ID   CPLX_HIRME              Reviewed;         144 AA.
AC   Q8I6U3;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Complexin-1;
DE   Flags: Precursor;
GN   Name=cpx1;
OS   Hirudo medicinalis (Medicinal leech).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Hirudinea; Hirudinida; Hirudiniformes; Hirudinidae; Hirudo.
OX   NCBI_TaxID=6421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=CNS;
RX   PubMed=14678834; DOI=10.1016/s1567-133x(03)00143-1;
RA   Dykes I.M., Davies J.A.;
RT   "Cloning and expression of a leech complexin.";
RL   Gene Expr. Patterns 4:93-97(2004).
CC   -!- FUNCTION: Positively regulates a late step in synaptic vesicle
CC       exocytosis. {ECO:0000250}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25,
CC       synaptobrevin and syntaxin-1. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in a subset of neurons in the central
CC       nervous system, including large serotoninergic Retzius neurons and
CC       pressure-sensitive P cells. {ECO:0000269|PubMed:14678834}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; AJ512832; CAD55800.1; -; mRNA.
DR   AlphaFoldDB; Q8I6U3; -.
DR   SMR; Q8I6U3; -.
DR   PRIDE; Q8I6U3; -.
DR   GO; GO:0016020; C:membrane; 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   Coiled coil; Exocytosis; Lipoprotein; Membrane; Methylation;
KW   Neurotransmitter transport; Prenylation; Transport.
FT   CHAIN           1..141
FT                   /note="Complexin-1"
FT                   /id="PRO_0000240239"
FT   PROPEP          142..144
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000240240"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..67
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        38..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         141
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           141
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   144 AA;  15987 MW;  F3C5F36A2262C38D CRC64;
     MVSFLGGGLL GNPLSGALEE KEDKKEGDEE EDPEIAEAKR EAEEKRNEKY RKMEEEREVM
     RQGIRDKYHI QKKELPKEDP GLEGRLGRKK KSPDEAVEGG DPLQSSAQSS GFPKNLDDLT
     AKVKELPGTV MTTVSGATDK CNLQ