SNAA_RAT
ID SNAA_RAT Reviewed; 295 AA.
AC P54921;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 159.
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=Snap, Snapa;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=White adipose tissue;
RA Mitchell J.R.D., Mitchell M., Holman D., Oldfield S.;
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pituitary;
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 INTERACTION WITH STX12.
RX PubMed=9507000; DOI=10.1074/jbc.273.12.6944;
RA Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.;
RT "Syntaxin 12, a member of the syntaxin family localized to the endosome.";
RL J. Biol. Chem. 273:6944-6950(1998).
RN [4]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8.
RX PubMed=9614193; DOI=10.1091/mbc.9.6.1549;
RA Wong S.H., Zhang T., Xu Y., Subramaniam V.N., Griffiths G., Hong W.;
RT "Endobrevin, a novel synaptobrevin/VAMP-like protein preferentially
RT associated with the early endosome.";
RL Mol. Biol. Cell 9:1549-1563(1998).
RN [5]
RP INTERACTION WITH PRKCABP.
RX PubMed=11931741; DOI=10.1016/s0896-6273(02)00638-4;
RA Hanley J.G., Khatri L., Hanson P.I., Ziff E.B.;
RT "NSF ATPase and alpha-/beta-SNAPs disassemble the AMPA receptor-PICK1
RT complex.";
RL Neuron 34:53-67(2002).
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
CC (PubMed:11931741). Found in a complex with VAMP8 (PubMed:9614193).
CC Component of a SNARE-like complex that contains at least ZW10, USE1L,
CC RINT1, STX18 and NAPA/SNAP-alpha (By similarity). Interacts with VTI1A
CC (By similarity). Interacts with STX12 (PubMed:9507000). 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:Q9DB05, ECO:0000269|PubMed:11931741,
CC ECO:0000269|PubMed:9507000, ECO:0000269|PubMed:9614193}.
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}.
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DR EMBL; X89968; CAA62005.1; -; mRNA.
DR EMBL; BC063156; AAH63156.1; -; mRNA.
DR PIR; S58285; S58285.
DR RefSeq; NP_542152.1; NM_080585.1.
DR PDB; 3J96; EM; 7.60 A; G/H/I/J=1-295.
DR PDB; 3J97; EM; 7.80 A; G/H/I/J=1-295.
DR PDB; 3J98; EM; 8.40 A; G/H/I/J=1-295.
DR PDB; 3J99; EM; 8.20 A; G/H/I/J=1-295.
DR PDB; 6MDM; EM; 4.40 A; K/L=1-295.
DR PDB; 6MDN; EM; 4.40 A; K/L=1-278.
DR PDBsum; 3J96; -.
DR PDBsum; 3J97; -.
DR PDBsum; 3J98; -.
DR PDBsum; 3J99; -.
DR PDBsum; 6MDM; -.
DR PDBsum; 6MDN; -.
DR AlphaFoldDB; P54921; -.
DR SMR; P54921; -.
DR BioGRID; 250832; 4.
DR CORUM; P54921; -.
DR DIP; DIP-37030N; -.
DR IntAct; P54921; 9.
DR MINT; P54921; -.
DR STRING; 10116.ENSRNOP00000002044; -.
DR iPTMnet; P54921; -.
DR PhosphoSitePlus; P54921; -.
DR jPOST; P54921; -.
DR PaxDb; P54921; -.
DR PRIDE; P54921; -.
DR GeneID; 140673; -.
DR KEGG; rno:140673; -.
DR UCSC; RGD:620855; rat.
DR CTD; 8775; -.
DR RGD; 620855; Napa.
DR VEuPathDB; HostDB:ENSRNOG00000001494; -.
DR eggNOG; KOG1586; Eukaryota.
DR HOGENOM; CLU_046329_0_2_1; -.
DR InParanoid; P54921; -.
DR OMA; NVEAYTD; -.
DR OrthoDB; 1191204at2759; -.
DR PhylomeDB; P54921; -.
DR TreeFam; TF316547; -.
DR Reactome; R-RNO-204005; COPII-mediated vesicle transport.
DR Reactome; R-RNO-432722; Golgi Associated Vesicle Biogenesis.
DR Reactome; R-RNO-6807878; COPI-mediated anterograde transport.
DR Reactome; R-RNO-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-RNO-6811438; Intra-Golgi traffic.
DR Reactome; R-RNO-6811440; Retrograde transport at the Trans-Golgi-Network.
DR PRO; PR:P54921; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000001494; Expressed in cerebellum and 20 other tissues.
DR Genevisible; P54921; RN.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
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:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; IDA:ParkinsonsUK-UCL.
DR GO; GO:0005483; F:soluble NSF attachment protein activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IDA:UniProtKB.
DR GO; GO:0045176; P:apical protein localization; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0006886; P:intracellular protein transport; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; NAS:RGD.
DR GO; GO:0030182; P:neuron differentiation; ISO:RGD.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:UniProtKB.
DR GO; GO:0032984; P:protein-containing complex disassembly; IDA:UniProtKB.
DR GO; GO:0010807; P:regulation of synaptic vesicle priming; ISO:RGD.
DR GO; GO:0035494; P:SNARE complex disassembly; ISO:RGD.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; ISO:RGD.
DR GO; GO:0016082; P:synaptic vesicle priming; ISO:RGD.
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 3D-structure; Acetylation; Cell membrane; ER-Golgi transport; Membrane;
KW Phosphoprotein; Protein transport; Reference proteome; Transport.
FT CHAIN 1..295
FT /note="Alpha-soluble NSF attachment protein"
FT /id="PRO_0000219058"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P54920"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DB05"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54920"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P54920"
SQ SEQUENCE 295 AA; 33193 MW; 662356859DF0BA3F CRC64;
MDTSGKQAEA 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 ESVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR
