ID A0A4W3H3N1_CALMI Unreviewed; 207 AA.
AC A0A4W3H3N1;
DT 18-SEP-2019, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:ENSCMIP00000011398.1};
OS Callorhinchus milii (Ghost shark).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Chondrichthyes;
OC Holocephali; Chimaeriformes; Callorhinchidae; Callorhinchus.
OX NCBI_TaxID=7868 {ECO:0000313|Ensembl:ENSCMIP00000011398.1, ECO:0000313|Proteomes:UP000314986};
RN [1] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17185593; DOI=10.1126/science.1130708;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Ancient noncoding elements conserved in the human genome.";
RL Science 314:1892-1892(2006).
RN [2] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17407382;
RA Venkatesh B., Kirkness E.F., Loh Y.H., Halpern A.L., Lee A.P., Johnson J.,
RA Dandona N., Viswanathan L.D., Tay A., Venter J.C., Strausberg R.L.,
RA Brenner S.;
RT "Survey sequencing and comparative analysis of the elephant shark
RT (Callorhinchus milii) genome.";
RL PLoS Biol. 5:E101-E101(2007).
RN [3] {ECO:0000313|Proteomes:UP000314986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24402279; DOI=10.1038/nature12826;
RG International Elephant Shark Genome Sequencing Consortium;
RA Venkatesh B., Lee A.P., Ravi V., Maurya A.K., Lian M.M., Swann J.B.,
RA Ohta Y., Flajnik M.F., Sutoh Y., Kasahara M., Hoon S., Gangu V., Roy S.W.,
RA Irimia M., Korzh V., Kondrychyn I., Lim Z.W., Tay B.H., Tohari S.,
RA Kong K.W., Ho S., Lorente-Galdos B., Quilez J., Marques-Bonet T.,
RA Raney B.J., Ingham P.W., Tay A., Hillier L.W., Minx P., Boehm T.,
RA Wilson R.K., Brenner S., Warren W.C.;
RT "Elephant shark genome provides unique insights into gnathostome
RT evolution.";
RL Nature 505:174-179(2014).
RN [4] {ECO:0000313|Ensembl:ENSCMIP00000011398.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
CC -!- FUNCTION: Plays an important role in the synaptic function of specific
CC neuronal systems. Associates with proteins involved in vesicle docking
CC and membrane fusion. {ECO:0000256|RuleBase:RU369075}.
CC -!- SUBCELLULAR LOCATION: Synapse, synaptosome
CC {ECO:0000256|RuleBase:RU369075}. Cell membrane
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 RefSeq; XP_007903664.1; XM_007905473.1.
DR AlphaFoldDB; A0A4W3H3N1; -.
DR Ensembl; ENSCMIT00000011679.1; ENSCMIP00000011398.1; ENSCMIG00000005925.1.
DR GeneID; 103186434; -.
DR CTD; 30712; -.
DR GeneTree; ENSGT00950000182843; -.
DR OrthoDB; 388796at2759; -.
DR Proteomes; UP000314986; Unassembled WGS sequence.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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:UP000314986};
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 19..81
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT DOMAIN 141..203
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 23291 MW; 334B81D609436082 CRC64;
MADETDMRSE LENMQQRAGQ VADESLESTR RMLQMVEESK DAGIRTLVML DEQGEQLDRV
EDGMNHINQD MKEAEKTLTD LGKCCGLFIC PCNKLKSSDA YKKAWGNNQD GVVASQPAAR
VMDEREQMAI SGGFIRRVTN DARENEMDEN LEQVSGIIGN LRHMALDMGN EIDTQNRQVD
RIMEKAESNK TRIDEANQRA TKMLGSG
//
