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Protein

Complexin-1

Gene

Cplx1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Positively regulates a late step in exocytosis of various cytoplasmic vesicles, such as synaptic vesicles and other secretory vesicles. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells. Essential for motor behavior.By similarity

GO - Molecular functioni

  • neurotransmitter transporter activity Source: Ensembl
  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: MGI

GO - Biological processi

  • insulin secretion Source: Ensembl
  • synaptic vesicle exocytosis Source: RGD
Complete GO annotation...

Keywords - Biological processi

Exocytosis, Neurotransmitter transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-181430. Norepinephrine Neurotransmitter Release Cycle.
R-RNO-210500. Glutamate Neurotransmitter Release Cycle.
R-RNO-264642. Acetylcholine Neurotransmitter Release Cycle.
R-RNO-888590. GABA synthesis, release, reuptake and degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Complexin-1
Alternative name(s):
Complexin I
Short name:
CPX I
Synaphin-2
Gene namesi
Name:Cplx1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 14

Organism-specific databases

RGDi70944. Cplx1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB-SubCell
  • dendrite Source: MGI
  • neuronal cell body Source: MGI
  • protein complex Source: RGD
  • synapse Source: MGI
  • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: MGI
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Complexin-1PRO_0000144872Add
BLAST

Proteomic databases

PaxDbiP63041.
PRIDEiP63041.

PTM databases

iPTMnetiP63041.
PhosphoSiteiP63041.

Expressioni

Tissue specificityi

Nervous system. Strongly expressed in brain, where it is predominant in neurons from cerebral cortex and thalamus (at protein level).4 Publications

Gene expression databases

GenevisibleiP63041. RN.

Interactioni

Subunit structurei

Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A.5 Publications

GO - Molecular functioni

  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: MGI

Protein-protein interaction databases

DIPiDIP-35502N.
IntActiP63041. 4 interactions.
STRINGi10116.ENSRNOP00000058432.

Structurei

Secondary structure

1
134
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 7036Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30E26-72[»]
ProteinModelPortaliP63041.
SMRiP63041. Positions 32-72.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63041.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 7023Interaction with the SNARE complexAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili29 – 6436Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the complexin/synaphin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IWGS. Eukaryota.
ENOG4111MX0. LUCA.
GeneTreeiENSGT00490000043416.
HOGENOMiHOG000017716.
HOVERGENiHBG062792.
InParanoidiP63041.
KOiK15294.
OMAiTVMKFIP.
OrthoDBiEOG71G9XG.
PhylomeDBiP63041.
TreeFamiTF315172.

Family and domain databases

InterProiIPR008849. Synaphin.
[Graphical view]
PANTHERiPTHR16705. PTHR16705. 1 hit.
PfamiPF05835. Synaphin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P63041-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEFVMKQALG GATKDMGKML GGDEEKDPDA AKKEEERQEA LRQAEEERKA
60 70 80 90 100
KYAKMEAERE VMRQGIRDKY GIKKKEEREA EAQAAMEANS EGSLTRPKKA
110 120 130
IPPGCGDEPE EEDESILDTV IKYLPGPLQD MFKK
Length:134
Mass (Da):15,122
Last modified:August 31, 2004 - v1
Checksum:iBA1B6F074923A3A4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35098 mRNA. Translation: AAC52270.1.
D70817 mRNA. Translation: BAA11097.1.
BC093605 mRNA. Translation: AAH93605.1.
PIRiA57233.
RefSeqiNP_074055.1. NM_022864.3.
XP_006250633.1. XM_006250571.2.
UniGeneiRn.10133.

Genome annotation databases

EnsembliENSRNOT00000061720; ENSRNOP00000058432; ENSRNOG00000000060.
GeneIDi64832.
KEGGirno:64832.
UCSCiRGD:70944. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35098 mRNA. Translation: AAC52270.1.
D70817 mRNA. Translation: BAA11097.1.
BC093605 mRNA. Translation: AAH93605.1.
PIRiA57233.
RefSeqiNP_074055.1. NM_022864.3.
XP_006250633.1. XM_006250571.2.
UniGeneiRn.10133.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30E26-72[»]
ProteinModelPortaliP63041.
SMRiP63041. Positions 32-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-35502N.
IntActiP63041. 4 interactions.
STRINGi10116.ENSRNOP00000058432.

PTM databases

iPTMnetiP63041.
PhosphoSiteiP63041.

Proteomic databases

PaxDbiP63041.
PRIDEiP63041.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000061720; ENSRNOP00000058432; ENSRNOG00000000060.
GeneIDi64832.
KEGGirno:64832.
UCSCiRGD:70944. rat.

Organism-specific databases

CTDi10815.
RGDi70944. Cplx1.

Phylogenomic databases

eggNOGiENOG410IWGS. Eukaryota.
ENOG4111MX0. LUCA.
GeneTreeiENSGT00490000043416.
HOGENOMiHOG000017716.
HOVERGENiHBG062792.
InParanoidiP63041.
KOiK15294.
OMAiTVMKFIP.
OrthoDBiEOG71G9XG.
PhylomeDBiP63041.
TreeFamiTF315172.

Enzyme and pathway databases

ReactomeiR-RNO-181430. Norepinephrine Neurotransmitter Release Cycle.
R-RNO-210500. Glutamate Neurotransmitter Release Cycle.
R-RNO-264642. Acetylcholine Neurotransmitter Release Cycle.
R-RNO-888590. GABA synthesis, release, reuptake and degradation.

Miscellaneous databases

EvolutionaryTraceiP63041.
PROiP63041.

Gene expression databases

GenevisibleiP63041. RN.

Family and domain databases

InterProiIPR008849. Synaphin.
[Graphical view]
PANTHERiPTHR16705. PTHR16705. 1 hit.
PfamiPF05835. Synaphin. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complexins: cytosolic proteins that regulate SNAP receptor function."
    McMahon H.T., Missler M., Li C., Suedhof T.C.
    Cell 83:111-119(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 19-49; 55-69 AND 74-96, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT.
    Tissue: Brain.
  2. "Distinct regional distribution in the brain of messenger RNAs for the two isoforms of synaphin associated with the docking/fusion complex."
    Ishizuka T., Saisu H., Odani S., Kumanishi T., Abe T.
    Neuroscience 88:295-306(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Regulatory roles of complexins in neurotransmitter release from mature presynaptic nerve terminals."
    Ono S., Baux G., Sekiguchi M., Fossier P., Morel N.F., Nihonmatsu I., Hirata K., Awaji T., Takahashi S., Takahashi M.
    Eur. J. Neurosci. 10:2143-2152(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Immunohistochemical distribution of the two isoforms of synaphin/complexin involved in neurotransmitter release: localization at the distinct central nervous system regions and synaptic types."
    Yamada M., Saisu H., Ishizuka T., Takahashi H., Abe T.
    Neuroscience 93:7-18(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions."
    Pabst S., Hazzard J.W., Antonin W., Suedhof T.C., Jahn R., Rizo J., Fasshauer D.
    J. Biol. Chem. 275:19808-19818(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  7. "Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis."
    Pabst S., Margittai M., Vainius D., Langen R., Jahn R., Fasshauer D.
    J. Biol. Chem. 277:7838-7848(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Structurally and functionally unique complexins at retinal ribbon synapses."
    Reim K., Wegmeyer H., Brandstaetter J.H., Xue M., Rosenmund C., Dresbach T., Hofmann K., Brose N.
    J. Cell Biol. 169:669-680(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  9. "Three-dimensional structure of the complexin/SNARE complex."
    Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J.
    Neuron 33:397-409(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 26-83 IN COMPLEX WITH STX1A; SNAP25 AND VAMP2, STRUCTURE BY NMR.

Entry informationi

Entry nameiCPLX1_RAT
AccessioniPrimary (citable) accession number: P63041
Secondary accession number(s): O09057
, O09142, Q566D7, Q64276
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: June 8, 2016
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.