ID   CPLX2_MOUSE             Reviewed;         134 AA.
AC   P84086; O09056; Q13329; Q28184; Q32KK4; Q64386;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 128.
DE   RecName: Full=Complexin-2;
DE   AltName: Full=921-L;
DE   AltName: Full=Complexin II;
DE            Short=CPX II;
DE   AltName: Full=Synaphin-1;
GN   Name=Cplx2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/Sv; TISSUE=Brain;
RX   PubMed=7553862; DOI=10.1016/0092-8674(95)90239-2;
RA   McMahon H.T., Missler M., Li C., Suedhof T.C.;
RT   "Complexins: cytosolic proteins that regulate SNAP receptor function.";
RL   Cell 83:111-119(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=BALB/cJ; TISSUE=Brain;
RX   PubMed=7635198; DOI=10.1016/0014-5793(95)00713-j;
RA   Takahashi S., Yamamoto H., Matsuda Z., Ogawa M., Yagyu K., Taniguchi T.,
RA   Miyata T., Kaba H., Higuchi T., Okutani F., Fujimoto S.;
RT   "Identification of two highly homologous presynaptic proteins distinctly
RT   localized at the dendritic and somatic synapses.";
RL   FEBS Lett. 368:455-460(1995).
RN   [3]
RP   IDENTIFICATION.
RC   TISSUE=Brain;
RX   PubMed=16162394; DOI=10.1016/j.gene.2005.07.005;
RA   Raevskaya N.M., Dergunova L.V., Vladychenskaya I.P., Stavchansky V.V.,
RA   Oborina M.V., Poltaraus A.B., Limborska S.A.;
RT   "Structural organization of the human complexin 2 gene (CPLX2) and aspects
RT   of its functional activity.";
RL   Gene 359:127-137(2005).
RN   [4]
RP   FUNCTION.
RX   PubMed=11163241; DOI=10.1016/s0092-8674(01)00192-1;
RA   Reim K., Mansour M., Varoqueaux F., McMahon H.T., Suedhof T.C., Brose N.,
RA   Rosenmund C.;
RT   "Complexins regulate a late step in Ca2+-dependent neurotransmitter
RT   release.";
RL   Cell 104:71-81(2001).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=12915444; DOI=10.1093/hmg/ddg249;
RA   Glynn D., Bortnick R.A., Morton A.J.;
RT   "Complexin II is essential for normal neurological function in mice.";
RL   Hum. Mol. Genet. 12:2431-2448(2003).
RN   [6]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=15911881; DOI=10.1083/jcb.200502115;
RA   Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C.,
RA   Dresbach T., Hofmann K., Brose N.;
RT   "Structurally and functionally unique complexins at retinal ribbon
RT   synapses.";
RL   J. Cell Biol. 169:669-680(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   FUNCTION.
RX   PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006;
RA   Ravanpay A.C., Hansen S.J., Olson J.M.;
RT   "Transcriptional inhibition of REST by NeuroD2 during neuronal
RT   differentiation.";
RL   Mol. Cell. Neurosci. 44:178-189(2010).
RN   [10]
RP   FUNCTION.
RX   PubMed=23345244; DOI=10.1523/jneurosci.4087-12.2013;
RA   Cao P., Yang X., Suedhof T.C.;
RT   "Complexin activates exocytosis of distinct secretory vesicles controlled
RT   by different synaptotagmins.";
RL   J. Neurosci. 33:1714-1727(2013).
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 (PubMed:11163241, PubMed:23345244). Also involved in mast cell
CC       exocytosis (PubMed:11163241). Although not essential for development,
CC       seems critical for the acquisition of higher cognitive functions in the
CC       adult brain (PubMed:12915444). {ECO:0000269|PubMed:11163241,
CC       ECO:0000269|PubMed:12915444, ECO:0000269|PubMed:20346398,
CC       ECO:0000269|PubMed:23345244}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7635198}.
CC       Presynapse {ECO:0000250|UniProtKB:P84087}. Nucleus
CC       {ECO:0000250|UniProtKB:P84087}. Perikaryon
CC       {ECO:0000250|UniProtKB:P84087}. Note=Translocated from the perikaryon
CC       to the presynaptic terminals during maturation of neuronal cells. In
CC       mast cells, cytosol and nucleus. Becomes enriched near plasma membrane
CC       following stimulation. {ECO:0000250|UniProtKB:P84087}.
CC   -!- TISSUE SPECIFICITY: Nervous system. Expressed predominantly in brain,
CC       where it is present in many regions, including hippocampus and
CC       cerebellum. In the retina, present at conventional amacrine cell
CC       synapses (at protein level). {ECO:0000269|PubMed:15911881,
CC       ECO:0000269|PubMed:7635198}.
CC   -!- DEVELOPMENTAL STAGE: In the brain, expression starts at P6 and
CC       increases to reach a plateau at P20. {ECO:0000269|PubMed:15911881}.
CC   -!- DISRUPTION PHENOTYPE: Mice show no obvious phenotypic changes and no
CC       significant motor deficiencies. However, they show abnormalities in a
CC       number of complex behaviors including exploration, socialization, motor
CC       coordination, learning and reversal learning.
CC       {ECO:0000269|PubMed:12915444}.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR   EMBL; U35101; AAC52272.1; -; Genomic_DNA.
DR   EMBL; D38613; BAA07604.1; -; mRNA.
DR   EMBL; BN000501; CAG26661.1; -; mRNA.
DR   EMBL; BN000502; CAG26662.1; -; mRNA.
DR   CCDS; CCDS36667.1; -.
DR   PIR; S66293; D57233.
DR   RefSeq; NP_034076.1; NM_009946.3.
DR   RefSeq; XP_017170864.1; XM_017315375.1.
DR   RefSeq; XP_017170865.1; XM_017315376.1.
DR   AlphaFoldDB; P84086; -.
DR   SMR; P84086; -.
DR   BioGRID; 198860; 7.
DR   CORUM; P84086; -.
DR   STRING; 10090.ENSMUSP00000026985; -.
DR   iPTMnet; P84086; -.
DR   PhosphoSitePlus; P84086; -.
DR   SwissPalm; P84086; -.
DR   MaxQB; P84086; -.
DR   PaxDb; 10090-ENSMUSP00000026985; -.
DR   PeptideAtlas; P84086; -.
DR   ProteomicsDB; 283935; -.
DR   Pumba; P84086; -.
DR   Antibodypedia; 45968; 201 antibodies from 26 providers.
DR   DNASU; 12890; -.
DR   Ensembl; ENSMUST00000026985.9; ENSMUSP00000026985.9; ENSMUSG00000025867.9.
DR   GeneID; 12890; -.
DR   KEGG; mmu:12890; -.
DR   UCSC; uc029sbi.1; mouse.
DR   AGR; MGI:104726; -.
DR   CTD; 10814; -.
DR   MGI; MGI:104726; Cplx2.
DR   VEuPathDB; HostDB:ENSMUSG00000025867; -.
DR   eggNOG; ENOG502RXXI; Eukaryota.
DR   GeneTree; ENSGT00950000182938; -.
DR   HOGENOM; CLU_132159_1_0_1; -.
DR   InParanoid; P84086; -.
DR   OMA; KHTRMEA; -.
DR   PhylomeDB; P84086; -.
DR   TreeFam; TF315172; -.
DR   BioGRID-ORCS; 12890; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Cplx2; mouse.
DR   PRO; PR:P84086; -.
DR   Proteomes; UP000000589; Chromosome 13.
DR   RNAct; P84086; Protein.
DR   Bgee; ENSMUSG00000025867; Expressed in dentate gyrus of hippocampal formation granule cell and 209 other cell types or tissues.
DR   GO; GO:0044305; C:calyx of Held; IDA:SynGO.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0030425; C:dendrite; ISO:MGI.
DR   GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; ISO:MGI.
DR   GO; GO:0098793; C:presynapse; IDA:SynGO.
DR   GO; GO:0031201; C:SNARE complex; ISO:MGI.
DR   GO; GO:0045202; C:synapse; ISO:MGI.
DR   GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; ISO:MGI.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR   GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR   GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR   GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR   GO; GO:0031915; P:positive regulation of synaptic plasticity; IDA:UniProtKB.
DR   GO; GO:0046928; P:regulation of neurotransmitter secretion; IBA:GO_Central.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IDA:SynGO.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:MGI.
DR   CDD; cd22808; Complexin_NTD_CPLX_I_II; 1.
DR   Gene3D; 1.20.5.580; Single Helix bin; 1.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; COMPLEXIN; 1.
DR   PANTHER; PTHR16705:SF9; COMPLEXIN-2; 1.
DR   Pfam; PF05835; Synaphin; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
DR   Genevisible; P84086; MM.
PE   1: Evidence at protein level;
KW   Cell projection; Coiled coil; Cytoplasm; Differentiation; Exocytosis;
KW   Mast cell degranulation; Neurogenesis; Neurotransmitter transport; Nucleus;
KW   Phosphoprotein; Reference proteome; Synapse; Transport.
FT   CHAIN           1..134
FT                   /note="Complexin-2"
FT                   /id="PRO_0000144876"
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
//