SNP23_RAT
ID SNP23_RAT Reviewed; 210 AA.
AC O70377; A0JPL8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Synaptosomal-associated protein 23;
DE Short=SNAP-23;
DE AltName: Full=Vesicle-membrane fusion protein SNAP-23;
GN Name=Snap23;
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].
RX PubMed=10051443; DOI=10.1042/bj3380709;
RA St Denis J.-F., Cabaniols J.-P., Cushman S.W., Roche P.A.;
RT "SNAP-23 participates in SNARE complex assembly in rat adipose cells.";
RL Biochem. J. 338:709-715(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 SNARE COMPLEX CHARACTERIZATION.
RX PubMed=14993220; DOI=10.1074/jbc.m400798200;
RA Rao S.K., Huynh C., Proux-Gillardeaux V., Galli T., Andrews N.W.;
RT "Identification of SNAREs involved in synaptotagmin VII-regulated lysosomal
RT exocytosis.";
RL J. Biol. Chem. 279:20471-20479(2004).
RN [4]
RP PROTEIN SEQUENCE OF 55-64, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RA Lubec G., Kang S.U., Lubec S.;
RL Submitted (SEP-2007) to UniProtKB.
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. {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3 (By similarity). Found in a complex
CC with VAMP8 and STX1A (By similarity). Found in a complex with VAMP8 and
CC STX4 in pancreas (By similarity). Interacts simultaneously with SNAPIN
CC and SYN4 (By similarity). Interacts with STX1A (By similarity).
CC Interacts with STX12 (By similarity). Interacts tightly to multiple
CC syntaxins and synaptobrevins/VAMPs (PubMed:14993220). Interacts with
CC ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17 (via
CC ANK repeats) (By similarity). {ECO:0000250|UniProtKB:O00161,
CC ECO:0000250|UniProtKB:O09044, ECO:0000269|PubMed:14993220}.
CC -!- INTERACTION:
CC O70377; Q9QY78: Ikbkb; NbExp=2; IntAct=EBI-1573765, EBI-1812464;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor
CC {ECO:0000250}. Synapse, synaptosome {ECO:0000250}. Cytoplasmic vesicle
CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
CC Note=Mainly localized to the plasma membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000305}.
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DR EMBL; AF052596; AAC06031.1; -; mRNA.
DR EMBL; BC127494; AAI27495.1; -; mRNA.
DR RefSeq; NP_073180.1; NM_022689.2.
DR AlphaFoldDB; O70377; -.
DR SMR; O70377; -.
DR BioGRID; 249168; 2.
DR CORUM; O70377; -.
DR IntAct; O70377; 7.
DR MINT; O70377; -.
DR iPTMnet; O70377; -.
DR PhosphoSitePlus; O70377; -.
DR PRIDE; O70377; -.
DR Ensembl; ENSRNOT00000096953; ENSRNOP00000091304; ENSRNOG00000050552.
DR GeneID; 64630; -.
DR KEGG; rno:64630; -.
DR UCSC; RGD:620221; rat.
DR CTD; 8773; -.
DR RGD; 620221; Snap23.
DR GeneTree; ENSGT00950000182843; -.
DR InParanoid; O70377; -.
DR OrthoDB; 1358184at2759; -.
DR PhylomeDB; O70377; -.
DR Reactome; R-RNO-1236974; ER-Phagosome pathway.
DR Reactome; R-RNO-199992; trans-Golgi Network Vesicle Budding.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013026; RHOB GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013406; RHOQ GTPase cycle.
DR Reactome; R-RNO-9013409; RHOJ GTPase cycle.
DR Reactome; R-RNO-9013423; RAC3 GTPase cycle.
DR Reactome; R-RNO-9035034; RHOF GTPase cycle.
DR PRO; PR:O70377; -.
DR Proteomes; UP000002494; Chromosome 3.
DR GO; GO:0005912; C:adherens junction; ISO:RGD.
DR GO; GO:0042582; C:azurophil granule; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0098982; C:GABA-ergic synapse; IDA:SynGO.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0098794; C:postsynapse; IDA:SynGO.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; ISO:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005484; F:SNAP receptor activity; IDA:FlyBase.
DR GO; GO:0019905; F:syntaxin binding; IPI:RGD.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0006887; P:exocytosis; ISO:RGD.
DR GO; GO:0002553; P:histamine secretion by mast cell; ISO:RGD.
DR GO; GO:0061025; P:membrane fusion; IDA:RGD.
DR GO; GO:0015031; P:protein transport; IMP:RGD.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:RGD.
DR GO; GO:0017157; P:regulation of exocytosis; IMP:RGD.
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:0016192; P:vesicle-mediated transport; IMP:RGD.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
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 Acetylation; Cell membrane; Coiled coil; Cytoplasmic vesicle;
KW Direct protein sequencing; Lipoprotein; Membrane; Palmitate;
KW Phosphoprotein; Protein transport; Reference proteome; Repeat; Synapse;
KW Synaptosome; Transport.
FT CHAIN 1..210
FT /note="Synaptosomal-associated protein 23"
FT /id="PRO_0000213600"
FT DOMAIN 14..76
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 145..207
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 104..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..76
FT /evidence="ECO:0000250"
FT COMPBIAS 105..136
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O09044"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00161"
FT LIPID 79
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 80
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 83
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 85
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
FT LIPID 87
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 210 AA; 23235 MW; 0D63E3A6F9FE3BA2 CRC64;
MDDLSPEEIQ LRAHQVTDES LESTRRILGL AIESQDAGIK TITMLDEQGE QLNRIEEGMD
QINKDMREAE KTLTELNKCC GLCVCPCNRT KNFESGKNYK ATWGDGGDSS PSNVVSKQPS
RITNGQPQQT TGAASGGYIK RITNDAREDE MEENLTQVGS ILGNLKNMAL DMGNEIDAQN
QQIQKITEKA DTNKNRIDIA NTRAKKLIDS
