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Protein

Copine-3

Gene

Cpne3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Calcium-dependent phospholipid-binding protein that plays a role in ERBB2-mediated tumor cell migration in response to growth factor heregulin stimulation.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-MMU-1483206. Glycerophospholipid biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Copine-3Curated
Alternative name(s):
Copine IIIBy similarityImported
Gene namesi
Name:Cpne3Imported
Synonyms:Kiaa0636
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1917818. Cpne3.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity
  • Cell membrane By similarity
  • Cell junction By similarity
  • Cell junctionfocal adhesion By similarity

  • Note: Associates to the membrane in a calcium-dependent manner. Translocates to the cell membrane and the nucleus in a calcium- or growth factor heregulin-dependent manner. Colocalizes with the tyrosine phosphorylated ERBB2 form at cell membrane and focal adhesions in a calcium- or growth factor heregulin-dependent manner.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 533533Copine-3PRO_0000144839Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141PhosphoserineBy similarity
Modified residuei197 – 1971PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on serine and threonine residues.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8BT60.
MaxQBiQ8BT60.
PaxDbiQ8BT60.
PRIDEiQ8BT60.

PTM databases

iPTMnetiQ8BT60.
PhosphoSiteiQ8BT60.

Expressioni

Gene expression databases

BgeeiQ8BT60.
CleanExiMM_CPNE3.
GenevisibleiQ8BT60. MM.

Interactioni

Subunit structurei

Monomer. Interacts with ERBB2 (preferentially with the tyrosine phosphorylated form); this interaction occurs at the cell membrane and is increased in a growth factor heregulin-dependent manner. Interacts with SHC1; this interaction may mediate the binding of CPNE3 with ERBB2. Interacts with RACK1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

IntActiQ8BT60. 2 interactions.
MINTiMINT-4091865.
STRINGi10090.ENSMUSP00000029885.

Structurei

3D structure databases

ProteinModelPortaliQ8BT60.
SMRiQ8BT60. Positions 8-254.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 9998C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini125 – 230106C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini291 – 513223VWFAPROSITE-ProRule annotationAdd
BLAST

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.
InParanoidiQ8BT60.
OMAiIDYYFEL.
OrthoDBiEOG77DJ57.
PhylomeDBiQ8BT60.
TreeFamiTF316419.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
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. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BT60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAQCVTKVE LNVSCNNLLD ADVTSKSDPL CVLFLNTSGH QWYEVERTER
60 70 80 90 100
IKNSLNPKFS KTFVIDYYFE VVQKLKFGIY DIDNKTIELS DDDFLGECEV
110 120 130 140 150
TLGQIVSSKK LTRPLVLKNG KPAGKGSITI SAEEIKDNRV VLFEMEARKL
160 170 180 190 200
DNKDLFGKSD PYLEFHKQTS DGHWLMVHRT EVIKNNLNPM WKPFKISLNS
210 220 230 240 250
LCYGDMDKTI KVECYDYDND GSHDLIGTFQ TTMTKLKEAS RSSPVEYECI
260 270 280 290 300
NEKKRQKKKS YKNSGVISVK HCEITVECTF LDYIMGGCQL NFTVGVDFTG
310 320 330 340 350
SNGDPSSPDS LHYISPNGVN EYLTAIWSVG LVIQDYDADK MFPAFGFGAQ
360 370 380 390 400
VPPQWQVSHE FPMNFNPSNP YCNGIQGIVE AYRTCLPQIR LYGPTNFSPI
410 420 430 440 450
INHVARFAAA ATQQQTASQY FVLLIITDGV ITDLDETRQA IVNAAKLPMS
460 470 480 490 500
IIIVGVGGAD FSAMEFLDGD GGSLRAPSGE VAIRDIVQFV PFRQFQNAPK
510 520 530
EALAQCVLAE IPQQVVGYFN TYKLLPPKNP AVK
Length:533
Mass (Da):59,585
Last modified:June 7, 2005 - v2
Checksum:iF76A4BDCA11C7F2E
GO

Sequence cautioni

The sequence BAD90244.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti37 – 371T → A in BAC25524 (PubMed:16141072).Curated
Sequence conflicti471 – 53363GGSLR…NPAVK → EWKSPCPFRRGGHKRYCSVC AFQTVPECSKRSACSVCLGR DSPAGGGLLQHIQTPSSQKP SCEVEEPGQLQDFKSCVEQR HLSHRMMYLPSALLTPGYMM in BAC25524 (PubMed:16141072).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220348 mRNA. Translation: BAD90244.1. Different initiation.
AK017651 mRNA. Translation: BAC25524.1.
BC090632 mRNA. Translation: AAH90632.1.
CCDSiCCDS17991.1.
RefSeqiNP_082045.1. NM_027769.2.
UniGeneiMm.38390.

Genome annotation databases

EnsembliENSMUST00000029885; ENSMUSP00000029885; ENSMUSG00000028228.
GeneIDi70568.
KEGGimmu:70568.
UCSCiuc008sby.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK220348 mRNA. Translation: BAD90244.1. Different initiation.
AK017651 mRNA. Translation: BAC25524.1.
BC090632 mRNA. Translation: AAH90632.1.
CCDSiCCDS17991.1.
RefSeqiNP_082045.1. NM_027769.2.
UniGeneiMm.38390.

3D structure databases

ProteinModelPortaliQ8BT60.
SMRiQ8BT60. Positions 8-254.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8BT60. 2 interactions.
MINTiMINT-4091865.
STRINGi10090.ENSMUSP00000029885.

PTM databases

iPTMnetiQ8BT60.
PhosphoSiteiQ8BT60.

Proteomic databases

EPDiQ8BT60.
MaxQBiQ8BT60.
PaxDbiQ8BT60.
PRIDEiQ8BT60.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029885; ENSMUSP00000029885; ENSMUSG00000028228.
GeneIDi70568.
KEGGimmu:70568.
UCSCiuc008sby.1. mouse.

Organism-specific databases

CTDi8895.
MGIiMGI:1917818. Cpne3.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG1327. Eukaryota.
ENOG410XPC8. LUCA.
GeneTreeiENSGT00760000119085.
HOGENOMiHOG000220898.
HOVERGENiHBG066841.
InParanoidiQ8BT60.
OMAiIDYYFEL.
OrthoDBiEOG77DJ57.
PhylomeDBiQ8BT60.
TreeFamiTF316419.

Enzyme and pathway databases

ReactomeiR-MMU-1483206. Glycerophospholipid biosynthesis.

Miscellaneous databases

PROiQ8BT60.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BT60.
CleanExiMM_CPNE3.
GenevisibleiQ8BT60. MM.

Family and domain databases

Gene3Di2.60.40.150. 2 hits.
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. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
    Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiCPNE3_MOUSE
AccessioniPrimary (citable) accession number: Q8BT60
Secondary accession number(s): Q5CZX9, Q5DU22
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: June 7, 2005
Last modified: June 8, 2016
This is version 103 of the entry and version 2 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.