ID A0A3Q3AZ41_KRYMA Unreviewed; 213 AA.
AC A0A3Q3AZ41;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 18-JUN-2025, entry version 31.
DE RecName: Full=Synaptosomal-associated protein {ECO:0000256|RuleBase:RU003496};
OS Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000016849.1, ECO:0000313|Proteomes:UP000264800};
RN [1] {ECO:0000313|Ensembl:ENSKMAP00000016849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) 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:0000256|ARBA:ARBA00053876}.
CC -!- SUBUNIT: Homotetramer (via coiled-coil domain), also forms
CC heterotetramers with STX4 and VAMP3. Found in a complex with VAMP8 and
CC STX1A. Found in a complex with VAMP8 and STX4 in pancreas. Interacts
CC simultaneously with SNAPIN and SYN4. Interacts with STX1A. Interacts
CC with STX12. Interacts tightly to multiple syntaxins and
CC synaptobrevins/VAMPs. Interacts with ZDHHC13 (via ANK repeats).
CC Interacts with ZDHHC17 (via ANK repeats).
CC {ECO:0000256|ARBA:ARBA00065910}.
CC -!- SUBCELLULAR LOCATION: Synapse, synaptosome
CC {ECO:0000256|ARBA:ARBA00034102}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family.
CC {ECO:0000256|ARBA:ARBA00009480, ECO:0000256|RuleBase:RU003496}.
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DR RefSeq; XP_017277093.1; XM_017421604.3.
DR AlphaFoldDB; A0A3Q3AZ41; -.
DR STRING; 37003.ENSKMAP00000016849; -.
DR Ensembl; ENSKMAT00000017083.1; ENSKMAP00000016849.1; ENSKMAG00000012575.1.
DR GeneID; 108239098; -.
DR GeneTree; ENSGT00950000182843; -.
DR OMA; ADMTNPF; -.
DR OrthoDB; 19261at2759; -.
DR Proteomes; UP000264800; Unplaced.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; IEA:TreeGrafter.
DR GO; GO:0005484; F:SNAP receptor activity; IEA:TreeGrafter.
DR GO; GO:0019905; F:syntaxin binding; IEA:TreeGrafter.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IEA:TreeGrafter.
DR GO; GO:0016082; P:synaptic vesicle priming; IEA:TreeGrafter.
DR CDD; cd15889; SNARE_SNAP25N_23N; 1.
DR FunFam; 1.20.5.110:FF:000007; Synaptosomal-associated protein; 1.
DR FunFam; 1.20.5.110:FF:000018; Synaptosomal-associated protein; 1.
DR Gene3D; 1.20.5.110; -; 2.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305; SYNAPTOSOMAL ASSOCIATED PROTEIN; 1.
DR PANTHER; PTHR19305:SF4; SYNAPTOSOMAL-ASSOCIATED PROTEIN 23; 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 Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW Reference proteome {ECO:0000313|Proteomes:UP000264800};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Synapse {ECO:0000256|ARBA:ARBA00023018};
KW Synaptosome {ECO:0000256|ARBA:ARBA00022599}.
FT DOMAIN 14..76
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 149..211
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 45..79
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 213 AA; 23736 MW; BDC930274CBF35F0 CRC64;
MEDMSVEQMA VRANQVTDES LESTRRMLQM AEESKQTGAN TMVMLDQQGE QLRRIEDGMD
QINEDMKQAD KNLTDLSKCC GLCVCPCDRA NSVENDQRYK RTWGTGTEDG DGSNSKVVSR
QPSAVRNGQA SQVQAPAPSG PYIKRITNDA REDEMEENLE VVGSIIGNLK DMAVNMGSEI
DKQNTQIDRI TDKADMNKVR IDVANDRANK LIK
//