LOCUS       NP_073180                210 aa            linear   ROD 24-APR-2024
DEFINITION  synaptosomal-associated protein 23 isoform 1 [Rattus norvegicus].
ACCESSION   NP_073180
VERSION     NP_073180.1
DBSOURCE    REFSEQ: accession NM_022689.2
KEYWORDS    RefSeq.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 210)
  AUTHORS   Chen,J., Wang,Z., Wang,T., Cheng,J., Zhuang,R. and Wang,W.
  TITLE     SNAP23 decreases insulin secretion by competitively inhibiting the
            interaction between SNAP25 and STX1A
  JOURNAL   Biosci Rep 43 (5) (2023)
   PUBMED   37057886
  REMARK    GeneRIF: SNAP23 decreases insulin secretion by competitively
            inhibiting the interaction between SNAP25 and STX1A.
REFERENCE   2  (residues 1 to 210)
  AUTHORS   Dolai,S., Takahashi,T., Qin,T., Liang,T., Xie,L., Kang,F.,
            Miao,Y.F., Xie,H., Kang,Y., Manuel,J., Winter,E., Roche,P.A.,
            Cattral,M.S. and Gaisano,H.Y.
  TITLE     Pancreas-specific SNAP23 depletion prevents pancreatitis by
            attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes
  JOURNAL   Autophagy 17 (10), 3068-3081 (2021)
   PUBMED   33213278
  REMARK    GeneRIF: Pancreas-specific SNAP23 depletion prevents pancreatitis
            by attenuating pathological basolateral exocytosis and formation of
            trypsin-activating autolysosomes.
REFERENCE   3  (residues 1 to 210)
  AUTHORS   Serrano-Lopez,E.M., Lopez-Martinez,D., Gomez-Fernandez,J.C.,
            Egea-Jimenez,A.L. and Corbalan-Garcia,S.
  TITLE     PKCepsilon controls the fusion of secretory vesicles in mast cells
            in a phosphatidic acid-dependent mode
  JOURNAL   Int J Biol Macromol 185, 377-389 (2021)
   PUBMED   34147527
  REMARK    GeneRIF: PKCepsilon controls the fusion of secretory vesicles in
            mast cells in a phosphatidic acid-dependent mode.
REFERENCE   4  (residues 1 to 210)
  AUTHORS   Naskar,P., Naqvi,N. and Puri,N.
  TITLE     Blocking dephosphorylation at Serine 120 residue in t-SNARE SNAP-23
            leads to massive inhibition in exocytosis from mast cells
  JOURNAL   J Biosci 43 (1), 127-138 (2018)
   PUBMED   29485121
  REMARK    GeneRIF: Blocking dephosphorylation at serine 120 residue in
            SNAP-23 leads to massive inhibition in exocytosis from mast cells.
REFERENCE   5  (residues 1 to 210)
  AUTHORS   Weber,P., Batoulis,H., Rink,K.M., Dahlhoff,S., Pinkwart,K.,
            Sollner,T.H. and Lang,T.
  TITLE     Electrostatic anchoring precedes stable membrane attachment of
            SNAP25/SNAP23 to the plasma membrane
  JOURNAL   Elife 6, e19394 (2017)
   PUBMED   28240595
  REMARK    GeneRIF: Electrostatic anchoring precedes stable membrane
            attachment of SNAP25 and SNAP23 to the plasma membrane.
            Publication Status: Online-Only
REFERENCE   6  (residues 1 to 210)
  AUTHORS   Rao,S.K., Huynh,C., Proux-Gillardeaux,V., Galli,T. and Andrews,N.W.
  TITLE     Identification of SNAREs involved in synaptotagmin VII-regulated
            lysosomal exocytosis
  JOURNAL   J Biol Chem 279 (19), 20471-20479 (2004)
   PUBMED   14993220
REFERENCE   7  (residues 1 to 210)
  AUTHORS   Abonyo,B.O., Gou,D., Wang,P., Narasaraju,T., Wang,Z. and Liu,L.
  TITLE     Syntaxin 2 and SNAP-23 are required for regulated surfactant
            secretion
  JOURNAL   Biochemistry 43 (12), 3499-3506 (2004)
   PUBMED   15035620
  REMARK    GeneRIF: SNAP-23 is expressed in alveolar type II cells of the
            lung; evidence supports its functional role in exocytosis of lung
            surfactant by alveolar type II cells.
REFERENCE   8  (residues 1 to 210)
  AUTHORS   Banerjee,A., Li,G., Alexander,E.A. and Schwartz,J.H.
  TITLE     Role of SNAP-23 in trafficking of H+-ATPase in cultured inner
            medullary collecting duct cells
  JOURNAL   Am J Physiol Cell Physiol 280 (4), C775-C781 (2001)
   PUBMED   11245593
REFERENCE   9  (residues 1 to 210)
  AUTHORS   Okamoto,M., Schoch,S. and Sudhof,T.C.
  TITLE     EHSH1/intersectin, a protein that contains EH and SH3 domains and
            binds to dynamin and SNAP-25. A protein connection between
            exocytosis and endocytosis?
  JOURNAL   J Biol Chem 274 (26), 18446-18454 (1999)
   PUBMED   10373452
REFERENCE   10 (residues 1 to 210)
  AUTHORS   St-Denis,J.F., Cabaniols,J.P., Cushman,S.W. and Roche,P.A.
  TITLE     SNAP-23 participates in SNARE complex assembly in rat adipose cells
  JOURNAL   Biochem J 338 (Pt 3) (Pt 3), 709-715 (1999)
   PUBMED   10051443
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from BC127494.1.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: BC127494.1, DY319893.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00132261, SAMD00132263
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..210
                     /organism="Rattus norvegicus"
                     /db_xref="taxon:10116"
                     /chromosome="3"
                     /map="3q35"
     Protein         1..210
                     /product="synaptosomal-associated protein 23 isoform 1"
                     /note="SNAP-23; vesicle-membrane fusion protein SNAP-23;
                     synaptosomal-associated protein, 23 kD;
                     synaptosomal-associated protein 23"
                     /calculated_mol_wt=23104
     Site            1
                     /site_type="acetylation"
                     /note="N-acetylmethionine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            5
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          9..75
                     /region_name="SNARE_SNAP23N"
                     /note="N-terminal SNARE motif of SNAP23; cd15895"
                     /db_xref="CDD:277248"
     Site            order(13,16..21,23..28,30..31,34..35,37..42,44..45,47..49,
                     51..56,58..59,61..63,65..66,68..70,72..73,75)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277248"
     Site            20
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            23
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O09044; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            34
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            48
                     /site_type="active"
                     /note="zero layer [active]"
                     /db_xref="CDD:277248"
     Region          86..147
                     /region_name="SNAP-25"
                     /note="SNAP-25 family; pfam00835"
                     /db_xref="CDD:459955"
     Region          104..136
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (O70377.1)"
     Site            110
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Region          148..206
                     /region_name="SNARE_SNAP23C"
                     /note="C-terminal SNARE motif of SNAP23; cd15884"
                     /db_xref="CDD:277237"
     Site            order(148,150..151,154..159,161..162,165..166,168..170,
                     172..173,176..177,179..180,182..187,189..190,193,196,200,
                     203,206)
                     /site_type="other"
                     /note="heterotetramer interface [polypeptide binding]"
                     /db_xref="CDD:277237"
     Site            160
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:O00161; propagated from
                     UniProtKB/Swiss-Prot (O70377.1)"
     Site            179
                     /site_type="other"
                     /note="zero layer"
                     /db_xref="CDD:277237"
     CDS             1..210
                     /gene="Snap23"
                     /coded_by="NM_022689.2:149..781"
                     /note="isoform 1 is encoded by transcript variant 1"
                     /db_xref="GeneID:64630"
                     /db_xref="RGD:620221"
ORIGIN      
        1 mddlspeeiq lrahqvtdes lestrrilgl aiesqdagik titmldeqge qlnrieegmd
       61 qinkdmreae ktltelnkcc glcvcpcnrt knfesgknyk atwgdggdss psnvvskqps
      121 ritngqpqqt tgaasggyik ritndarede meenltqvgs ilgnlknmal dmgneidaqn
      181 qqiqkiteka dtnknridia ntrakklids
//
