ID   CPLX1_MACFA             Reviewed;         134 AA.
AC   Q4R4N1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   03-AUG-2022, entry version 64.
DE   RecName: Full=Complexin-1;
GN   Name=CPLX1; ORFNames=QccE-19379;
OS   Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RA   Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA   Suzuki Y., Sugano S., Hashimoto K.;
RT   "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL   Submitted (JUN-2005) 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; AB169863; BAE01944.1; -; mRNA.
DR   RefSeq; NP_001271686.1; NM_001284757.1.
DR   RefSeq; XP_015305472.1; XM_015449986.1.
DR   AlphaFoldDB; Q4R4N1; -.
DR   BMRB; Q4R4N1; -.
DR   STRING; 9541.XP_005554308.1; -.
DR   GeneID; 102114990; -.
DR   KEGG; mcf:102114990; -.
DR   CTD; 10815; -.
DR   VEuPathDB; HostDB:ENSMFAG00000040997; -.
DR   eggNOG; ENOG502S3I2; Eukaryota.
DR   OMA; TPIMDIF; -.
DR   OrthoDB; 1556534at2759; -.
DR   Proteomes; UP000233100; Chromosome 5.
DR   GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0098793; C:presynapse; IEA:UniProtKB-SubCell.
DR   GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
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_0000240232"
FT   REGION          1..113
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;  15062 MW;  BA0F980A5BBA28A4 CRC64;
     MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
     AMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV
     IKYLPGPLQD MLKK