ENSMUSG00000022765.11. DR GeneID; 67474; -. DR KEGG; mmu:67474; -. DR UCSC; uc007yku.1; mouse. DR AGR; MGI:1914724; -. 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; 4213488at2759; -. 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 77 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 248 other cell types or tissues. 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:0005829; C:cytosol; ISO:MGI. DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI. 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:0008021; C:synaptic vesicle; ISO:MGI. 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:2000300; P:regulation of synaptic vesicle exocytosis; 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 CDD; cd15856; SNARE_SNAP29C; 1. DR CDD; cd15887; SNARE_SNAP29N; 1. DR Gene3D; 1.20.5.110; -; 2. DR InterPro; IPR000727; T_SNARE_dom. DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR19305:SF9; SYNAPTOSOMAL-ASSOCIATED PROTEIN 29; 1. DR SMART; SM00397; t_SNARE; 2. DR SUPFAM; SSF58038; SNARE fusion complex; 2. DR PROSITE; PS50192; T_SNARE; 1. DR Genevisible; Q9ERB0; MM. 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 //