Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Copine-6

Gene

Cpne6

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

Functioni

Calcium-dependent phospholipid-binding protein that plays a role in calcium-mediated intracellular processes. Binds phospholipid membranes in a calcium-dependent manner (PubMed:9886090). Plays a role in dendrite formation by melanocytes (By similarity).By similarity1 Publication

GO - Molecular functioni

  • phosphatidylserine binding Source: MGI

GO - Biological processi

  • cellular response to calcium ion Source: UniProtKB
  • positive regulation of dendrite extension Source: MGI
Complete GO annotation...

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

ReactomeiR-MMU-1483206. Glycerophospholipid biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Copine-6Curated
Alternative name(s):
Copine VIBy similarityImported
Neuronal-copine1 Publication
Short name:
N-copine1 Publication
Gene namesi
Name:Cpne6Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 14

Organism-specific databases

MGIiMGI:1334445. Cpne6.

Subcellular locationi

GO - Cellular componenti

  • axon Source: MGI
  • clathrin-coated endocytic vesicle Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • dendrite Source: MGI
  • endosome Source: UniProtKB-SubCell
  • extracellular exosome Source: MGI
  • membrane Source: MGI
  • perikaryon Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi33 – 331D → N: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-35; N-93 and N-96. 1 Publication
Mutagenesisi35 – 351D → N: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-93 and N-96. 1 Publication
Mutagenesisi93 – 931D → N: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-35 and N-96. 1 Publication
Mutagenesisi96 – 961D → N: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with N-33; N-35 and N-93. 1 Publication
Mutagenesisi167 – 1671D → N: Inhibits strongly calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-173. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-173; N-229 and N-231. 1 Publication
Mutagenesisi173 – 1731D → N: Inhibits strongly calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-167. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-229 and N-231. 1 Publication
Mutagenesisi229 – 2291D → N: Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-231. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-173 and N-231. 1 Publication
Mutagenesisi231 – 2311D → N: Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits strongly calcium-dependent translocation to the cell membrane; when associated with N-229. Leads to the constitutive (calcium-independent) attachment to the cell membrane; when associated with N-167; N-173 and N-229. 1 Publication
Mutagenesisi272 – 2721K → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-273 and A-274. 1 Publication
Mutagenesisi273 – 2731K → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-272 and A-274. 1 Publication
Mutagenesisi274 – 2741K → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with A-272 and A-273. 1 Publication
Mutagenesisi282 – 2821V → G: Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-283 and G-284. 1 Publication
Mutagenesisi282 – 2821V → S: Inhibits calcium-dependent translocation to the cell membrane; when associated with S-283 and S-284. 1 Publication
Mutagenesisi283 – 2831V → G: Does not inhibit calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-282 and G-284. 1 Publication
Mutagenesisi283 – 2831V → S: Inhibits calcium-dependent translocation to the cell membrane; when associated with S-282 and S-284. 1 Publication
Mutagenesisi284 – 2841L → G: Inhibits partially calcium-dependent translocation to the cell membrane. Inhibits calcium-dependent translocation to the cell membrane; when associated with G-282 and G-283. 1 Publication
Mutagenesisi284 – 2841L → S: Inhibits calcium-dependent translocation to the cell membrane; when associated with S-282 and S-283. 1 Publication
Mutagenesisi286 – 2861Q → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-287 and G-288. 1 Publication
Mutagenesisi287 – 2871C → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-286 and G-288. 1 Publication
Mutagenesisi288 – 2881T → A: Does not inhibit calcium-dependent translocation to the cell membrane; when associated with G-286 and G-287. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 557557Copine-6PRO_0000144846Add
BLAST

Proteomic databases

EPDiQ9Z140.
MaxQBiQ9Z140.
PaxDbiQ9Z140.
PeptideAtlasiQ9Z140.
PRIDEiQ9Z140.

PTM databases

iPTMnetiQ9Z140.
PhosphoSiteiQ9Z140.

Expressioni

Tissue specificityi

Expressed in the brain (PubMed:9645480). Expressed in pyramidal cells, granule cells, and neurons in the dentate gyrus of the hippocampus and in granule cells of the olfactory bulb (at protein level). Expressed in pyramidal cells of the CA1-CA3 regions, in granule cells of the dentate gyrus, in granule cells of the olfactory bulbs, in the mitral cell layer and in neurons of the cerebral cortex layer II, brainstem and spinal cord (PubMed:9886090). Not detected in glial cells (PubMed:9645480, PubMed:9886090).2 Publications

Inductioni

Up-regulated by long-term potentiation (PubMed:9645480). Up-regulated by kainate in an NMDA-type glutamate receptor-dependent manner (PubMed:9645480).1 Publication

Gene expression databases

BgeeiQ9Z140.
CleanExiMM_CPNE6.
ExpressionAtlasiQ9Z140. baseline and differential.
GenevisibleiQ9Z140. MM.

Interactioni

Subunit structurei

Interacts (via second C2 domain) with OS9 (via C-terminus); this interaction occurs in a calcium-dependent manner in vitro (PubMed:10403379). May interact with NECAB1 (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi198861. 2 interactions.
IntActiQ9Z140. 3 interactions.
MINTiMINT-4091900.
STRINGi10090.ENSMUSP00000073847.

Structurei

3D structure databases

ProteinModelPortaliQ9Z140.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 11188C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini138 – 243106C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini306 – 526221VWFAPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni244 – 30360Linker region2 PublicationsAdd
BLAST

Domaini

The C2 domain 1 binds phospholipids in a calcium-independent manner and is not necessary for calcium-mediated translocation and association to the plasma membrane (PubMed:9886090, PubMed:26175110). The C2 domain 2 binds phospholipids in a calcium-dependent manner and is necessary for calcium-mediated translocation and association to the plasma membrane (PubMed:9886090, PubMed:26175110). The linker region contributes to the calcium-dependent translocation and association to the plasma membrane (PubMed:21087455, PubMed:26175110). The VWFA domain is necessary for association with intracellular clathrin-coated vesicles in a calcium-dependent manner (PubMed:21087455).3 Publications

Sequence similaritiesi

Belongs to the copine family.Curated
Contains 2 C2 domains.PROSITE-ProRule annotation
Contains 1 VWFA domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG1327. Eukaryota.
ENOG410XPC8. LUCA.
GeneTreeiENSGT00760000119085.
HOGENOMiHOG000220898.
HOVERGENiHBG066841.
InParanoidiQ9Z140.
OMAiDMSDPEM.
PhylomeDBiQ9Z140.
TreeFamiTF316419.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.40.50.410. 1 hit.
InterProiIPR000008. C2_dom.
IPR010734. Copine.
IPR002035. VWF_A.
[Graphical view]
PfamiPF00168. C2. 2 hits.
PF07002. Copine. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF53300. SSF53300. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Z140-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDPEMGWVP EPPAMTLGAS RVELRVSCHG LLDRDTLTKP HPCVLLKLYS
60 70 80 90 100
DEQWVEVERT EVLRSCSSPV FSRVLAIEYF FEEKQPLQFH VFDAEDGATS
110 120 130 140 150
PSSDTFLGST ECTLGQIVSQ TKVTKPLLLK NGKTAGKSTI TIVAEEVSGT
160 170 180 190 200
NDYVQLTFRA HKLDNKDLFS KSDPFMEIYK TNGDQSDQLV WRTEVVKNNL
210 220 230 240 250
NPSWEPFRLS LHSLCSCDIH RPLKFLVYDY DSSGKHDFIG EFTSTFQEMQ
260 270 280 290 300
EGTANPGQEM QWDCINPKYR DKKKNYKSSG TVVLAQCTVE KVHTFLDYIM
310 320 330 340 350
GGCQISFTVA IDFTASNGDP RSSQSLHCLS PRQPNHYLQA LRTVGGICQD
360 370 380 390 400
YDSDKRFPAF GFGARIPPNF EVSHDFAINF DPENPECEEI SGVIASYRRC
410 420 430 440 450
LPQIQLYGPT NVAPIINRVA EPAQREQSTG QATKYSVLLV LTDGVVSDMA
460 470 480 490 500
ETRTAIVRAS RLPMSIIIVG VGNADFSDMR LLDGDDGPLR CPKGVPAARD
510 520 530 540 550
IVQFVPFRDF KDAAPSALAK CVLAEVPRQV VEYYASQGIS PGAPRPSTPA

MTPSPSP
Length:557
Mass (Da):61,781
Last modified:May 1, 1999 - v1
Checksum:i043D6C1487E2ECAC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008893 mRNA. Translation: BAA75898.1.
BC050766 mRNA. Translation: AAH50766.1.
CCDSiCCDS27112.1.
RefSeqiNP_001129529.1. NM_001136057.2.
NP_034077.1. NM_009947.3.
XP_006518569.1. XM_006518506.2.
UniGeneiMm.5249.

Genome annotation databases

EnsembliENSMUST00000074225; ENSMUSP00000073847; ENSMUSG00000022212.
ENSMUST00000163767; ENSMUSP00000126493; ENSMUSG00000022212.
ENSMUST00000171643; ENSMUSP00000128555; ENSMUSG00000022212.
GeneIDi12891.
KEGGimmu:12891.
UCSCiuc007tyr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB008893 mRNA. Translation: BAA75898.1.
BC050766 mRNA. Translation: AAH50766.1.
CCDSiCCDS27112.1.
RefSeqiNP_001129529.1. NM_001136057.2.
NP_034077.1. NM_009947.3.
XP_006518569.1. XM_006518506.2.
UniGeneiMm.5249.

3D structure databases

ProteinModelPortaliQ9Z140.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198861. 2 interactions.
IntActiQ9Z140. 3 interactions.
MINTiMINT-4091900.
STRINGi10090.ENSMUSP00000073847.

PTM databases

iPTMnetiQ9Z140.
PhosphoSiteiQ9Z140.

Proteomic databases

EPDiQ9Z140.
MaxQBiQ9Z140.
PaxDbiQ9Z140.
PeptideAtlasiQ9Z140.
PRIDEiQ9Z140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000074225; ENSMUSP00000073847; ENSMUSG00000022212.
ENSMUST00000163767; ENSMUSP00000126493; ENSMUSG00000022212.
ENSMUST00000171643; ENSMUSP00000128555; ENSMUSG00000022212.
GeneIDi12891.
KEGGimmu:12891.
UCSCiuc007tyr.2. mouse.

Organism-specific databases

CTDi9362.
MGIiMGI:1334445. Cpne6.

Phylogenomic databases

eggNOGiKOG1327. Eukaryota.
ENOG410XPC8. LUCA.
GeneTreeiENSGT00760000119085.
HOGENOMiHOG000220898.
HOVERGENiHBG066841.
InParanoidiQ9Z140.
OMAiDMSDPEM.
PhylomeDBiQ9Z140.
TreeFamiTF316419.

Enzyme and pathway databases

ReactomeiR-MMU-1483206. Glycerophospholipid biosynthesis.

Miscellaneous databases

PROiQ9Z140.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z140.
CleanExiMM_CPNE6.
ExpressionAtlasiQ9Z140. baseline and differential.
GenevisibleiQ9Z140. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
3.40.50.410. 1 hit.
InterProiIPR000008. C2_dom.
IPR010734. Copine.
IPR002035. VWF_A.
[Graphical view]
PfamiPF00168. C2. 2 hits.
PF07002. Copine. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 2 hits.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 2 hits.
SSF53300. SSF53300. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS50234. VWFA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "N-copine: a novel two C2-domain-containing protein with neuronal activity-regulated expression."
    Nakayama T., Yaoi T., Yasui M., Kuwajima G.
    FEBS Lett. 428:80-84(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION, TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "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.
  3. "Ca2(+)-dependent interaction of N-copine, a member of the two C2 domain protein family, with OS-9, the product of a gene frequently amplified in osteosarcoma."
    Nakayama T., Yaoi T., Kuwajima G., Yoshie O., Sakata T.
    FEBS Lett. 453:77-80(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OS9.
  4. "Localization and subcellular distribution of N-copine in mouse brain."
    Nakayama T., Yaoi T., Kuwajima G.
    J. Neurochem. 72:373-379(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain and Liver.
  6. "Copines-1, -2, -3, -6 and -7 show different calcium-dependent intracellular membrane translocation and targeting."
    Perestenko P.V., Pooler A.M., Noorbakhshnia M., Gray A., Bauccio C., Jeffrey McIlhinney R.A.
    FEBS J. 277:5174-5189(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN.
  7. "The second C2-domain of copines -2, -6 and -7 is responsible for their calcium-dependent membrane association."
    Perestenko P., Watanabe M., Beusnard-Bee T., Guna P., McIlhinney J.
    FEBS J. 282:3722-3736(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF ASP-33; ASP-35; ASP-93; ASP-96; ASP-167; ASP-173; ASP-229; ASP-231; LYS-272; LYS-273; LYS-274; VAL-282; VAL-283; LEU-284; GLN-286; CYS-287 AND THR-288.

Entry informationi

Entry nameiCPNE6_MOUSE
AccessioniPrimary (citable) accession number: Q9Z140
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: July 6, 2016
This is version 113 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

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.