CPLX1_MOUSE
ID CPLX1_MOUSE Reviewed; 134 AA.
AC P63040; O09057; O09142; Q3UYB3; Q64276; Q91WJ3;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Complexin-1;
DE AltName: Full=921-S {ECO:0000303|PubMed:7635198};
DE AltName: Full=Complexin I;
DE Short=CPX I;
DE AltName: Full=Synaphin-2;
GN Name=Cplx1;
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], 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear, Medulla oblongata, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=15126625; DOI=10.1242/jcs.01041;
RA Abderrahmani A., Niederhauser G., Plaisance V., Roehrich M.-E., Lenain V.,
RA Coppola T., Regazzi R., Waeber G.;
RT "Complexin I regulates glucose-induced secretion in pancreatic beta-
RT cells.";
RL J. Cell Sci. 117:2239-2247(2004).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=16000319; DOI=10.1093/hmg/ddi239;
RA Glynn D., Drew C.J., Reim K., Brose N., Morton A.J.;
RT "Profound ataxia in complexin I knockout mice masks a complex phenotype
RT that includes exploratory and habituation deficits.";
RL Hum. Mol. Genet. 14:2369-2385(2005).
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=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 [8]
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: Positively regulates a late step in exocytosis of various
CC cytoplasmic vesicles, such as synaptic vesicles and other secretory
CC vesicles (PubMed:23345244). Organizes the SNAREs into a cross-linked
CC zigzag topology that, when interposed between the vesicle and plasma
CC membranes, is incompatible with fusion, thereby preventing SNAREs from
CC releasing neurotransmitters until an action potential arrives at the
CC synapse (PubMed:23345244). Also involved in glucose-induced secretion
CC of insulin by pancreatic beta-cells. Essential for motor behavior
CC (PubMed:15126625, PubMed:16000319). {ECO:0000269|PubMed:15126625,
CC ECO:0000269|PubMed:16000319, ECO:0000269|PubMed:23345244}.
CC -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC STX1A. {ECO:0000250|UniProtKB:O14810}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15126625,
CC ECO:0000269|PubMed:7635198}. Perikaryon {ECO:0000269|PubMed:7635198}.
CC Presynapse {ECO:0000269|PubMed:7635198}. Note=Enriched at synaptic-
CC releasing sites in mature neurons. {ECO:0000269|PubMed:7635198}.
CC -!- TISSUE SPECIFICITY: Nervous system, and pancreatic islet cells. Present
CC in many brain regions, including hippocampus and cerebellum. In the
CC retina, present at conventional amacrine cell synapses (at protein
CC level). {ECO:0000269|PubMed:15126625, 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 have no obvious brain abnormality, but
CC suffer from severe ataxia with dystonia starting from P7. Adult mice
CC lacking Cplx1 are not capable of coordinated running or swimming and
CC exhibit pronounced resting tremor. They also fail to habituate to
CC confinement and have reduced exploration abilities in open field.
CC {ECO:0000269|PubMed:16000319}.
CC -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR EMBL; D38614; BAA07605.1; -; mRNA.
DR EMBL; AK134820; BAE22299.1; -; mRNA.
DR EMBL; AK158166; BAE34390.1; -; mRNA.
DR EMBL; AK159026; BAE34774.1; -; mRNA.
DR EMBL; BC014803; AAH14803.1; -; mRNA.
DR CCDS; CCDS39206.1; -.
DR PIR; S66294; S66294.
DR RefSeq; NP_031782.3; NM_007756.3.
DR AlphaFoldDB; P63040; -.
DR BMRB; P63040; -.
DR SMR; P63040; -.
DR BioGRID; 198859; 9.
DR CORUM; P63040; -.
DR STRING; 10090.ENSMUSP00000038502; -.
DR iPTMnet; P63040; -.
DR PhosphoSitePlus; P63040; -.
DR MaxQB; P63040; -.
DR PaxDb; P63040; -.
DR PeptideAtlas; P63040; -.
DR PRIDE; P63040; -.
DR ProteomicsDB; 285290; -.
DR Antibodypedia; 22160; 178 antibodies from 26 providers.
DR DNASU; 12889; -.
DR Ensembl; ENSMUST00000046892; ENSMUSP00000038502; ENSMUSG00000033615.
DR GeneID; 12889; -.
DR KEGG; mmu:12889; -.
DR UCSC; uc008yof.2; mouse.
DR CTD; 10815; -.
DR MGI; MGI:104727; Cplx1.
DR VEuPathDB; HostDB:ENSMUSG00000033615; -.
DR eggNOG; ENOG502S3I2; Eukaryota.
DR GeneTree; ENSGT00950000182938; -.
DR HOGENOM; CLU_132159_1_0_1; -.
DR InParanoid; P63040; -.
DR OMA; TPIMDIF; -.
DR PhylomeDB; P63040; -.
DR TreeFam; TF315172; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-MMU-888590; GABA synthesis, release, reuptake and degradation.
DR BioGRID-ORCS; 12889; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Cplx1; mouse.
DR PRO; PR:P63040; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P63040; protein.
DR Bgee; ENSMUSG00000033615; Expressed in motor neuron and 188 other tissues.
DR ExpressionAtlas; P63040; baseline and differential.
DR Genevisible; P63040; 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: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:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0031201; C:SNARE complex; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; ISO:MGI.
DR GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0017075; F:syntaxin-1 binding; ISO:MGI.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IDA:SynGO.
DR GO; GO:0030073; P:insulin secretion; IMP: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; IMP:UniProtKB.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; IDA:SynGO.
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; Exocytosis;
KW Neurotransmitter transport; Reference proteome; Synapse; Transport.
FT CHAIN 1..134
FT /note="Complexin-1"
FT /id="PRO_0000144871"
FT REGION 1..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..70
FT /note="Interaction with the SNARE complex"
FT /evidence="ECO:0000250"
FT REGION 74..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 29..64
FT /evidence="ECO:0000255"
FT COMPBIAS 18..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 84
FT /note="A -> V (in Ref. 3; AAH14803)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 134 AA; 15122 MW; BA1B6F074923A3A4 CRC64;
MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEPE EEDESILDTV
IKYLPGPLQD MFKK
