ID   CPLX2_BOVIN             Reviewed;         134 AA.
AC   P84088; O09056; Q13329; Q28184; Q64386;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Complexin-2;
DE   AltName: Full=Complexin II;
DE            Short=CPX II;
DE   AltName: Full=Synaphin-1 {ECO:0000303|PubMed:7654227};
GN   Name=CPLX2;
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 [MRNA], AND PROTEIN SEQUENCE OF 56-76.
RC   TISSUE=Brain;
RX   PubMed=7654227; DOI=10.1006/bbrc.1995.2241;
RA   Ishizuka T., Saisu H., Odani S., Abe T.;
RT   "Synaphin: a protein associated with the docking/fusion complex in
RT   presynaptic terminals.";
RL   Biochem. Biophys. Res. Commun. 213:1107-1114(1995).
RN   [2]
RP   TISSUE SPECIFICITY, AND FUNCTION.
RX   PubMed=11929859; DOI=10.1074/jbc.c200166200;
RA   Archer D.A., Graham M.E., Burgoyne R.D.;
RT   "Complexin regulates the closure of the fusion pore during regulated
RT   vesicle exocytosis.";
RL   J. Biol. Chem. 277:18249-18252(2002).
RN   [3]
RP   SUBUNIT, AND FUNCTION.
RX   PubMed=12200427; DOI=10.1074/jbc.m205044200;
RA   Hu K., Carroll J., Rickman C., Davletov B.;
RT   "Action of complexin on SNARE complex.";
RL   J. Biol. Chem. 277:41652-41656(2002).
CC   -!- FUNCTION: Negatively regulates the formation of synaptic vesicle
CC       clustering at active zone to the presynaptic membrane in postmitotic
CC       neurons. Positively regulates a late step in exocytosis of various
CC       cytoplasmic vesicles, such as synaptic vesicles and other secretory
CC       vesicles. Also involved in mast cell exocytosis.
CC       {ECO:0000269|PubMed:11929859, ECO:0000269|PubMed:12200427}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000269|PubMed:12200427}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P84087}. Presynapse
CC       {ECO:0000250|UniProtKB:P84087}. Nucleus {ECO:0000250|UniProtKB:P84087}.
CC       Perikaryon {ECO:0000250|UniProtKB:P84087}. Note=Translocated from the
CC       perikaryon to the presynaptic terminals during maturation of neuronal
CC       cells. In mast cells, cytosol and nucleus. Becomes enriched near plasma
CC       membrane following stimulation. {ECO:0000250|UniProtKB:P84087}.
CC   -!- TISSUE SPECIFICITY: Nervous system. Also present in adrenal chromaffin
CC       cells (at protein level). {ECO:0000269|PubMed:11929859}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; D50807; BAA09434.1; -; mRNA.
DR   RefSeq; NP_776708.1; NM_174283.2.
DR   RefSeq; XP_005211237.1; XM_005211180.3.
DR   RefSeq; XP_005211238.1; XM_005211181.3.
DR   AlphaFoldDB; P84088; -.
DR   SMR; P84088; -.
DR   CORUM; P84088; -.
DR   STRING; 9913.ENSBTAP00000018256; -.
DR   iPTMnet; P84088; -.
DR   PaxDb; P84088; -.
DR   GeneID; 281711; -.
DR   KEGG; bta:281711; -.
DR   CTD; 10814; -.
DR   eggNOG; ENOG502RXXI; Eukaryota.
DR   HOGENOM; CLU_132159_1_0_1; -.
DR   InParanoid; P84088; -.
DR   TreeFam; TF315172; -.
DR   Proteomes; UP000009136; Unplaced.
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:0005634; C:nucleus; 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:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS:UniProtKB.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; PTHR16705; 1.
DR   Pfam; PF05835; Synaphin; 1.
PE   1: Evidence at protein level;
KW   Cell projection; Coiled coil; Cytoplasm; Direct protein sequencing;
KW   Exocytosis; Mast cell degranulation; Neurotransmitter transport; Nucleus;
KW   Phosphoprotein; Reference proteome; Synapse; Transport.
FT   CHAIN           1..134
FT                   /note="Complexin-2"
FT                   /id="PRO_0000144874"
FT   REGION          1..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          41..97
FT                   /note="Interaction with the SNARE complex"
FT                   /evidence="ECO:0000250"
FT   COILED          28..84
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        18..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         93
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P84087"
SQ   SEQUENCE   134 AA;  15394 MW;  7791812FD4194AC5 CRC64;
     MDFVMKQALG GATKDMGKML GGEEEKDPDA QKKEEERQEA LRQQEEERKA KHARMEAERE
     KVRQQIRDKY GLKKKEEKEA EEKAALEQPC EGSLTRPKKA IPAGCGDEEE EEEESILDTV
     LKYLPGPLQD MFKK