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Protein

Complexin-2

Gene

Cplx2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Negatively regulates the formation of synaptic vesicle clustering at active zone to the presynaptic membrane in postmitotic neurons. Positively regulates a late step in synaptic vesicle exocytosis. Also involved in mast cell exocytosis. Although not essential for development, seems critical for the acquisition of higher cognitive functions in the adult brain.3 Publications

GO - Molecular functioni

  1. syntaxin-1 binding Source: MGI

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. mast cell degranulation Source: UniProtKB-KW
  3. nervous system development Source: UniProtKB-KW
  4. positive regulation of synaptic plasticity Source: UniProtKB
  5. synaptic vesicle exocytosis Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Differentiation, Exocytosis, Mast cell degranulation, Neurogenesis, Neurotransmitter transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Complexin-2
Alternative name(s):
921-L
Complexin II
Short name:
CPX II
Synaphin-1
Gene namesi
Name:Cplx2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 13

Organism-specific databases

MGIiMGI:104726. Cplx2.

Subcellular locationi

Cytoplasmcytosol 1 Publication
Note: Enriched at synaptic-releasing sites in mature neurons.

GO - Cellular componenti

  1. cytosol Source: UniProtKB-SubCell
  2. dendrite Source: MGI
  3. mast cell granule Source: GOC
  4. neuronal cell body Source: MGI
  5. synapse Source: MGI
  6. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Mice show no obvious phenotypic changes and no significant motor deficiencies. However, they show abnormalities in a number of complex behaviors including exploration, socialization, motor coordination, learning and reversal learning.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 134134Complexin-2PRO_0000144876Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei93 – 931PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP84086.
PaxDbiP84086.
PRIDEiP84086.

PTM databases

PhosphoSiteiP84086.

Expressioni

Tissue specificityi

Nervous system. Expressed predominantly in brain, where it is present in many regions, including hippocampus and cerebellum. In the retina, present at conventional amacrine cell synapses (at protein level).2 Publications

Developmental stagei

In the brain, expression starts at P6 and increases to reach a plateau at P20.1 Publication

Gene expression databases

BgeeiP84086.
CleanExiMM_CPLX2.
GenevestigatoriP84086.

Interactioni

Subunit structurei

Binds to the SNARE core complex containing SNAP25, VAMP2 and STX1A.By similarity

Protein-protein interaction databases

IntActiP84086. 1 interaction.
MINTiMINT-4153241.

Structurei

3D structure databases

ProteinModelPortaliP84086.
SMRiP84086. Positions 32-72.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni41 – 9757Interaction with the SNARE complexBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili28 – 8457Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the complexin/synaphin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG85303.
GeneTreeiENSGT00490000043416.
HOGENOMiHOG000017716.
HOVERGENiHBG062792.
InParanoidiP84086.
KOiK15294.
OMAiAMEQPCE.
OrthoDBiEOG71G9XG.
PhylomeDBiP84086.
TreeFamiTF315172.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P84086-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDFVMKQALG GATKDMGKML GGEEEKDPDA QKKEEERQEA LRQQEEERKA
60 70 80 90 100
KHARMEAERE KVRQQIRDKY GLKKKEEKEA EEKAALEQPC EGSLTRPKKA
110 120 130
IPAGCGDEEE EEEESILDTV LKYLPGPLQD MFKK
Length:134
Mass (Da):15,394
Last modified:August 16, 2004 - v1
Checksum:i7791812FD4194AC5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35101 Genomic DNA. Translation: AAC52272.1.
D38613 mRNA. Translation: BAA07604.1.
BN000501 mRNA. Translation: CAG26661.1.
BN000502 mRNA. Translation: CAG26662.1.
CCDSiCCDS36667.1.
PIRiS66293. D57233.
RefSeqiNP_034076.1. NM_009946.3.
UniGeneiMm.268902.

Genome annotation databases

EnsembliENSMUST00000026985; ENSMUSP00000026985; ENSMUSG00000025867.
GeneIDi12890.
KEGGimmu:12890.
UCSCiuc029sbi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35101 Genomic DNA. Translation: AAC52272.1.
D38613 mRNA. Translation: BAA07604.1.
BN000501 mRNA. Translation: CAG26661.1.
BN000502 mRNA. Translation: CAG26662.1.
CCDSiCCDS36667.1.
PIRiS66293. D57233.
RefSeqiNP_034076.1. NM_009946.3.
UniGeneiMm.268902.

3D structure databases

ProteinModelPortaliP84086.
SMRiP84086. Positions 32-72.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP84086. 1 interaction.
MINTiMINT-4153241.

PTM databases

PhosphoSiteiP84086.

Proteomic databases

MaxQBiP84086.
PaxDbiP84086.
PRIDEiP84086.

Protocols and materials databases

DNASUi12890.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000026985; ENSMUSP00000026985; ENSMUSG00000025867.
GeneIDi12890.
KEGGimmu:12890.
UCSCiuc029sbi.1. mouse.

Organism-specific databases

CTDi10814.
MGIiMGI:104726. Cplx2.

Phylogenomic databases

eggNOGiNOG85303.
GeneTreeiENSGT00490000043416.
HOGENOMiHOG000017716.
HOVERGENiHBG062792.
InParanoidiP84086.
KOiK15294.
OMAiAMEQPCE.
OrthoDBiEOG71G9XG.
PhylomeDBiP84086.
TreeFamiTF315172.

Miscellaneous databases

ChiTaRSiCplx2. mouse.
NextBioi282490.
PROiP84086.
SOURCEiSearch...

Gene expression databases

BgeeiP84086.
CleanExiMM_CPLX2.
GenevestigatoriP84086.

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].
    Strain: 129/Sv.
    Tissue: Brain.
  2. "Identification of two highly homologous presynaptic proteins distinctly localized at the dendritic and somatic synapses."
    Takahashi S., Yamamoto H., Matsuda Z., Ogawa M., Yagyu K., Taniguchi T., Miyata T., Kaba H., Higuchi T., Okutani F., Fujimoto S.
    FEBS Lett. 368:455-460(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Strain: BALB/c.
    Tissue: Brain.
  3. "Structural organization of the human complexin 2 gene (CPLX2) and aspects of its functional activity."
    Raevskaya N.M., Dergunova L.V., Vladychenskaya I.P., Stavchansky V.V., Oborina M.V., Poltaraus A.B., Limborska S.A.
    Gene 359:127-137(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
    Tissue: Brain.
  4. "Complexins regulate a late step in Ca2+-dependent neurotransmitter release."
    Reim K., Mansour M., Varoqueaux F., McMahon H.T., Suedhof T.C., Brose N., Rosenmund C.
    Cell 104:71-81(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Complexin II is essential for normal neurological function in mice."
    Glynn D., Bortnick R.A., Morton A.J.
    Hum. Mol. Genet. 12:2431-2448(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "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: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  8. "Transcriptional inhibition of REST by NeuroD2 during neuronal differentiation."
    Ravanpay A.C., Hansen S.J., Olson J.M.
    Mol. Cell. Neurosci. 44:178-189(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiCPLX2_MOUSE
AccessioniPrimary (citable) accession number: P84086
Secondary accession number(s): O09056
, Q13329, Q28184, Q32KK4, Q64386
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: March 4, 2015
This is version 78 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.