SNAA_MOUSE
ID SNAA_MOUSE Reviewed; 295 AA.
AC Q9DB05; Q543I3;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Alpha-soluble NSF attachment protein;
DE Short=SNAP-alpha;
DE AltName: Full=N-ethylmaleimide-sensitive factor attachment protein alpha;
GN Name=Napa; Synonyms=Snapa;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Cerebellum, Epididymis, Spleen, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP PROTEIN SEQUENCE OF 247-264 AND 272-282, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Lubec G., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP INTERACTION WITH VTI1A.
RX PubMed=9705316; DOI=10.1074/jbc.273.34.21783;
RA Xu Y., Wong S.H., Tang B.L., Subramaniam V.N., Zhang T., Hong W.;
RT "A 29-kilodalton Golgi soluble N-ethylmaleimide-sensitive factor attachment
RT protein receptor (Vti1-rp2) implicated in protein trafficking in the
RT secretory pathway.";
RL J. Biol. Chem. 273:21783-21789(1998).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26 AND SER-195, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus. Together with GNA12 promotes CDH5
CC localization to plasma membrane. {ECO:0000250|UniProtKB:P54920}.
CC -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between
CC GRIA2 and PRKCABP, leading to the internalization of GRIA2 (By
CC similarity). Found in a complex with VAMP8 (By similarity). Component
CC of a SNARE-like complex that contains at least ZW10, USE1L, RINT1,
CC STX18 and NAPA/SNAP-alpha (By similarity). Interacts with VTI1A
CC (PubMed:9705316). Interacts with STX12 (By similarity). Interacts with
CC GNA12 (via N-terminus); the interaction promotes CDH5 localization to
CC plasma membrane (By similarity). {ECO:0000250|UniProtKB:P54920,
CC ECO:0000250|UniProtKB:P54921, ECO:0000269|PubMed:9705316}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54920};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P54920}.
CC -!- SIMILARITY: Belongs to the SNAP 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; AK005372; BAB23981.1; -; mRNA.
DR EMBL; AK050623; BAC34348.1; -; mRNA.
DR EMBL; AK136689; BAE23100.1; -; mRNA.
DR EMBL; AK171998; BAE42767.1; -; mRNA.
DR EMBL; BC004804; AAH04804.1; -; mRNA.
DR CCDS; CCDS20843.1; -.
DR RefSeq; NP_080174.1; NM_025898.3.
DR AlphaFoldDB; Q9DB05; -.
DR SMR; Q9DB05; -.
DR BioGRID; 223847; 16.
DR IntAct; Q9DB05; 2.
DR STRING; 10090.ENSMUSP00000006181; -.
DR iPTMnet; Q9DB05; -.
DR PhosphoSitePlus; Q9DB05; -.
DR SwissPalm; Q9DB05; -.
DR REPRODUCTION-2DPAGE; Q9DB05; -.
DR EPD; Q9DB05; -.
DR jPOST; Q9DB05; -.
DR MaxQB; Q9DB05; -.
DR PaxDb; Q9DB05; -.
DR PeptideAtlas; Q9DB05; -.
DR PRIDE; Q9DB05; -.
DR ProteomicsDB; 257532; -.
DR Antibodypedia; 4110; 276 antibodies from 33 providers.
DR DNASU; 108124; -.
DR Ensembl; ENSMUST00000006181; ENSMUSP00000006181; ENSMUSG00000006024.
DR GeneID; 108124; -.
DR KEGG; mmu:108124; -.
DR UCSC; uc009fgw.1; mouse.
DR CTD; 8775; -.
DR MGI; MGI:104563; Napa.
DR VEuPathDB; HostDB:ENSMUSG00000006024; -.
DR eggNOG; KOG1586; Eukaryota.
DR GeneTree; ENSGT00390000005826; -.
DR HOGENOM; CLU_046329_0_2_1; -.
DR InParanoid; Q9DB05; -.
DR OMA; NVEAYTD; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; Q9DB05; -.
DR TreeFam; TF316547; -.
DR Reactome; R-MMU-204005; COPII-mediated vesicle transport.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR Reactome; R-MMU-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-MMU-6811438; Intra-Golgi traffic.
DR Reactome; R-MMU-6811440; Retrograde transport at the Trans-Golgi-Network.
DR BioGRID-ORCS; 108124; 24 hits in 71 CRISPR screens.
DR ChiTaRS; Napa; mouse.
DR PRO; PR:Q9DB05; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9DB05; protein.
DR Bgee; ENSMUSG00000006024; Expressed in dentate gyrus of hippocampal formation granule cell and 277 other tissues.
DR ExpressionAtlas; Q9DB05; baseline and differential.
DR Genevisible; Q9DB05; MM.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IDA:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0000149; F:SNARE binding; ISS:ParkinsonsUK-UCL.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:MGI.
DR GO; GO:0045176; P:apical protein localization; IMP:MGI.
DR GO; GO:0007420; P:brain development; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IMP:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; ISO:MGI.
DR GO; GO:0032984; P:protein-containing complex disassembly; ISO:MGI.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IDA:SynGO.
DR GO; GO:0035494; P:SNARE complex disassembly; IGI:MGI.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IGI:MGI.
DR GO; GO:0016082; P:synaptic vesicle priming; IDA:SynGO.
DR CDD; cd15832; SNAP; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR000744; NSF_attach.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR13768; PTHR13768; 1.
DR PRINTS; PR00448; NSFATTACHMNT.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell membrane; Direct protein sequencing; ER-Golgi transport;
KW Membrane; Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..295
FT /note="Alpha-soluble NSF attachment protein"
FT /id="PRO_0000219057"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54920"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54920"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 295 AA; 33190 MW; 30D099B598992AA3 CRC64;
MDNSGKQAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA
AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA
AKHHISIAEI YETELVDVEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAAQLEQYQK
AIDIYEQVGT SAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE
CKLMKKLLEA HEEQNVDSYT EAVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR
