SNP23_HUMAN
ID SNP23_HUMAN Reviewed; 211 AA.
AC O00161; O00162; Q13602; Q6IAE3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Synaptosomal-associated protein 23;
DE Short=SNAP-23;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN Name=SNAP23;
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] (ISOFORM SNAP-23A).
RC TISSUE=B-cell;
RX PubMed=8663154; DOI=10.1074/jbc.271.23.13300;
RA Ravichandran V., Chawla A., Roche P.A.;
RT "Identification of a novel syntaxin- and synaptobrevin/VAMP-binding
RT protein, SNAP-23, expressed in non-neuronal tissues.";
RL J. Biol. Chem. 271:13300-13303(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
RC TISSUE=Neutrophil;
RX PubMed=9070898; DOI=10.1006/bbrc.1997.6196;
RA Mollinedo F., Lazo P.A.;
RT "Identification of two isoforms of the vesicle-membrane fusion protein
RT SNAP-23 in human neutrophils and HL-60 cells.";
RL Biochem. Biophys. Res. Commun. 231:808-812(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RX PubMed=11354632; DOI=10.1007/s004390100480;
RA Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J.,
RA Nabokina S.M., Mollinedo F., Estivill X.;
RT "Genomic organization, chromosomal localization, alternative splicing, and
RT isoforms of human Synaptosome associated protein-23 gene implicated in
RT vesicle-membrane fusion.";
RL Hum. Genet. 108:211-215(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
RC TISSUE=Cervix, Placenta, and Testis;
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 PROTEIN SEQUENCE OF 1-12, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [8]
RP PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
RX PubMed=12130530; DOI=10.1182/blood.v100.3.1081;
RA Polgar J., Chung S.H., Reed G.L.;
RT "Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in
RT human platelets and are required for granule secretion.";
RL Blood 100:1081-1083(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
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 [14]
RP PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
RX PubMed=21044946; DOI=10.1194/jlr.d011106;
RA Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,
RA Stamler J.S., Casey P.J.;
RT "Site-specific analysis of protein S-acylation by resin-assisted capture.";
RL J. Lipid Res. 52:393-398(2011).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-34 AND SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5; SER-6; SER-20; SER-34 AND
RP SER-110, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-110 AND SER-161, AND
RP IDENTIFICATION BY 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 [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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).
RN [21]
RP INTERACTION WITH ZDHHC17.
RX PubMed=28882895; DOI=10.1074/jbc.m117.799650;
RA Lemonidis K., MacLeod R., Baillie G.S., Chamberlain L.H.;
RT "Peptide array based screening reveals a large number of proteins
RT interacting with the ankyrin repeat domain of the zDHHC17 S-
RT acyltransferase.";
RL J. Biol. Chem. 292:17190-17202(2017).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN, AND
RP SUBUNIT.
RX PubMed=12556468; DOI=10.1074/jbc.m210483200;
RA Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.;
RT "Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain.";
RL J. Biol. Chem. 278:13462-13467(2003).
CC -!- FUNCTION: Essential component of the high affinity receptor for the
CC general membrane fusion machinery and an important regulator of
CC transport vesicle docking and fusion.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3 (PubMed:12556468). Found in a
CC complex with VAMP8 and STX1A (PubMed:12130530). Found in a complex with
CC VAMP8 and STX4 in pancreas (By similarity). Interacts simultaneously
CC with SNAPIN and SYN4 (By similarity). Interacts with STX1A (By
CC similarity). Interacts with STX12 (By similarity). Interacts tightly to
CC multiple syntaxins and synaptobrevins/VAMPs (By similarity). Interacts
CC with ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17
CC (via ANK repeats) (PubMed:28882895). {ECO:0000250|UniProtKB:O09044,
CC ECO:0000250|UniProtKB:O70377, ECO:0000269|PubMed:12130530,
CC ECO:0000269|PubMed:12556468, ECO:0000269|PubMed:28882895}.
CC -!- INTERACTION:
CC O00161; P54920: NAPA; NbExp=3; IntAct=EBI-745000, EBI-749652;
CC O00161; Q9H115: NAPB; NbExp=3; IntAct=EBI-745000, EBI-3921185;
CC O00161; O75558: STX11; NbExp=10; IntAct=EBI-745000, EBI-714135;
CC O00161; Q15836: VAMP3; NbExp=2; IntAct=EBI-745000, EBI-722343;
CC O00161; Q8IUH5: ZDHHC17; NbExp=4; IntAct=EBI-745000, EBI-524753;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. Cell
CC membrane; Lipid-anchor. Synapse, synaptosome. Note=Mainly localized to
CC the plasma membrane.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=SNAP-23a;
CC IsoId=O00161-1; Sequence=Displayed;
CC Name=SNAP-23b;
CC IsoId=O00161-2; Sequence=VSP_006187, VSP_006188;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highest levels where found in placenta.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; U55936; AAC50537.1; -; mRNA.
DR EMBL; Y09567; CAA70760.1; -; mRNA.
DR EMBL; Y09568; CAA70761.1; -; mRNA.
DR EMBL; AJ011915; CAA09864.1; -; mRNA.
DR EMBL; AJ278972; CAC07504.1; -; Genomic_DNA.
DR EMBL; AJ278973; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; AJ278974; CAC07504.1; JOINED; Genomic_DNA.
DR EMBL; BT006916; AAP35562.1; -; mRNA.
DR EMBL; CR457212; CAG33493.1; -; mRNA.
DR EMBL; BC000148; AAH00148.1; -; mRNA.
DR EMBL; BC003686; AAH03686.1; -; mRNA.
DR EMBL; BC022890; AAH22890.1; -; mRNA.
DR CCDS; CCDS10087.1; -. [O00161-1]
DR CCDS; CCDS10088.1; -. [O00161-2]
DR PIR; JC5296; JC5296.
DR PIR; JC5297; JC5297.
DR RefSeq; NP_003816.2; NM_003825.3. [O00161-1]
DR RefSeq; NP_570710.1; NM_130798.2. [O00161-2]
DR PDB; 1NHL; X-ray; 2.30 A; A=23-76.
DR PDB; 3ZUS; X-ray; 2.95 A; A/B/C/D=150-211.
DR PDBsum; 1NHL; -.
DR PDBsum; 3ZUS; -.
DR AlphaFoldDB; O00161; -.
DR SMR; O00161; -.
DR BioGRID; 114303; 166.
DR CORUM; O00161; -.
DR IntAct; O00161; 59.
DR MINT; O00161; -.
DR STRING; 9606.ENSP00000249647; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR iPTMnet; O00161; -.
DR MetOSite; O00161; -.
DR PhosphoSitePlus; O00161; -.
DR SwissPalm; O00161; -.
DR BioMuta; SNAP23; -.
DR OGP; O00161; -.
DR EPD; O00161; -.
DR jPOST; O00161; -.
DR MassIVE; O00161; -.
DR MaxQB; O00161; -.
DR PaxDb; O00161; -.
DR PeptideAtlas; O00161; -.
DR PRIDE; O00161; -.
DR ProteomicsDB; 47748; -. [O00161-1]
DR ProteomicsDB; 47749; -. [O00161-2]
DR Antibodypedia; 712; 431 antibodies from 36 providers.
DR DNASU; 8773; -.
DR Ensembl; ENST00000249647.8; ENSP00000249647.3; ENSG00000092531.10. [O00161-1]
DR Ensembl; ENST00000349777.5; ENSP00000207062.1; ENSG00000092531.10. [O00161-2]
DR Ensembl; ENST00000397138.5; ENSP00000380327.1; ENSG00000092531.10. [O00161-2]
DR GeneID; 8773; -.
DR KEGG; hsa:8773; -.
DR MANE-Select; ENST00000249647.8; ENSP00000249647.3; NM_003825.4; NP_003816.2.
DR UCSC; uc001zpz.3; human. [O00161-1]
DR CTD; 8773; -.
DR DisGeNET; 8773; -.
DR GeneCards; SNAP23; -.
DR HGNC; HGNC:11131; SNAP23.
DR HPA; ENSG00000092531; Low tissue specificity.
DR MIM; 602534; gene.
DR neXtProt; NX_O00161; -.
DR OpenTargets; ENSG00000092531; -.
DR PharmGKB; PA35979; -.
DR VEuPathDB; HostDB:ENSG00000092531; -.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; O00161; -.
DR OMA; NYAVHKA; -.
DR OrthoDB; 1358184at2759; -.
DR PhylomeDB; O00161; -.
DR TreeFam; TF315125; -.
DR PathwayCommons; O00161; -.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1445148; Translocation of SLC2A4 (GLUT4) to the plasma membrane.
DR Reactome; R-HSA-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; O00161; -.
DR SIGNOR; O00161; -.
DR BioGRID-ORCS; 8773; 425 hits in 1091 CRISPR screens.
DR ChiTaRS; SNAP23; human.
DR EvolutionaryTrace; O00161; -.
DR GeneWiki; SNAP23; -.
DR GenomeRNAi; 8773; -.
DR Pharos; O00161; Tbio.
DR PRO; PR:O00161; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O00161; protein.
DR Bgee; ENSG00000092531; Expressed in monocyte and 203 other tissues.
DR ExpressionAtlas; O00161; baseline and differential.
DR Genevisible; O00161; HS.
DR GO; GO:0005912; C:adherens junction; IDA:BHF-UCL.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IDA:CACAO.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0030670; C:phagocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IPI:UniProtKB.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0002553; P:histamine secretion by mast cell; IMP:UniProtKB.
DR GO; GO:0061025; P:membrane fusion; TAS:ProtInc.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR GO; GO:0016082; P:synaptic vesicle priming; IBA:GO_Central.
DR GO; GO:0006906; P:vesicle fusion; IBA:GO_Central.
DR GO; GO:0006903; P:vesicle targeting; TAS:ProtInc.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR Pfam; PF00835; SNAP-25; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Synapse;
KW Synaptosome; Transport.
FT CHAIN 1..211
FT /note="Synaptosomal-associated protein 23"
FT /id="PRO_0000213598"
FT DOMAIN 14..76
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 146..208
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..76
FT /evidence="ECO:0000269|PubMed:12556468"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.8,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 6
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09044"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 79
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 80
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 83
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 87
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT LIPID 112
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000269|PubMed:21044946"
FT VAR_SEQ 89
FT /note="R -> S (in isoform SNAP-23b)"
FT /evidence="ECO:0000303|PubMed:9070898"
FT /id="VSP_006187"
FT VAR_SEQ 90..142
FT /note="Missing (in isoform SNAP-23b)"
FT /evidence="ECO:0000303|PubMed:9070898"
FT /id="VSP_006188"
FT CONFLICT 135
FT /note="A -> V (in Ref. 1; AAC50537)"
FT /evidence="ECO:0000305"
FT HELIX 24..74
FT /evidence="ECO:0007829|PDB:1NHL"
SQ SEQUENCE 211 AA; 23354 MW; AC378E9786C3A239 CRC64;
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ
NPQIKRITDK ADTNRDRIDI ANARAKKLID S
