ID   CPLX1_BOVIN             Reviewed;         134 AA.
AC   Q0IIL7;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Complexin-1;
GN   Name=CPLX1;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Thalamus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Positively regulates a late step in synaptic vesicle
CC       exocytosis. Organizes the SNAREs into a cross-linked zigzag topology
CC       that, when interposed between the vesicle and plasma membranes, is
CC       incompatible with fusion, thereby preventing SNAREs from releasing
CC       neurotransmitters until an action potential arrives at the synapse.
CC       Also involved in glucose-induced secretion of insulin by pancreatic
CC       beta-cells (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P63040}. Perikaryon
CC       {ECO:0000250|UniProtKB:P63040}. Presynapse
CC       {ECO:0000250|UniProtKB:P63040}. Note=Enriched at synaptic-releasing
CC       sites in mature neurons. {ECO:0000250|UniProtKB:P63040}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; BC122583; AAI22584.1; -; mRNA.
DR   RefSeq; NP_001071571.1; NM_001078103.1.
DR   AlphaFoldDB; Q0IIL7; -.
DR   iPTMnet; Q0IIL7; -.
DR   PRIDE; Q0IIL7; -.
DR   Ensembl; ENSBTAT00000070551; ENSBTAP00000070039; ENSBTAG00000050808.
DR   GeneID; 768228; -.
DR   KEGG; bta:768228; -.
DR   CTD; 10815; -.
DR   VEuPathDB; HostDB:ENSBTAG00000050808; -.
DR   VGNC; VGNC:58459; CPLX1.
DR   GeneTree; ENSGT00950000182938; -.
DR   InParanoid; Q0IIL7; -.
DR   OMA; TPIMDIF; -.
DR   OrthoDB; 1556534at2759; -.
DR   Proteomes; UP000009136; Chromosome 6.
DR   Bgee; ENSBTAG00000050808; Expressed in retina and 49 other tissues.
DR   ExpressionAtlas; Q0IIL7; baseline.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; PTHR16705; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   2: Evidence at transcript level;
KW   Cell projection; Coiled coil; Cytoplasm; Exocytosis;
KW   Neurotransmitter transport; Reference proteome; Synapse; Transport.
FT   CHAIN           1..134
FT                   /note="Complexin-1"
FT                   /id="PRO_0000290028"
FT   REGION          1..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          48..70
FT                   /note="Interaction with the SNARE complex"
FT                   /evidence="ECO:0000250"
FT   COILED          29..69
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        18..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   134 AA;  15000 MW;  CCB58BFE014D6CA0 CRC64;
     MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQEEEERKA KYAKMEAERE
     AVRQGIRDKY GIKKKEEREA EAQAALEANS EGSLTRPKKA IPPGCGDAAE EEDESILDTV
     IKYLPGPLQD IFKK