SNAA_HUMAN
ID SNAA_HUMAN Reviewed; 295 AA.
AC P54920; A8K879; Q96IK3; Q9BVJ3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 196.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Platelet;
RX PubMed=9269766;
RA Lemons P.P., Chen D., Bernstein A.M., Bennett M.K., Whiteheart S.W.;
RT "Regulated secretion in platelets: identification of elements of the
RT platelet exocytosis machinery.";
RL Blood 90:1490-1500(1997).
RN [2]
RP SEQUENCE REVISION TO 91; 133 AND 289.
RA Chen D., Shao H.P., Whiteheart S.W.;
RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Placenta;
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A COMPLEX WITH
RP RINT1; USE1L; NAPA AND ZW10.
RX PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT "Implication of ZW10 in membrane trafficking between the endoplasmic
RT reticulum and Golgi.";
RL EMBO J. 23:1267-1278(2004).
RN [8]
RP FUNCTION, INTERACTION WITH GNA12, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-122 AND LYS-140.
RX PubMed=15980433; DOI=10.1074/jbc.m502844200;
RA Andreeva A.V., Kutuzov M.A., Vaiskunaite R., Profirovic J., Meigs T.E.,
RA Predescu S., Malik A.B., Voyno-Yasenetskaya T.;
RT "G alpha12 interaction with alphaSNAP induces VE-cadherin localization at
RT endothelial junctions and regulates barrier function.";
RL J. Biol. Chem. 280:30376-30383(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC reticulum and the Golgi apparatus (Probable). Together with GNA12
CC promotes CDH5 localization to plasma membrane (PubMed:15980433).
CC {ECO:0000269|PubMed:15980433, ECO:0000305}.
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 (PubMed:15029241). Interacts with VTI1A (By
CC similarity). Interacts with STX12 (By similarity). Interacts with GNA12
CC (via N-terminus); the interaction promotes CDH5 localization to plasma
CC membrane (PubMed:15980433). {ECO:0000250|UniProtKB:P54921,
CC ECO:0000250|UniProtKB:Q9DB05, ECO:0000269|PubMed:15029241,
CC ECO:0000269|PubMed:15980433}.
CC -!- INTERACTION:
CC P54920; P42858: HTT; NbExp=3; IntAct=EBI-749652, EBI-466029;
CC P54920; P46459: NSF; NbExp=3; IntAct=EBI-749652, EBI-712251;
CC P54920; O00161: SNAP23; NbExp=3; IntAct=EBI-749652, EBI-745000;
CC P54920; Q12846: STX4; NbExp=3; IntAct=EBI-749652, EBI-744942;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15980433};
CC Peripheral membrane protein {ECO:0000305|PubMed:15029241}.
CC -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR EMBL; U39412; AAC80170.1; -; mRNA.
DR EMBL; BT019568; AAV38375.1; -; mRNA.
DR EMBL; AK292244; BAF84933.1; -; mRNA.
DR EMBL; CH471126; EAW57491.1; -; Genomic_DNA.
DR EMBL; BC001165; AAH01165.1; -; mRNA.
DR EMBL; BC007432; AAH07432.1; -; mRNA.
DR EMBL; BC028234; AAH28234.1; -; mRNA.
DR EMBL; BC091511; AAH91511.1; -; mRNA.
DR CCDS; CCDS12702.1; -.
DR PIR; G02238; G02238.
DR RefSeq; NP_003818.2; NM_003827.3.
DR AlphaFoldDB; P54920; -.
DR SMR; P54920; -.
DR BioGRID; 114305; 157.
DR IntAct; P54920; 62.
DR MINT; P54920; -.
DR STRING; 9606.ENSP00000263354; -.
DR GlyGen; P54920; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P54920; -.
DR MetOSite; P54920; -.
DR PhosphoSitePlus; P54920; -.
DR SwissPalm; P54920; -.
DR BioMuta; NAPA; -.
DR DMDM; 116242794; -.
DR OGP; P54920; -.
DR CPTAC; CPTAC-547; -.
DR CPTAC; CPTAC-548; -.
DR EPD; P54920; -.
DR jPOST; P54920; -.
DR MassIVE; P54920; -.
DR MaxQB; P54920; -.
DR PaxDb; P54920; -.
DR PeptideAtlas; P54920; -.
DR PRIDE; P54920; -.
DR ProteomicsDB; 56747; -.
DR TopDownProteomics; P54920; -.
DR Antibodypedia; 4110; 276 antibodies from 33 providers.
DR DNASU; 8775; -.
DR Ensembl; ENST00000263354.8; ENSP00000263354.2; ENSG00000105402.8.
DR GeneID; 8775; -.
DR KEGG; hsa:8775; -.
DR MANE-Select; ENST00000263354.8; ENSP00000263354.2; NM_003827.4; NP_003818.2.
DR UCSC; uc002pha.3; human.
DR CTD; 8775; -.
DR DisGeNET; 8775; -.
DR GeneCards; NAPA; -.
DR HGNC; HGNC:7641; NAPA.
DR HPA; ENSG00000105402; Low tissue specificity.
DR MIM; 603215; gene.
DR neXtProt; NX_P54920; -.
DR OpenTargets; ENSG00000105402; -.
DR PharmGKB; PA31443; -.
DR VEuPathDB; HostDB:ENSG00000105402; -.
DR eggNOG; KOG1586; Eukaryota.
DR GeneTree; ENSGT00390000005826; -.
DR HOGENOM; CLU_046329_0_1_1; -.
DR InParanoid; P54920; -.
DR OMA; NVEAYTD; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; P54920; -.
DR TreeFam; TF316547; -.
DR PathwayCommons; P54920; -.
DR Reactome; R-HSA-204005; COPII-mediated vesicle transport.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR Reactome; R-HSA-6811440; Retrograde transport at the Trans-Golgi-Network.
DR SignaLink; P54920; -.
DR BioGRID-ORCS; 8775; 766 hits in 1056 CRISPR screens.
DR ChiTaRS; NAPA; human.
DR GeneWiki; NAPA_(gene); -.
DR GenomeRNAi; 8775; -.
DR Pharos; P54920; Tbio.
DR PRO; PR:P54920; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P54920; protein.
DR Bgee; ENSG00000105402; Expressed in right hemisphere of cerebellum and 97 other tissues.
DR ExpressionAtlas; P54920; baseline and differential.
DR Genevisible; P54920; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0045176; P:apical protein localization; IEA:Ensembl.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0006891; P:intra-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0035494; P:SNARE complex disassembly; IBA:GO_Central.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IEA:Ensembl.
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; ER-Golgi transport; Membrane; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..295
FT /note="Alpha-soluble NSF attachment protein"
FT /id="PRO_0000219056"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB05"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MUTAGEN 122
FT /note="K->A: Does not affect interaction with GNA12."
FT /evidence="ECO:0000269|PubMed:15980433"
FT MUTAGEN 140
FT /note="K->A: Increases interaction with GNA12."
FT /evidence="ECO:0000269|PubMed:15980433"
FT CONFLICT 195
FT /note="S -> T (in Ref. 1; AAC80170)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 33233 MW; 7704A619A441E609 CRC64;
MDNSGKEAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA
AGNAFCQAAQ LHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA
AKHHISIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAALLEQYQK
AIDIYEQVGT NAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE
CKLMKKLLEA HEEQNVDSYT ESVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR
