ID   CPLX1_HUMAN             Reviewed;         134 AA.
AC   O14810; A6NI80; B2R4R5; D3DVN3; F1T0G1;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   28-JAN-2026, entry version 175.
DE   RecName: Full=Complexin-1;
DE   AltName: Full=Complexin I;
DE            Short=CPX I;
DE   AltName: Full=Synaphin-2;
GN   Name=CPLX1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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].
RC   TISSUE=Fetal brain;
RX   PubMed=24722188; DOI=10.1038/ncomms4650;
RA   Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M.,
RA   Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I.,
RA   Kuang X., Zhao N., Malhotra D., Michaelson J.J., Vacic V., Calderwood M.A.,
RA   Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D.,
RA   Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.;
RT   "Protein interaction network of alternatively spliced isoforms from brain
RT   links genetic risk factors for autism.";
RL   Nat. Commun. 5:3650-3650(2014).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=21697133; DOI=10.1167/iovs.11-7479;
RA   Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S.,
RA   Usami R., Ohtoko K., Kato S.;
RT   "Full-length transcriptome analysis of human retina-derived cell lines
RT   ARPE-19 and Y79 using the vector-capping method.";
RL   Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
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   [9]
RP   TISSUE SPECIFICITY.
RX   PubMed=9853440; DOI=10.1016/s0140-6736(98)03341-8;
RA   Harrison P.J., Eastwood S.L.;
RT   "Preferential involvement of excitatory neurons in medial temporal lobe in
RT   schizophrenia.";
RL   Lancet 352:1669-1673(1998).
RN   [10]
RP   TISSUE SPECIFICITY.
RX   PubMed=11483314; DOI=10.1016/s0306-4522(01)00141-5;
RA   Eastwood S.L., Cotter D., Harrison P.J.;
RT   "Cerebellar synaptic protein expression in schizophrenia.";
RL   Neuroscience 105:219-229(2001).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
RX   PubMed=15526345; DOI=10.1002/pmic.200400848;
RA   Basso M., Giraudo S., Corpillo D., Bergamasco B., Lopiano L., Fasano M.;
RT   "Proteome analysis of human substantia nigra in Parkinson's disease.";
RL   Proteomics 4:3943-3952(2004).
RN   [12]
RP   INVOLVEMENT IN DEE63, AND VARIANT DEE63 108-GLU--LYS-134 DEL.
RX   PubMed=26539891; DOI=10.1016/j.neuron.2015.09.048;
RA   Karaca E., Harel T., Pehlivan D., Jhangiani S.N., Gambin T.,
RA   Coban Akdemir Z., Gonzaga-Jauregui C., Erdin S., Bayram Y., Campbell I.M.,
RA   Hunter J.V., Atik M.M., Van Esch H., Yuan B., Wiszniewski W., Isikay S.,
RA   Yesil G., Yuregir O.O., Tug Bozdogan S., Aslan H., Aydin H., Tos T.,
RA   Aksoy A., De Vivo D.C., Jain P., Geckinli B.B., Sezer O., Gul D.,
RA   Durmaz B., Cogulu O., Ozkinay F., Topcu V., Candan S., Cebi A.H., Ikbal M.,
RA   Yilmaz Gulec E., Gezdirici A., Koparir E., Ekici F., Coskun S., Cicek S.,
RA   Karaer K., Koparir A., Duz M.B., Kirat E., Fenercioglu E., Ulucan H.,
RA   Seven M., Guran T., Elcioglu N., Yildirim M.S., Aktas D., Alikasifoglu M.,
RA   Ture M., Yakut T., Overton J.D., Yuksel A., Ozen M., Muzny D.M.,
RA   Adams D.R., Boerwinkle E., Chung W.K., Gibbs R.A., Lupski J.R.;
RT   "Genes that affect brain structure and function identified by rare variant
RT   analyses of mendelian neurologic disease.";
RL   Neuron 88:499-513(2015).
RN   [13]
RP   INVOLVEMENT IN DEE63, AND VARIANTS DEE63 105-CYS--LYS-134 DEL AND MET-128.
RX   PubMed=28422131; DOI=10.1038/ejhg.2017.52;
RA   Redler S., Strom T.M., Wieland T., Cremer K., Engels H., Distelmaier F.,
RA   Schaper J., Kuechler A., Lemke J.R., Jeschke S., Schreyer N., Sticht H.,
RA   Koch M., Luedecke H.J., Wieczorek D.;
RT   "Variants in CPLX1 in two families with autosomal-recessive severe
RT   infantile myoclonic epilepsy and ID.";
RL   Eur. J. Hum. Genet. 25:889-893(2017).
RN   [14]
RP   X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 28-83 ALONE AND IN COMPLEX WITH
RP   SNAP25; VAMP2 AND RAT STX1A, SUBUNIT, AND FUNCTION.
RX   PubMed=21785414; DOI=10.1038/nsmb.2101;
RA   Kummel D., Krishnakumar S.S., Radoff D.T., Li F., Giraudo C.G., Pincet F.,
RA   Rothman J.E., Reinisch K.M.;
RT   "Complexin cross-links prefusion SNAREs into a zigzag array.";
RL   Nat. Struct. Mol. Biol. 18:927-933(2011).
CC   -!- FUNCTION: Positively regulates a late step in exocytosis of various
CC       cytoplasmic vesicles, such as synaptic vesicles and other secretory
CC       vesicles (PubMed:21785414). 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:21785414). Also involved in glucose-induced secretion
CC       of insulin by pancreatic beta-cells. Essential for motor behavior.
CC       {ECO:0000250|UniProtKB:P63040, ECO:0000269|PubMed:21785414}.
CC   -!- SUBUNIT: Binds to the SNARE core complex containing SNAP25, VAMP2 and
CC       STX1A. {ECO:0000269|PubMed:21785414}.
CC   -!- INTERACTION:
CC       O14810; P60880-2: SNAP25; NbExp=6; IntAct=EBI-2691813, EBI-12177361;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P63040}. Perikaryon
CC       {ECO:0000250|UniProtKB:P63040}. Presynapse
CC       {ECO:0000250|UniProtKB:P63040}. Note=Enriched at synaptic-releasing
CC       sites in mature neurons. {ECO:0000250|UniProtKB:P63040}.
CC   -!- TISSUE SPECIFICITY: Nervous system. In hippocampus and cerebellum,
CC       expressed mainly by inhibitory neurons. Overexpressed in substantia
CC       nigra from patients with Parkinson disease.
CC       {ECO:0000269|PubMed:11483314, ECO:0000269|PubMed:15526345,
CC       ECO:0000269|PubMed:9853440}.
CC   -!- DISEASE: Developmental and epileptic encephalopathy 63 (DEE63)
CC       [MIM:617976]: A form of epileptic encephalopathy, a heterogeneous group
CC       of severe early-onset epilepsies characterized by refractory seizures,
CC       neurodevelopmental impairment, and poor prognosis. Development is
CC       normal prior to seizure onset, after which cognitive and motor delays
CC       become apparent. DEE63 is an autosomal recessive disease with onset in
CC       infancy. {ECO:0000269|PubMed:26539891, ECO:0000269|PubMed:28422131}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF022383; AAB72108.1; -; mRNA.
DR   EMBL; KJ534815; AHW56455.1; -; mRNA.
DR   EMBL; BT007029; AAP35676.1; -; mRNA.
DR   EMBL; AB593095; BAJ84035.1; -; mRNA.
DR   EMBL; AK311921; BAG34862.1; -; mRNA.
DR   EMBL; AC139887; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471131; EAW82648.1; -; Genomic_DNA.
DR   EMBL; CH471131; EAW82649.1; -; Genomic_DNA.
DR   EMBL; BC002471; AAH02471.1; -; mRNA.
DR   CCDS; CCDS46995.1; -.
DR   RefSeq; NP_006642.1; NM_006651.4.
DR   PDB; 3RK3; X-ray; 3.50 A; E=26-83.
DR   PDB; 3RL0; X-ray; 3.80 A; g/h/i/j/k/l/m/n=26-83.
DR   PDBsum; 3RK3; -.
DR   PDBsum; 3RL0; -.
DR   AlphaFoldDB; O14810; -.
DR   SMR; O14810; -.
DR   BioGRID; 116028; 42.
DR   CORUM; O14810; -.
DR   DIP; DIP-56109N; -.
DR   FunCoup; O14810; 335.
DR   IntAct; O14810; 13.
DR   MINT; O14810; -.
DR   STRING; 9606.ENSP00000305613; -.
DR   iPTMnet; O14810; -.
DR   PhosphoSitePlus; O14810; -.
DR   BioMuta; CPLX1; -.
DR   jPOST; O14810; -.
DR   MassIVE; O14810; -.
DR   PaxDb; 9606-ENSP00000305613; -.
DR   PeptideAtlas; O14810; -.
DR   ProteomicsDB; 48251; -.
DR   Antibodypedia; 22160; 175 antibodies from 25 providers.
DR   DNASU; 10815; -.
DR   Ensembl; ENST00000304062.11; ENSP00000305613.6; ENSG00000168993.16.
DR   GeneID; 10815; -.
DR   KEGG; hsa:10815; -.
DR   MANE-Select; ENST00000304062.11; ENSP00000305613.6; NM_006651.4; NP_006642.1.
DR   UCSC; uc003gbi.4; human.
DR   AGR; HGNC:2309; -.
DR   ClinPGx; PA26826; -.
DR   CTD; 10815; -.
DR   DisGeNET; 10815; -.
DR   GeneCards; CPLX1; -.
DR   HGNC; HGNC:2309; CPLX1.
DR   HPA; ENSG00000168993; Tissue enriched (brain).
DR   MalaCards; CPLX1; -.
DR   MIM; 605032; gene.
DR   MIM; 617976; phenotype.
DR   OpenTargets; ENSG00000168993; -.
DR   Orphanet; 352582; Familial infantile myoclonic epilepsy.
DR   Orphanet; 280; Wolf-Hirschhorn syndrome.
DR   VEuPathDB; HostDB:ENSG00000168993; -.
DR   eggNOG; ENOG502S3I2; Eukaryota.
DR   GeneTree; ENSGT00950000182938; -.
DR   InParanoid; O14810; -.
DR   OMA; RVHESHA; -.
DR   OrthoDB; 5972090at2759; -.
DR   PAN-GO; O14810; 5 GO annotations based on evolutionary models.
DR   PhylomeDB; O14810; -.
DR   PathwayCommons; O14810; -.
DR   Reactome; R-HSA-181429; Serotonin Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-181430; Norepinephrine Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-210500; Glutamate Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-212676; Dopamine Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-264642; Acetylcholine Neurotransmitter Release Cycle.
DR   Reactome; R-HSA-888590; GABA synthesis, release, reuptake and degradation.
DR   SignaLink; O14810; -.
DR   Agora; ENSG00000168993; Agora Nominated Target for Alzheimer's Disease.
DR   BioGRID-ORCS; 10815; 7 hits in 1142 CRISPR screens.
DR   EvolutionaryTrace; O14810; -.
DR   GeneWiki; CPLX1; -.
DR   GenomeRNAi; 10815; -.
DR   Pharos; O14810; Tbio.
DR   PRO; PR:O14810; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; O14810; protein.
DR   Bgee; ENSG00000168993; Expressed in lateral nuclear group of thalamus and 124 other cell types or tissues.
DR   ExpressionAtlas; O14810; baseline and differential.
DR   GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0098794; C:postsynapse; IEA:Ensembl.
DR   GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl.
DR   GO; GO:0031201; C:SNARE complex; IBA:GO_Central.
DR   GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IEA:Ensembl.
DR   GO; GO:0070554; C:synaptobrevin 2-SNAP-25-syntaxin-3-complexin complex; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0043195; C:terminal bouton; IBA:GO_Central.
DR   GO; GO:0000149; F:SNARE binding; IBA:GO_Central.
DR   GO; GO:0017075; F:syntaxin-1 binding; IEA:Ensembl.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0006887; P:exocytosis; TAS:ProtInc.
DR   GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
DR   GO; GO:0050804; P:modulation of chemical synaptic transmission; IBA:GO_Central.
DR   GO; GO:0099145; P:regulation of exocytic insertion of neurotransmitter receptor to postsynaptic membrane; IEA:Ensembl.
DR   GO; GO:0017157; P:regulation of exocytosis; TAS:ParkinsonsUK-UCL.
DR   GO; GO:0031630; P:regulation of synaptic vesicle fusion to presynaptic active zone membrane; IBA:GO_Central.
DR   GO; GO:0016079; P:synaptic vesicle exocytosis; IBA:GO_Central.
DR   CDD; cd22740; Complexin_NTD; 1.
DR   DisProt; DP02360; -.
DR   FunFam; 1.20.5.580:FF:000001; Complexin 2; 1.
DR   Gene3D; 1.20.5.580; Single Helix bin; 1.
DR   InterPro; IPR008849; Synaphin.
DR   PANTHER; PTHR16705; COMPLEXIN; 1.
DR   PANTHER; PTHR16705:SF6; COMPLEXIN-1; 1.
DR   Pfam; PF05835; Synaphin; 1.
DR   SUPFAM; SSF58038; SNARE fusion complex; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell projection; Coiled coil; Cytoplasm; Disease variant;
KW   Epilepsy; Exocytosis; Neurotransmitter transport;
KW   Proteomics identification; Reference proteome; Synapse; Transport.
FT   CHAIN           1..134
FT                   /note="Complexin-1"
FT                   /id="PRO_0000144870"
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..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          29..69
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VARIANT         105..134
FT                   /note="Missing (in DEE63)"
FT                   /evidence="ECO:0000269|PubMed:28422131"
FT                   /id="VAR_080795"
FT   VARIANT         108..134
FT                   /note="Missing (in DEE63)"
FT                   /evidence="ECO:0000269|PubMed:26539891"
FT                   /id="VAR_080796"
FT   VARIANT         128
FT                   /note="L -> M (in DEE63; uncertain significance;
FT                   dbSNP:rs371709824)"
FT                   /evidence="ECO:0000269|PubMed:28422131"
FT                   /id="VAR_080797"
FT   HELIX           29..70
FT                   /evidence="ECO:0007829|PDB:3RK3"
SQ   SEQUENCE   134 AA;  15030 MW;  A7A52F17F10D28A4 CRC64;
     MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
     AVRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEVE EEDESILDTV
     IKYLPGPLQD MLKK
//