ID   CPLX_DORPE              Reviewed;         152 AA.
AC   Q95PA1;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Complexin;
DE   AltName: Full=Synaphin;
DE   Flags: Precursor;
GN   Name=cpx;
OS   Doryteuthis pealeii (Longfin inshore squid) (Loligo pealeii).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Myopsina; Loliginidae; Doryteuthis.
OX   NCBI_TaxID=1051067;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-26 AND 90-96,
RP   SUBCELLULAR LOCATION, SUBUNIT, AND FUNCTION.
RC   TISSUE=Optic lobe;
RX   PubMed=11239399; DOI=10.1016/s0092-8674(01)00229-x;
RA   Tokumaru H., Umayahara K., Pellegrini L.L., Ishizuka T., Saisu H., Betz H.,
RA   Augustine G.J., Abe T.;
RT   "SNARE complex oligomerization by synaphin/complexin is essential for
RT   synaptic vesicle exocytosis.";
RL   Cell 104:421-432(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 25-98 IN COMPLEX WITH THE SNARE
RP   CORE COMPLEX.
RX   PubMed=12004067; DOI=10.1074/jbc.m203460200;
RA   Bracher A., Kadlec J., Betz H., Weissenhorn W.;
RT   "X-ray structure of a neuronal complexin-SNARE complex from squid.";
RL   J. Biol. Chem. 277:26517-26523(2002).
CC   -!- FUNCTION: Positively regulates a late step in synaptic vesicle
CC       exocytosis. {ECO:0000269|PubMed:11239399}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25,
CC       synaptobrevin and syntaxin-1. {ECO:0000269|PubMed:11239399,
CC       ECO:0000269|PubMed:12004067}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}. Cytoplasm, cytosol {ECO:0000269|PubMed:11239399}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; AB003700; BAB62069.1; -; mRNA.
DR   PDB; 1L4A; X-ray; 2.95 A; E=25-98.
DR   PDBsum; 1L4A; -.
DR   AlphaFoldDB; Q95PA1; -.
DR   SMR; Q95PA1; -.
DR   IntAct; Q95PA1; 3.
DR   MINT; Q95PA1; -.
DR   EvolutionaryTrace; Q95PA1; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Exocytosis;
KW   Lipoprotein; Membrane; Methylation; Neurotransmitter transport;
KW   Prenylation; Transport.
FT   CHAIN           1..149
FT                   /note="Complexin"
FT                   /id="PRO_0000240241"
FT   PROPEP          150..152
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000240242"
FT   REGION          1..119
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          59..75
FT                   /note="Interaction with the SNARE complex"
FT   COMPBIAS        19..106
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         149
FT                   /note="Cysteine methyl ester"
FT                   /evidence="ECO:0000255"
FT   LIPID           149
FT                   /note="S-farnesyl cysteine"
FT                   /evidence="ECO:0000255"
FT   HELIX           50..73
FT                   /evidence="ECO:0007829|PDB:1L4A"
SQ   SEQUENCE   152 AA;  17235 MW;  6FA6B17168BE7533 CRC64;
     MAAFIAKQMV GDQLKSVKAM GGDEGEKEGN ENAEEEAAAI EEARREAEER RKEKHRKMEE
     EREEMRQTIR DKYGLKKKVK EEPEAEADLD EGRVGRKKKT KEELAAEANE EEDDDEFAKF
     PTDLSDLTTK VSELPQKMAA SVGEVTEKCS LQ