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Protein

Protein canopy homolog 3

Gene

Cnpy3

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

Functioni

Toll-like receptor (TLR)-specific co-chaperone for HSP90B1. Required for proper TLR folding, except that of TLR3, and hence controls TLR exit from the endoplasmic reticulum. Consequently, required for both innate and adaptive immune responses.3 Publications

GO - Molecular functioni

  • receptor binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-MMU-1679131. Trafficking and processing of endosomal TLR.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein canopy homolog 3
Alternative name(s):
Protein associated with Tlr4
Trinucleotide repeat-containing gene 5 protein
Gene namesi
Name:Cnpy3
Synonyms:Prat4a, Tnrc5
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1919279. Cnpy3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Disruption phenotypei

Impairs expression of TLR1 and TLR4 on cell surface and lack of ligand-induced TLR9 relocation from the endoplasmic reticulum to endolysosome. Affects TLR responses to whole bacteria and to TLR2, TLR4 and TLR9 ligands.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi95 – 951R → L: Does not affect association with TLR2, TLR4 and TLR9; does not affect cell-surface expression of TLR2, TLR4 and TLR9; does not affect responses of TLR2, TLR4 and TLR9. 1 Publication
Mutagenesisi145 – 1451M → K: Loss of HSP90B1-binding. Impairs association with TLR2 and TLR4; does not impair association with TLR9; partially affects responses of TLR2 and TLR4; affects responses of TLR9; does not affect cell-surface expression of TLR2; affects cell-surface expression of TLR4 and TLR9. 2 Publications
Mutagenesisi231 – 2311S → I: Does not affect association with TLR2, TLR4 and TLR9; does not affect cell-surface expression of TLR2, TLR4 and TLR9; does not affect responses of TLR2, TLR4 and TLR9. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence analysisAdd
BLAST
Chaini27 – 276250Protein canopy homolog 3PRO_0000313781Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi49 ↔ 206By similarity
Disulfide bondi52 ↔ 194By similarity
Disulfide bondi104 ↔ 166By similarity
Glycosylationi153 – 1531N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9DAU1.
MaxQBiQ9DAU1.
PaxDbiQ9DAU1.
PRIDEiQ9DAU1.

PTM databases

iPTMnetiQ9DAU1.
PhosphoSiteiQ9DAU1.

Expressioni

Gene expression databases

BgeeiQ9DAU1.
CleanExiMM_CNPY3.
ExpressionAtlasiQ9DAU1. baseline and differential.
GenevisibleiQ9DAU1. MM.

Interactioni

Subunit structurei

Interacts with HSP90B1; this interaction is disrupted in the presence of ATP. Interacts with TLR1, TLR2, TLR4 and TLR9. Strongest interaction with TLR4.5 Publications

GO - Molecular functioni

  • receptor binding Source: MGI

Protein-protein interaction databases

IntActiQ9DAU1. 3 interactions.
MINTiMINT-4127930.
STRINGi10090.ENSMUSP00000050309.

Structurei

3D structure databases

ProteinModelPortaliQ9DAU1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 269223Saposin B-typeAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili153 – 17927Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the canopy family.Curated
Contains 1 saposin B-type domain.Curated

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG4052. Eukaryota.
ENOG4111GVI. LUCA.
GeneTreeiENSGT00390000014072.
HOGENOMiHOG000030912.
HOVERGENiHBG107736.
InParanoidiQ9DAU1.
OMAiDLTQFLC.
OrthoDBiEOG7SBNPF.
PhylomeDBiQ9DAU1.
TreeFamiTF318951.

Family and domain databases

InterProiIPR021852. DUF3456.
[Graphical view]
PfamiPF11938. DUF3456. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9DAU1-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MESMSELAPR CLLFPLLLLL PLLLLPAPKL GPSPAGAEET DWVRLPSKCE
60 70 80 90 100
VCKYVAVELK SAFEETGKTK EVIDTGYGIL DGKGSGVKYT KSDLRLIEVT
110 120 130 140 150
ETICKRLLDY SLHKERTGSN RFAKGMSETF ETLHNLVHKG VKVVMDIPYE
160 170 180 190 200
LWNETSAEVA DLKKQCDVLV EEFEEVIEDW YRNHQEEDLT EFLCANHVLK
210 220 230 240 250
GKDTSCLAER WSGKKGDIAS LGGKKSKKKR SGVKGSSSGS SKQRKELGGL
260 270
GEDANAEEEE GVQKASPLPH SPPDEL
Length:276
Mass (Da):30,538
Last modified:June 1, 2001 - v1
Checksum:i7C69F60BA3BE1745
GO
Isoform 2 (identifier: Q9DAU1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-125: Missing.

Show »
Length:151
Mass (Da):16,771
Checksum:iC28FA56F99670FBA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti256 – 2561A → AE in BAD90134 (PubMed:15449545).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 125125Missing in isoform 2. 1 PublicationVSP_030134Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361644 mRNA. Translation: AAK52494.1.
AK005532 mRNA. Translation: BAB24103.1.
AK031742 mRNA. Translation: BAC27534.1.
AK049358 mRNA. Translation: BAC33707.1.
AK082340 mRNA. Translation: BAC38471.1.
AK082749 mRNA. Translation: BAC38599.1.
AK085617 mRNA. Translation: BAC39489.1.
AK086940 mRNA. Translation: BAC39769.1.
AK143428 mRNA. Translation: BAE25373.1.
BC013549 mRNA. Translation: AAH13549.1.
AK220209 mRNA. Translation: BAD90134.1.
CCDSiCCDS28839.1. [Q9DAU1-1]
RefSeqiNP_001292917.1. NM_001305988.1.
NP_001292918.1. NM_001305989.1. [Q9DAU1-2]
NP_001292919.1. NM_001305990.1. [Q9DAU1-2]
NP_082341.1. NM_028065.4. [Q9DAU1-1]
XP_006525020.1. XM_006524957.2. [Q9DAU1-2]
XP_006525021.1. XM_006524958.2. [Q9DAU1-2]
XP_006525022.1. XM_006524959.1. [Q9DAU1-2]
UniGeneiMm.240325.

Genome annotation databases

EnsembliENSMUST00000059844; ENSMUSP00000050309; ENSMUSG00000023973. [Q9DAU1-1]
GeneIDi72029.
KEGGimmu:72029.
UCSCiuc008cuf.2. mouse. [Q9DAU1-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF361644 mRNA. Translation: AAK52494.1.
AK005532 mRNA. Translation: BAB24103.1.
AK031742 mRNA. Translation: BAC27534.1.
AK049358 mRNA. Translation: BAC33707.1.
AK082340 mRNA. Translation: BAC38471.1.
AK082749 mRNA. Translation: BAC38599.1.
AK085617 mRNA. Translation: BAC39489.1.
AK086940 mRNA. Translation: BAC39769.1.
AK143428 mRNA. Translation: BAE25373.1.
BC013549 mRNA. Translation: AAH13549.1.
AK220209 mRNA. Translation: BAD90134.1.
CCDSiCCDS28839.1. [Q9DAU1-1]
RefSeqiNP_001292917.1. NM_001305988.1.
NP_001292918.1. NM_001305989.1. [Q9DAU1-2]
NP_001292919.1. NM_001305990.1. [Q9DAU1-2]
NP_082341.1. NM_028065.4. [Q9DAU1-1]
XP_006525020.1. XM_006524957.2. [Q9DAU1-2]
XP_006525021.1. XM_006524958.2. [Q9DAU1-2]
XP_006525022.1. XM_006524959.1. [Q9DAU1-2]
UniGeneiMm.240325.

3D structure databases

ProteinModelPortaliQ9DAU1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9DAU1. 3 interactions.
MINTiMINT-4127930.
STRINGi10090.ENSMUSP00000050309.

PTM databases

iPTMnetiQ9DAU1.
PhosphoSiteiQ9DAU1.

Proteomic databases

EPDiQ9DAU1.
MaxQBiQ9DAU1.
PaxDbiQ9DAU1.
PRIDEiQ9DAU1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000059844; ENSMUSP00000050309; ENSMUSG00000023973. [Q9DAU1-1]
GeneIDi72029.
KEGGimmu:72029.
UCSCiuc008cuf.2. mouse. [Q9DAU1-1]

Organism-specific databases

CTDi10695.
MGIiMGI:1919279. Cnpy3.

Phylogenomic databases

eggNOGiKOG4052. Eukaryota.
ENOG4111GVI. LUCA.
GeneTreeiENSGT00390000014072.
HOGENOMiHOG000030912.
HOVERGENiHBG107736.
InParanoidiQ9DAU1.
OMAiDLTQFLC.
OrthoDBiEOG7SBNPF.
PhylomeDBiQ9DAU1.
TreeFamiTF318951.

Enzyme and pathway databases

ReactomeiR-MMU-1679131. Trafficking and processing of endosomal TLR.

Miscellaneous databases

PROiQ9DAU1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAU1.
CleanExiMM_CNPY3.
ExpressionAtlasiQ9DAU1. baseline and differential.
GenevisibleiQ9DAU1. MM.

Family and domain databases

InterProiIPR021852. DUF3456.
[Graphical view]
PfamiPF11938. DUF3456. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Trapping and characterization of novel retinoid response elements."
    Glozak M.A., Li Y., Reuille R., Kim K.H., Vo M.N., Rogers M.B.
    Mol. Endocrinol. 17:27-41(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Embryonic carcinoma.
  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] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Cerebellum, Embryonic stem cell, Fetal head, Kidney, Lung, Ovary and Placenta.
  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] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Kidney.
  4. "Prediction of the coding sequences of mouse homologues of FLJ genes: the complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.
    DNA Res. 11:127-135(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-276 (ISOFORM 1).
    Tissue: Spleen.
  5. "A molecule that is associated with Toll-like receptor 4 and regulates its cell surface expression."
    Konno K., Wakabayashi Y., Akashi-Takamura S., Ishii T., Kobayashi M., Takahashi K., Kusumoto Y., Saitoh S., Yoshizawa Y., Miyake K.
    Biochem. Biophys. Res. Commun. 339:1076-1082(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLR4.
  6. Cited for: FUNCTION, INTERACTION WITH TLR4.
  7. "A protein associated with Toll-like receptor (TLR) 4 (PRAT4A) is required for TLR-dependent immune responses."
    Takahashi K., Shibata T., Akashi-Takamura S., Kiyokawa T., Wakabayashi Y., Tanimura N., Kobayashi T., Matsumoto F., Fukui R., Kouro T., Nagai Y., Takatsu K., Saitoh S., Miyake K.
    J. Exp. Med. 204:2963-2976(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH TLR1 AND TLR9, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  8. "A single base mutation in the PRAT4A gene reveals differential interaction of PRAT4A with Toll-like receptors."
    Kiyokawa T., Akashi-Takamura S., Shibata T., Matsumoto F., Nishitani C., Kuroki Y., Seto Y., Miyake K.
    Int. Immunol. 20:1407-1415(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TLR2; TLR4 AND TLR9, MUTAGENESIS OF ARG-95; MET-145 AND SER-231.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  10. "Folding of Toll-like receptors by the HSP90 paralogue gp96 requires a substrate-specific cochaperone."
    Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
    Nat. Commun. 1:79-79(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HSP90B1 AND TLR9, SUBCELLULAR LOCATION, MUTAGENESIS OF MET-145.
  11. Erratum
    Liu B., Yang Y., Qiu Z., Staron M., Hong F., Li Y., Wu S., Li Y., Hao B., Bona R., Han D., Li Z.
    Nat. Commun. 3:653-653(2012)

Entry informationi

Entry nameiCNPY3_MOUSE
AccessioniPrimary (citable) accession number: Q9DAU1
Secondary accession number(s): Q571I0
, Q8BUS5, Q8BUV5, Q8C0C5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 97 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.