ID A0A2R8ZYH0_PANPA Unreviewed; 201 AA.
AC A0A2R8ZYH0;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|RuleBase:RU003496, ECO:0000256|RuleBase:RU369075};
DE Includes:
DE RecName: Full=Synaptosomal-associated protein 25 {ECO:0000256|RuleBase:RU369075};
DE Short=SNAP-25 {ECO:0000256|RuleBase:RU369075};
DE Includes:
DE RecName: Full=Synaptosomal-associated protein {ECO:0000256|RuleBase:RU003496};
GN Name=SNAP25 {ECO:0000313|Ensembl:ENSPPAP00000009617.1};
OS Pan paniscus (Pygmy chimpanzee) (Bonobo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9597 {ECO:0000313|Ensembl:ENSPPAP00000009617.1, ECO:0000313|Proteomes:UP000240080};
RN [1] {ECO:0000313|Ensembl:ENSPPAP00000009617.1, ECO:0000313|Proteomes:UP000240080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22722832; DOI=10.1038/nature11128;
RA Prufer K., Munch K., Hellmann I., Akagi K., Miller J.R., Walenz B.,
RA Koren S., Sutton G., Kodira C., Winer R., Knight J.R., Mullikin J.C.,
RA Meader S.J., Ponting C.P., Lunter G., Higashino S., Hobolth A., Dutheil J.,
RA Karakoc E., Alkan C., Sajjadian S., Catacchio C.R., Ventura M.,
RA Marques-Bonet T., Eichler E.E., Andre C., Atencia R., Mugisha L.,
RA Junhold J., Patterson N., Siebauer M., Good J.M., Fischer A., Ptak S.E.,
RA Lachmann M., Symer D.E., Mailund T., Schierup M.H., Andres A.M., Kelso J.,
RA Paabo S.;
RT "The bonobo genome compared with the chimpanzee and human genomes.";
RL Nature 486:527-531(2012).
RN [2] {ECO:0000313|Ensembl:ENSPPAP00000009617.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: t-SNARE involved in the molecular regulation of
CC neurotransmitter release. Plays an important role in the synaptic
CC function of specific neuronal systems. Associates with proteins
CC involved in vesicle docking and membrane fusion. Regulates plasma
CC membrane recycling through its interaction with CENPF. Modulates the
CC gating characteristics of the delayed rectifier voltage-dependent
CC potassium channel KCNB1 in pancreatic beta cells.
CC {ECO:0000256|RuleBase:RU369075}.
CC -!- SUBUNIT: Part of the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A; this complex binds CPLX1. Found in a complex containing SYT1,
CC SV2B and syntaxin-1. Found in a ternary complex with STX1A and VAMP8.
CC Interacts with HSC70 and with SYT9, forming a complex with DNAJC5. The
CC interaction with SYT9 is inhibited in presence of calcium. Isoform 1
CC and isoform 2 interact with BLOC1S6. Interacts with CENPF. Interacts
CC with EQTN. Interacts with HGS. Interacts with KCNB1 (via N-terminus);
CC reduces the voltage-dependent potassium channel KCNB1 activity in
CC pancreatic beta cells. Interacts with OTOF. Interacts with RIMS1.
CC Interacts with SNAPIN. Interacts with STXBP6. Interacts with TRIM9.
CC Interacts with ZDHHC13 (via ANK repeats). Interacts with ZDHHC17 (via
CC ANK repeats). Associates with the BLOC-1 complex. Interacts with PLCL1
CC (via C2 domain). Interacts with PRRT2; this interaction may impair the
CC formation of the SNARE complex. Interacts with alpha-synuclein/SNCA.
CC Interacts with PRPH2. Interacts with ROM1. Interacts with STX3.
CC {ECO:0000256|RuleBase:RU369075}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004193,
CC ECO:0000256|RuleBase:RU369075}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004193}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}. Photoreceptor inner segment
CC {ECO:0000256|ARBA:ARBA00004437}. Synapse, synaptosome
CC {ECO:0000256|RuleBase:RU369075}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC {ECO:0000256|ARBA:ARBA00009480, ECO:0000256|RuleBase:RU003496}.
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DR EMBL; AJFE02032707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2R8ZYH0; -.
DR Ensembl; ENSPPAT00000032260.1; ENSPPAP00000009617.1; ENSPPAG00000028032.1.
DR GeneTree; ENSGT00950000182843; -.
DR Proteomes; UP000240080; Chromosome 20.
DR Bgee; ENSPPAG00000028032; Expressed in cerebellum and 6 other cell types or tissues.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0001917; C:photoreceptor inner segment; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031201; C:SNARE complex; IEA:UniProt.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0017075; F:syntaxin-1 binding; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; IEA:UniProt.
DR CDD; cd15885; SNARE_SNAP25C; 1.
DR CDD; cd15894; SNARE_SNAP25N; 1.
DR Gene3D; 1.20.5.110; -; 2.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR039077; SNAP-25_N_SNARE_chord.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR19305:SF5; SYNAPTOSOMAL-ASSOCIATED PROTEIN 25; 1.
DR Pfam; PF00835; SNAP-25; 1.
DR SMART; SM00397; t_SNARE; 2.
DR SUPFAM; SSF58038; SNARE fusion complex; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU369075};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU369075};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369075};
KW Reference proteome {ECO:0000313|Proteomes:UP000240080};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU369075};
KW Synapse {ECO:0000256|ARBA:ARBA00023018, ECO:0000256|RuleBase:RU369075};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599, ECO:0000256|RuleBase:RU369075}.
FT DOMAIN 32..76
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 135..197
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 52..79
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 201 AA; 22633 MW; 5FE764E88AA63A26 CRC64;
MAEDADMRNE LEEMQRRADQ LADEVRSGDL GRESKDAGIR TLVMLDEQGE QLDRVEEGMN
HINQDMKEAE KNLKDLGKCC GLFICPCNKL KSSDAYKKAW GNNQDGVVAS QPARVVDERE
QMAISGGFIR RVTNDARENE MDENLEQVSG IIGNLRHMAL DMGNEIDTQN RQIDRIMEKA
DSNKTRIDEA NQRATKMLGS G
//
