CPLX1_RAT
ID CPLX1_RAT Reviewed; 134 AA.
AC P63041; O09057; O09142; Q566D7; Q64276;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 31-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Complexin-1;
DE AltName: Full=Complexin I;
DE Short=CPX I;
DE AltName: Full=Synaphin-2;
GN Name=Cplx1;
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 74-96,
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 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 [5]
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 [6]
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 [7]
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 [8]
RP SUBUNIT, 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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-83 IN COMPLEX WITH STX1A;
RP SNAP25 AND VAMP2, AND STRUCTURE BY NMR.
RX PubMed=11832227; DOI=10.1016/s0896-6273(02)00583-4;
RA Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C.,
RA Rizo J.;
RT "Three-dimensional structure of the complexin/SNARE complex.";
RL Neuron 33:397-409(2002).
CC -!- FUNCTION: Positively regulates a late step in exocytosis of various
CC cytoplasmic vesicles, such as synaptic vesicles and other secretory
CC vesicles. Organizes the SNAREs into a cross-linked zigzag topology
CC that, when interposed between the vesicle and plasma membranes, is
CC incompatible with fusion, thereby preventing SNAREs from releasing
CC neurotransmitters until an action potential arrives at the synapse.
CC Also involved in glucose-induced secretion of insulin by pancreatic
CC beta-cells. Essential for motor behavior.
CC {ECO:0000250|UniProtKB:P63040}.
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:11832227, ECO:0000269|PubMed:15911881,
CC ECO:0000269|PubMed:7553862}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15911881,
CC ECO:0000269|PubMed:7553862, ECO:0000269|PubMed:9753100}. Presynapse
CC {ECO:0000269|PubMed:7553862}. Perikaryon {ECO:0000269|PubMed:7553862}.
CC Note=Enriched at synaptic-releasing sites in mature neurons.
CC {ECO:0000269|PubMed:7553862}.
CC -!- TISSUE SPECIFICITY: Nervous system. Strongly expressed in brain, where
CC it is predominant in neurons from cerebral cortex and thalamus (at
CC protein level). {ECO:0000269|PubMed:10051208,
CC ECO:0000269|PubMed:10430466, ECO:0000269|PubMed:15911881,
CC ECO:0000269|PubMed:7553862}.
CC -!- SIMILARITY: Belongs to the complexin/synaphin family. {ECO:0000305}.
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DR EMBL; U35098; AAC52270.1; -; mRNA.
DR EMBL; D70817; BAA11097.1; -; mRNA.
DR EMBL; BC093605; AAH93605.1; -; mRNA.
DR PIR; A57233; A57233.
DR RefSeq; NP_074055.1; NM_022864.3.
DR RefSeq; XP_006250633.1; XM_006250571.3.
DR PDB; 1KIL; X-ray; 2.30 A; E=26-72.
DR PDB; 5W5C; X-ray; 1.85 A; E=1-83.
DR PDB; 5W5D; X-ray; 2.50 A; E=1-83.
DR PDBsum; 1KIL; -.
DR PDBsum; 5W5C; -.
DR PDBsum; 5W5D; -.
DR AlphaFoldDB; P63041; -.
DR BMRB; P63041; -.
DR SMR; P63041; -.
DR BioGRID; 249210; 1.
DR CORUM; P63041; -.
DR DIP; DIP-35502N; -.
DR IntAct; P63041; 6.
DR MINT; P63041; -.
DR STRING; 10116.ENSRNOP00000058432; -.
DR iPTMnet; P63041; -.
DR PhosphoSitePlus; P63041; -.
DR jPOST; P63041; -.
DR PaxDb; P63041; -.
DR PRIDE; P63041; -.
DR GeneID; 64832; -.
DR KEGG; rno:64832; -.
DR UCSC; RGD:70944; rat.
DR CTD; 10815; -.
DR RGD; 70944; Cplx1.
DR VEuPathDB; HostDB:ENSRNOG00000000048; -.
DR eggNOG; ENOG502S3I2; Eukaryota.
DR HOGENOM; CLU_132159_1_0_1; -.
DR InParanoid; P63041; -.
DR OMA; TPIMDIF; -.
DR PhylomeDB; P63041; -.
DR TreeFam; TF315172; -.
DR Reactome; R-RNO-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-RNO-181430; Norepinephrine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-RNO-212676; Dopamine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-264642; Acetylcholine Neurotransmitter Release Cycle.
DR Reactome; R-RNO-888590; GABA synthesis, release, reuptake and degradation.
DR EvolutionaryTrace; P63041; -.
DR PRO; PR:P63041; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Bgee; ENSRNOG00000000060; Expressed in cerebellum and 18 other tissues.
DR Genevisible; P63041; 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: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; IDA:RGD.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0031201; C:SNARE complex; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0070032; C:synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex; IDA:MGI.
DR GO; GO:0043195; C:terminal bouton; HDA:ParkinsonsUK-UCL.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; ISO:RGD.
DR GO; GO:0000149; F:SNARE binding; IDA:RGD.
DR GO; GO:0017075; F:syntaxin-1 binding; IDA:MGI.
DR GO; GO:0098967; P:exocytic insertion of neurotransmitter receptor to postsynaptic membrane; ISO:RGD.
DR GO; GO:0030073; P:insulin secretion; ISO:RGD.
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:0099003; P:vesicle-mediated transport in synapse; ISO:RGD.
DR InterPro; IPR008849; Synaphin.
DR PANTHER; PTHR16705; PTHR16705; 1.
DR Pfam; PF05835; Synaphin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Exocytosis; Neurotransmitter transport;
KW Reference proteome; Synapse; Transport.
FT CHAIN 1..134
FT /note="Complexin-1"
FT /id="PRO_0000144872"
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 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 HELIX 52..70
FT /evidence="ECO:0007829|PDB:5W5C"
SQ SEQUENCE 134 AA; 15122 MW; BA1B6F074923A3A4 CRC64;
MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA KYAKMEAERE
VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA IPPGCGDEPE EEDESILDTV
IKYLPGPLQD MFKK
