CPLX2_MOUSE
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 03-AUG-2022, entry version 120.
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; 6.
DR CORUM; P84086; -.
DR STRING; 10090.ENSMUSP00000026985; -.
DR iPTMnet; P84086; -.
DR PhosphoSitePlus; P84086; -.
DR MaxQB; P84086; -.
DR PaxDb; P84086; -.
DR PeptideAtlas; P84086; -.
DR PRIDE; P84086; -.
DR ProteomicsDB; 283935; -.
DR Antibodypedia; 45968; 182 antibodies from 26 providers.
DR DNASU; 12890; -.
DR Ensembl; ENSMUST00000026985; ENSMUSP00000026985; ENSMUSG00000025867.
DR GeneID; 12890; -.
DR KEGG; mmu:12890; -.
DR UCSC; uc029sbi.1; mouse.
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 75 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 208 other tissues.
DR Genevisible; P84086; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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 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; 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
