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   27-MAR-2024, entry version 205.
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; 224.
DR   IntAct; P54920; 65.
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; 9606-ENSP00000263354; -.
DR   PeptideAtlas; P54920; -.
DR   PRIDE; P54920; -.
DR   ProteomicsDB; 56747; -.
DR   Pumba; P54920; -.
DR   TopDownProteomics; P54920; -.
DR   Antibodypedia; 4110; 305 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   AGR; HGNC:7641; -.
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; HFCIDSL; -.
DR   OrthoDB; 4487902at2759; -.
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; 801 hits in 1136 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 99 other cell types or tissues.
DR   ExpressionAtlas; P54920; baseline and differential.
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: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; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR000744; NSF_attach.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   PANTHER; PTHR13768:SF23; ALPHA-SOLUBLE NSF ATTACHMENT PROTEIN; 1.
DR   PANTHER; PTHR13768; SOLUBLE NSF ATTACHMENT PROTEIN SNAP; 1.
DR   Pfam; PF14938; SNAP; 1.
DR   PRINTS; PR00448; NSFATTACHMNT.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   Genevisible; P54920; HS.
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
//