SN25B_DANRE
ID SN25B_DANRE Reviewed; 203 AA.
AC Q6PC54; O93579; O93580; Q78CL9; Q9YHT9;
DT 16-DEC-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Synaptosomal-associated protein 25-B {ECO:0000250|UniProtKB:P36978};
DE Short=SNAP-B {ECO:0000250|UniProtKB:P36978};
DE AltName: Full=Synaptosome-associated protein 25.2 {ECO:0000312|EMBL:AAC73006.1};
DE Short=SNAP-25.2 {ECO:0000303|PubMed:9843147};
GN Name=snap25b {ECO:0000312|ZFIN:ZDB-GENE-980526-392};
GN Synonyms=Snap {ECO:0000312|EMBL:AAC73006.1},
GN snap25.2 {ECO:0000303|PubMed:9843147};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC73006.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 57-93
RP (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=9843147;
RX DOI=10.1002/(sici)1097-4547(19981201)54:5<563::aid-jnr1>3.0.co;2-7;
RA Risinger C., Salaneck E., Soederberg C., Gates M., Postlethwait J.H.,
RA Larhammar D.;
RT "Cloning of two loci for synapse protein Snap25 in zebrafish: comparison of
RT paralogous linkage groups suggests loss of one locus in the mammalian
RT lineage.";
RL J. Neurosci. Res. 54:563-573(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAH59469.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Retina {ECO:0000312|EMBL:AAH59469.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play an important role in the synaptic function of
CC specific neuronal systems. Associates with proteins involved in vesicle
CC docking and membrane fusion. {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Synapse, synaptosome
CC {ECO:0000250|UniProtKB:P36978, ECO:0000250|UniProtKB:P60880}. Cell
CC membrane {ECO:0000250|UniProtKB:P60881}. Note=Complexed with
CC macromolecular elements of the nerve terminal.
CC {ECO:0000250|UniProtKB:P36978, ECO:0000250|UniProtKB:P60880}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Isoforms differ by the usage of two alternative homologous
CC exons which code for positions 55 to 94 and differ only in 14
CC positions out of 40.;
CC Name=1 {ECO:0000269|PubMed:9843147};
CC IsoId=Q6PC54-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9843147};
CC IsoId=Q6PC54-2; Sequence=VSP_052975;
CC -!- TISSUE SPECIFICITY: Expressed in several regions throughout the adult
CC brain, including the mesencephalon. {ECO:0000269|PubMed:9843147}.
CC -!- SIMILARITY: Belongs to the SNAP-25 family. {ECO:0000255}.
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DR EMBL; AF091594; AAC64290.1; -; mRNA.
DR EMBL; AF091595; AAC64291.1; -; mRNA.
DR EMBL; AF091596; AAC73006.1; -; Transcribed_RNA.
DR EMBL; AF091596; AAC73007.1; -; Transcribed_RNA.
DR EMBL; BC059469; AAH59469.1; -; mRNA.
DR RefSeq; NP_571509.1; NM_131434.1.
DR AlphaFoldDB; Q6PC54; -.
DR SMR; Q6PC54; -.
DR STRING; 7955.ENSDARP00000075371; -.
DR PaxDb; Q6PC54; -.
DR DNASU; 30711; -.
DR Ensembl; ENSDART00000080927; ENSDARP00000075371; ENSDARG00000058117. [Q6PC54-1]
DR Ensembl; ENSDART00000185724; ENSDARP00000146456; ENSDARG00000058117. [Q6PC54-1]
DR GeneID; 30711; -.
DR KEGG; dre:30711; -.
DR CTD; 30711; -.
DR ZFIN; ZDB-GENE-980526-392; snap25b.
DR eggNOG; KOG3065; Eukaryota.
DR GeneTree; ENSGT00950000182843; -.
DR HOGENOM; CLU_096939_0_0_1; -.
DR InParanoid; Q6PC54; -.
DR OMA; MENEPRT; -.
DR OrthoDB; 1197028at2759; -.
DR PhylomeDB; Q6PC54; -.
DR TreeFam; TF315125; -.
DR PRO; PR:Q6PC54; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 17.
DR Bgee; ENSDARG00000058117; Expressed in larva and 14 other tissues.
DR ExpressionAtlas; Q6PC54; baseline.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098793; C:presynapse; IEA:GOC.
DR GO; GO:0031201; C:SNARE complex; ISS:UniProtKB.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IBA:GO_Central.
DR GO; GO:0005484; F:SNAP receptor activity; IBA:GO_Central.
DR GO; GO:0019905; F:syntaxin binding; IBA:GO_Central.
DR GO; GO:0017075; F:syntaxin-1 binding; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:ZFIN.
DR GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR GO; GO:0007626; P:locomotory behavior; IMP:ZFIN.
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 InterPro; IPR039077; SNAP-25.
DR InterPro; IPR000928; SNAP-25_dom.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR19305:SF5; PTHR19305:SF5; 1.
DR Pfam; PF00835; SNAP-25; 1.
DR SMART; SM00397; t_SNARE; 2.
DR PROSITE; PS50192; T_SNARE; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Coiled coil; Membrane;
KW Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..203
FT /note="Synaptosomal-associated protein 25-B"
FT /id="PRO_0000355575"
FT DOMAIN 19..81
FT /note="t-SNARE coiled-coil homology 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT DOMAIN 137..199
FT /note="t-SNARE coiled-coil homology 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00202"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 60..93
FT /note="IEEGMDQINKDMKEAEKNLTDLGNLCGLCPCPCN -> VEDGMNHINKDMME
FT AEKSFKDVGKCCGLVCPCD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9843147"
FT /id="VSP_052975"
FT CONFLICT 55
FT /note="E -> G (in Ref. 1; AAC64291)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 203 AA; 22693 MW; 48D7590DD0C1179A CRC64;
MADESDMRNE LNDMQARADQ LGDESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI
EEGMDQINKD MKEAEKNLTD LGNLCGLCPC PCNKLKGGGQ SWGNNQDGVV SSQPARVVDE
REQMAISGGF IRRVTNDARE NEMDENLEQV GSIIGNLRHM ALDMGNEIDT QNRQIDRIMD
MADSNKTRID EANQRATKML GSG