CPLX2_RAT
ID CPLX2_RAT Reviewed; 134 AA.
AC P84087; 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 114.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-49; 55-69 AND 84-98,
RP TISSUE SPECIFICITY, AND SUBUNIT.
RC 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], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=10051208; DOI=10.1016/s0306-4522(98)00223-1;
RA Ishizuka T., Saisu H., Odani S., Kumanishi T., Abe T.;
RT "Distinct regional distribution in the brain of messenger RNAs for the two
RT isoforms of synaphin associated with the docking/fusion complex.";
RL Neuroscience 88:295-306(1999).
RN [3]
RP PROTEIN SEQUENCE OF 84-122, PHOSPHORYLATION AT SER-93, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=16499873; DOI=10.1016/j.bbrc.2006.02.029;
RA Hill J.J., Callaghan D.A., Ding W., Kelly J.F., Chakravarthy B.R.;
RT "Identification of okadaic acid-induced phosphorylation events by a mass
RT spectrometry approach.";
RL Biochem. Biophys. Res. Commun. 342:791-799(2006).
RN [4]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [5]
RP SUBCELLULAR LOCATION.
RX PubMed=9753100; DOI=10.1046/j.1460-9568.1998.00225.x;
RA Ono S., Baux G., Sekiguchi M., Fossier P., Morel N.F., Nihonmatsu I.,
RA Hirata K., Awaji T., Takahashi S., Takahashi M.;
RT "Regulatory roles of complexins in neurotransmitter release from mature
RT presynaptic nerve terminals.";
RL Eur. J. Neurosci. 10:2143-2152(1998).
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=10430466; DOI=10.1016/s0306-4522(99)00104-9;
RA Yamada M., Saisu H., Ishizuka T., Takahashi H., Abe T.;
RT "Immunohistochemical distribution of the two isoforms of synaphin/complexin
RT involved in neurotransmitter release: localization at the distinct central
RT nervous system regions and synaptic types.";
RL Neuroscience 93:7-18(1999).
RN [7]
RP SUBUNIT.
RX PubMed=10777504; DOI=10.1074/jbc.m002571200;
RA Pabst S., Hazzard J.W., Antonin W., Suedhof T.C., Jahn R., Rizo J.,
RA Fasshauer D.;
RT "Selective interaction of complexin with the neuronal SNARE complex.
RT Determination of the binding regions.";
RL J. Biol. Chem. 275:19808-19818(2000).
RN [8]
RP SUBUNIT.
RX PubMed=11751907; DOI=10.1074/jbc.m109507200;
RA Pabst S., Margittai M., Vainius D., Langen R., Jahn R., Fasshauer D.;
RT "Rapid and selective binding to the synaptic SNARE complex suggests a
RT modulatory role of complexins in neuroexocytosis.";
RL J. Biol. Chem. 277:7838-7848(2002).
RN [9]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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 [10]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15870114; DOI=10.1242/jcs.02338;
RA Tadokoro S., Nakanishi M., Hirashima N.;
RT "Complexin II facilitates exocytotic release in mast cells by enhancing
RT Ca2+ sensitivity of the fusion process.";
RL J. Cell Sci. 118:2239-2246(2005).
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 (PubMed:15870114).
CC {ECO:0000269|PubMed:15870114}.
CC -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A. {ECO:0000269|PubMed:10777504, ECO:0000269|PubMed:11751907,
CC ECO:0000269|PubMed:7553862}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:7654227}.
CC Presynapse {ECO:0000269|PubMed:15911881, ECO:0000269|PubMed:7654227}.
CC Nucleus. Perikaryon {ECO:0000269|PubMed:9753100}. Note=Translocated
CC from the perikaryon to the presynaptic terminals during maturation of
CC neuronal cells (PubMed:7654227). In mast cells, cytosol and nucleus.
CC Becomes enriched near plasma membrane following stimulation.
CC {ECO:0000269|PubMed:7654227}.
CC -!- TISSUE SPECIFICITY: Nervous system. Strongly expressed in brain, where
CC it is predominant in neurons from cerebral cortex and hippocampus. Also
CC present in mast cells (at protein level). {ECO:0000269|PubMed:10051208,
CC ECO:0000269|PubMed:10430466, ECO:0000269|PubMed:15870114,
CC ECO:0000269|PubMed:15911881, ECO:0000269|PubMed:7553862,
CC ECO:0000269|PubMed:7654227}.
CC -!- PTM: Ser-93 is dephosphorylated by PP2A.
CC -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR EMBL; U35099; AAC52271.1; -; mRNA.
DR EMBL; D70816; BAA11096.1; -; mRNA.
DR PIR; C57233; C57233.
DR PIR; JC4226; JC4226.
DR RefSeq; NP_446330.1; NM_053878.1.
DR RefSeq; XP_017455929.1; XM_017600440.1.
DR RefSeq; XP_017455930.1; XM_017600441.1.
DR AlphaFoldDB; P84087; -.
DR SMR; P84087; -.
DR BioGRID; 250542; 1.
DR CORUM; P84087; -.
DR DIP; DIP-48643N; -.
DR IntAct; P84087; 2.
DR STRING; 10116.ENSRNOP00000000117; -.
DR iPTMnet; P84087; -.
DR PhosphoSitePlus; P84087; -.
DR jPOST; P84087; -.
DR PaxDb; P84087; -.
DR PRIDE; P84087; -.
DR Ensembl; ENSRNOT00000091046; ENSRNOP00000072664; ENSRNOG00000000105.
DR GeneID; 116657; -.
DR KEGG; rno:116657; -.
DR UCSC; RGD:70945; rat.
DR CTD; 10814; -.
DR RGD; 70945; Cplx2.
DR eggNOG; ENOG502RXXI; Eukaryota.
DR GeneTree; ENSGT00950000182938; -.
DR InParanoid; P84087; -.
DR OMA; KHTRMEA; -.
DR PhylomeDB; P84087; -.
DR TreeFam; TF315172; -.
DR PRO; PR:P84087; -.
DR Proteomes; UP000002494; Chromosome 17.
DR Bgee; ENSRNOG00000000105; Expressed in frontal cortex and 18 other tissues.
DR Genevisible; P84087; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0044305; C:calyx of Held; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA: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; IDA:SynGO.
DR GO; GO:0098793; C:presynapse; IDA:SynGO.
DR GO; GO:0031201; C:SNARE complex; IDA:RGD.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0070033; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex; IDA:RGD.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:RGD.
DR GO; GO:0000149; F:SNARE binding; IDA:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:MGI.
DR GO; GO:0043303; P:mast cell degranulation; IEA:UniProtKB-KW.
DR GO; GO:0031915; P:positive regulation of synaptic plasticity; ISS: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; ISO:RGD.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; TAS:ProtInc.
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_0000144877"
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 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:0000269|PubMed:16499873"
SQ SEQUENCE 134 AA; 15394 MW; 7791812FD4194AC5 CRC64;
MDFVMKQALG GATKDMGKML GGEEEKDPDA QKKEEERQEA LRQQEEERKA KHARMEAERE
KVRQQIRDKY GLKKKEEKEA EEKAALEQPC EGSLTRPKKA IPAGCGDEEE EEEESILDTV
LKYLPGPLQD MFKK
