ID   SNAA_BOVIN              Reviewed;         295 AA.
AC   P81125;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 105.
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   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, PARTIAL PROTEIN SEQUENCE, FUNCTION, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=8455721; DOI=10.1038/362353a0;
RA   Whiteheart S.W., Griff I.C., Brunner M., Clary D.O., Mayer T., Buhrow S.A.,
RA   Rothman J.E.;
RT   "SNAP family of NSF attachment proteins includes a brain-specific
RT   isoform.";
RL   Nature 362:353-355(1993).
CC   -!- FUNCTION: Required for vesicular transport between the endoplasmic
CC       reticulum and the Golgi apparatus (PubMed:8455721). Together with GNA12
CC       promotes CDH5 localization to plasma membrane (By similarity).
CC       {ECO:0000250|UniProtKB:P54920, ECO:0000269|PubMed:8455721}.
CC   -!- SUBUNIT: Interacts with PRKCABP, and disrupts the interaction between
CC       GRIA2 and PRKCABP, leading to the internalization of GRIA2. Found in a
CC       complex with VAMP8. Component of a SNARE-like complex that contains at
CC       least ZW10, USE1L, RINT1, STX18 and NAPA/SNAP-alpha. Interacts with
CC       VTI1A. Interacts with STX12. Interacts with GNA12 (via N-terminus); the
CC       interaction promotes CDH5 localization to plasma membrane.
CC       {ECO:0000250|UniProtKB:P54920, ECO:0000250|UniProtKB:P54921,
CC       ECO:0000250|UniProtKB:Q9DB05}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P54920};
CC       Peripheral membrane protein {ECO:0000250|UniProtKB:P54920}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Highest expression in brain.
CC       {ECO:0000269|PubMed:8455721}.
CC   -!- SIMILARITY: Belongs to the SNAP family. {ECO:0000305}.
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DR   PIR; S32367; S32367.
DR   PDB; 6IP1; EM; 3.90 A; E/F/G/H=1-295.
DR   PDBsum; 6IP1; -.
DR   AlphaFoldDB; P81125; -.
DR   SMR; P81125; -.
DR   DIP; DIP-61490N; -.
DR   IntAct; P81125; 1.
DR   STRING; 9913.ENSBTAP00000017397; -.
DR   PaxDb; P81125; -.
DR   PRIDE; P81125; -.
DR   eggNOG; KOG1586; Eukaryota.
DR   InParanoid; P81125; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0045202; C:synapse; IEA:GOC.
DR   GO; GO:0070044; C:synaptobrevin 2-SNAP-25-syntaxin-1a complex; IBA:GO_Central.
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:0006886; P:intracellular protein transport; IBA:GO_Central.
DR   GO; GO:0010807; P:regulation of synaptic vesicle priming; IBA:GO_Central.
DR   GO; GO:0035494; P:SNARE complex disassembly; IMP:CAFA.
DR   GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
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; Direct protein sequencing;
KW   ER-Golgi transport; Membrane; Phosphoprotein; Protein transport;
KW   Reference proteome; Transport.
FT   CHAIN           1..295
FT                   /note="Alpha-soluble NSF attachment protein"
FT                   /id="PRO_0000219055"
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;  33225 MW;  0453C5457D147E40 CRC64;
     MDNSGKEAEA MALLAEAERK VKNSQSFFSG LFGGSSKIEE ACEIYARAAN MFKMAKNWSA
     AGSAFCQAAH VHLQLQSKHD AATCFVDAGN AFKKADPQEA INCLMRAIEI YTDMGRFTIA
     AKHHISIAEI YETELVDIEK AIAHYEQSAD YYKGEESNSS ANKCLLKVAG YAAQLEQYQK
     AIDIYEQVGT NAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AKLAVQKYEE LFPAFSDSRE
     CKRIKKLLEA HEEQNVDSYT EAVKEYDSIS RLDQWLTTML LRIKKTIQGD EEDLR