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Protein

Caspase recruitment domain-containing protein 9

Gene

Card9

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

Functioni

Adapter protein that plays a key role in innate immune response to a number of intracellular pathogens, such as C.albicans and L.monocytogenes. Is at the crossroads of ITAM-tyrosine kinase and the Toll-like receptors (TLR) and NOD2 signaling pathways. Probably controls various innate immune response pathways depending on the intracellular pathogen. In response to L.monocytogenes infection, acts by connecting NOD2 recognition of peptidoglycan to downstream activation of MAP kinases (MAPK) without activating NF-kappa-B. In response to fungal infection, may be required for the development and subsequent differentiation of interleukin 17-producing T helper (TH-17) cells. Also involved in activation of myeloid cells via classical ITAM-associated receptors and TLR: required for TLR-mediated activation of MAPK, while it is not required for TLR-induced activation of NF-kappa-B (By similarity). Controls CLEC7A (dectin-1)-mediated myeloid cell activation induced by the yeast cell wall component zymosan, leading to cytokine production and innate anti-fungal immunity: acts by regulating BCL10-MALT1-mediated NF-kappa-B activation pathway. Activates NF-kappa-B via BCL10. In response to the hyphal form of C.albicans, mediates CLEC6A (dectin-2)-induced I-kappa-B kinase ubiquitination, leading to NF-kappa-B activation via interaction with BCL10.By similarity1 Publication

GO - Molecular functioni

  • protein domain specific binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Enzyme and pathway databases

ReactomeiR-RNO-5607764. CLEC7A (Dectin-1) signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Caspase recruitment domain-containing protein 9
Short name:
rCARD9
Gene namesi
Name:Card9
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi708370. Card9.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi526 – 5261T → A: Abolished phosphorylation by CK2 and increased activation of NF-kappa-B; when associated with A-528; A-531 and A-533. 1 Publication
Mutagenesisi528 – 5281S → A: Abolished phosphorylation by CK2 and increased activation of NF-kappa-B; when associated with A-526; A-531 and A-533. 1 Publication
Mutagenesisi531 – 5311T → A: Abolished phosphorylation by CK2 and increased activation of NF-kappa-B; when associated with A-526; A-528 and A-533. 1 Publication
Mutagenesisi533 – 5331T → A: Abolished phosphorylation by CK2 and increased activation of NF-kappa-B; when associated with A-526; A-528 and A-531. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536Caspase recruitment domain-containing protein 9PRO_0000144083Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei424 – 4241PhosphoserineCombined sources
Modified residuei425 – 4251PhosphoserineCombined sources
Modified residuei431 – 4311PhosphoserineBy similarity
Modified residuei451 – 4511PhosphoserineCombined sources
Modified residuei461 – 4611PhosphoserineCombined sources
Modified residuei531 – 5311Phosphothreonine; by CK21 Publication
Modified residuei533 – 5331Phosphothreonine; by CK21 Publication

Post-translational modificationi

Phosphorylated at Thr-531 and Thr-533 by CK2 following interaction with VHL, leading to inhibit the ability to activate NF-kappa-B.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9EPY0.
PRIDEiQ9EPY0.

PTM databases

iPTMnetiQ9EPY0.
PhosphoSiteiQ9EPY0.

Expressioni

Gene expression databases

GenevisibleiQ9EPY0. RN.

Interactioni

Subunit structurei

Self-associates. Interacts (via CARD domain) with BCL10 (via CARD domain). Interacts with NOD2 (via NACHT domain) (By similarity). Interacts with RIPK2 (By similarity). Interacts with VHL; without leading to protein degradation (PubMed:17936701).By similarity1 Publication

GO - Molecular functioni

  • protein domain specific binding Source: RGD

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025456.

Structurei

3D structure databases

ProteinModelPortaliQ9EPY0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 9893CARDPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili117 – 277161Sequence analysisAdd
BLAST
Coiled coili303 – 420118Sequence analysisAdd
BLAST

Sequence similaritiesi

Contains 1 CARD domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IE3N. Eukaryota.
ENOG410Y2EE. LUCA.
GeneTreeiENSGT00530000063108.
HOGENOMiHOG000231538.
HOVERGENiHBG058091.
InParanoidiQ9EPY0.
KOiK12794.
OrthoDBiEOG747PH5.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9EPY0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDYENDDEC WSALESFRVK LISVIDPSRI TPYLRQCKVL NPDDEEQVLS
60 70 80 90 100
DPNLVIRKRK VGVLLDILQR TGHKGYVAFL ESLELYYPQL YRKVTGKEPA
110 120 130 140 150
RVFSMIIDAS GESGLTQLLM TEVMKLQKKV QDLTALLSSK DDFIKELRVK
160 170 180 190 200
DSLLRKHQER VQRLKEECEL SSAELKRCKD ENYDLAMRLA HLSEEKGAAL
210 220 230 240 250
MRNRDLQLEV DQLRHSLMKA EDDCKVERKH TLKLRHAMEQ RPSQELLWDL
260 270 280 290 300
QQERDLLQAR VQELEVSVQE GKLHRNSPYI QVLEEDWRQA LQEHQEQAST
310 320 330 340 350
IFSLRKDLRQ AEALRTRCME EKEMFELQCL ALRKDAKMYK DRIEAILQQM
360 370 380 390 400
EEVSIERDQA MTSREELHAQ CAQSFQDKDK LRKQVRELDE KADELQLQLF
410 420 430 440 450
QTESRLLAAE GRLKQQQLDM LILSSDLEDS SPRNSQELSL PQDLEEDAQL
460 470 480 490 500
SDKGVLADRE SPEQPFVVLN KKHLSQTHDT VPSSSEPPEK ERRRLKESFE
510 520 530
NYRRKRALRK MQNSWRQGEG DHGNTTGSDN TDTEGS
Length:536
Mass (Da):62,632
Last modified:March 1, 2001 - v1
Checksum:i6F33089CB7E6BAC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311288 mRNA. Translation: AAG28791.1.
AABR06021907 Genomic DNA. No translation available.
RefSeqiNP_071639.1. NM_022303.1.
UniGeneiRn.64486.

Genome annotation databases

EnsembliENSRNOT00000091484; ENSRNOP00000074450; ENSRNOG00000051470.
GeneIDi64171.
KEGGirno:64171.
UCSCiRGD:708370. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF311288 mRNA. Translation: AAG28791.1.
AABR06021907 Genomic DNA. No translation available.
RefSeqiNP_071639.1. NM_022303.1.
UniGeneiRn.64486.

3D structure databases

ProteinModelPortaliQ9EPY0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000025456.

PTM databases

iPTMnetiQ9EPY0.
PhosphoSiteiQ9EPY0.

Proteomic databases

PaxDbiQ9EPY0.
PRIDEiQ9EPY0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000091484; ENSRNOP00000074450; ENSRNOG00000051470.
GeneIDi64171.
KEGGirno:64171.
UCSCiRGD:708370. rat.

Organism-specific databases

CTDi64170.
RGDi708370. Card9.

Phylogenomic databases

eggNOGiENOG410IE3N. Eukaryota.
ENOG410Y2EE. LUCA.
GeneTreeiENSGT00530000063108.
HOGENOMiHOG000231538.
HOVERGENiHBG058091.
InParanoidiQ9EPY0.
KOiK12794.
OrthoDBiEOG747PH5.

Enzyme and pathway databases

ReactomeiR-RNO-5607764. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

NextBioi35576475.
PROiQ9EPY0.

Gene expression databases

GenevisibleiQ9EPY0. RN.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR001315. CARD.
IPR011029. DEATH-like_dom.
[Graphical view]
PfamiPF00619. CARD. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
PROSITEiPS50209. CARD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "CARD9 is a novel caspase recruitment domain-containing protein that interacts with Bcl10/CLAP and activates NF-kappa B."
    Bertin J., Guo Y., Wang L., Srinivasula S.M., Jacobson M.D., Poyet J.-L., Merriam S., Du M.-Q., Dyer M.J.S., Robison K.E., DiStefano P.S., Alnemri E.S.
    J. Biol. Chem. 275:41082-41086(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2."
    Yang H., Minamishima Y.A., Yan Q., Schlisio S., Ebert B.L., Zhang X., Zhang L., Kim W.Y., Olumi A.F., Kaelin W.G. Jr.
    Mol. Cell 28:15-27(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-531 AND THR-533, MUTAGENESIS OF THR-526; SER-528; THR-531 AND THR-533, FUNCTION, INTERACTION WITH VHL.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-424; SER-425; SER-451 AND SER-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCARD9_RAT
AccessioniPrimary (citable) accession number: Q9EPY0
Secondary accession number(s): F1LQK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: March 1, 2001
Last modified: January 20, 2016
This is version 93 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. 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.