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P70343 (CASP4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-4

Short name=CASP-4
EC=3.4.22.64
Alternative name(s):
Caspase-11
Short name=CASP-11
Protease ICH-3

Cleaved into the following 2 chains:

  1. Caspase-4 subunit p10
  2. Caspase-4 subunit p20
Gene names
Name:Casp4
Synonyms:Casp11, Caspl, Ich3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the activation cascade of caspases responsible for apoptosis execution. Promotes IL-1 beta processing by ICE, so may also have a role in inflammatory responses.

Catalytic activity

Strict requirement for Asp at the P1 position and has a preferred cleavage sequence of (Ile/Leu/Val/Phe)-Gly-His-Asp-|-.

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 10 kDa (p10) subunit.

Tissue specificity

Mostly expressed in lung and spleen; weaker in heart and lung; little in liver, skeletal muscle, kidney and testis. Not found in the brain.

Induction

Activity increased 30-fold by endotoxins (LPS).

Post-translational modification

The two subunits are derived from the precursor sequence by a autocatalytic mechanism.

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Ontologies

Keywords
   Biological processApoptosis
   Molecular functionHydrolase
Protease
Thiol protease
   PTMPhosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processapoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Inferred from mutant phenotype. Source: MGI

   Cellular componentintracellular

Inferred from electronic annotation. Source: InterPro

   Molecular functioncysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 8080 Potential
PRO_0000004600
Chain81 – 266186Caspase-4 subunit p20
PRO_0000004601
Propeptide267 – 28519 Potential
PRO_0000004602
Chain286 – 37388Caspase-4 subunit p10
PRO_0000004603

Regions

Domain1 – 9191CARD

Sites

Active site2061 By similarity
Active site2541

Amino acid modifications

Modified residue831Phosphoserine By similarity

Experimental info

Mutagenesis2541C → G: No cell death.
Sequence conflict1521N → K in AAB09469. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P70343 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 110D7AA75E71C2B3

FASTA37342,742
        10         20         30         40         50         60 
MAENKHPDKP LKVLEQLGKE VLTEYLEKLV QSNVLKLKEE DKQKFNNAER SDKRWVFVDA 

        70         80         90        100        110        120 
MKKKHSKVGE MLLQTFFSVD PGSHHGEANL EMEEPEESLN TLKLCSPEEF TRLCREKTQE 

       130        140        150        160        170        180 
IYPIKEANGR TRKALIICNT EFKHLSLRYG ANFDIIGMKG LLEDLGYDVV VKEELTAEGM 

       190        200        210        220        230        240 
ESEMKDFAAL SEHQTSDSTF LVLMSHGTLH GICGTMHSEK TPDVLQYDTI YQIFNNCHCP 

       250        260        270        280        290        300 
GLRDKPKVII VQACRGGNSG EMWIRESSKP QLCRGVDLPR NMEADAVKLS HVEKDFIAFY 

       310        320        330        340        350        360 
STTPHHLSYR DKTGGSYFIT RLISCFRKHA CSCHLFDIFL KVQQSFEKAS IHSQMPTIDR 

       370 
ATLTRYFYLF PGN 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of Ich-3, a member of the interleukin-1beta converting enzyme (ICE)/Ced-3 family and an upstream regulator of ICE."
Wang S., Miura M., Jung Y.-K., Zhu H., Gagliardini V., Shi L., Greenberg A.H., Yuan J.
J. Biol. Chem. 271:20580-20587(1996) [PubMed: 8702803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6 X CBA.
Tissue: Thymus.
[2]"Characterization of seven murine caspase family members."
van de Craen M., Vandenabeele P., Declercq W., van den Brande I., van Loo G., Molemans F., Schotte P., van Criekinge W., Beyaert R., Fiers W.
FEBS Lett. 403:61-69(1997) [PubMed: 9038361] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/An.
[3]"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. expand/collapse author list , 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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow and Spleen.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59463 mRNA. Translation: AAB09469.1.
Y13089 mRNA. Translation: CAA73531.1.
AK151547 mRNA. Translation: BAE30493.1.
AK171877 mRNA. Translation: BAE42715.1.
CH466636 Genomic DNA. Translation: EDL09318.1.
IPIIPI00108178.
RefSeqNP_031635.2. NM_007609.2.
UniGeneMm.1569.

3D structure databases

ProteinModelPortalP70343.
SMRP70343. Positions 96-373.
ModBaseSearch...

Protein-protein interaction databases

STRINGP70343.

Protein family/group databases

MEROPSC14.012.

PTM databases

PhosphoSiteP70343.

Proteomic databases

PRIDEP70343.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027012; ENSMUSP00000027012; ENSMUSG00000033538.
GeneID12363.
KEGGmmu:12363.

Organism-specific databases

CTD837.
MGIMGI:107700. Casp4.

Phylogenomic databases

eggNOGmaNOG09574.
HOGENOMHBG505276.
HOVERGENHBG076981.
InParanoidP70343.
OrthoDBEOG49W2FS.

Enzyme and pathway databases

BRENDA3.4.22.57. 3474.

Gene expression databases

ArrayExpressP70343.
BgeeP70343.
CleanExMM_CASP4.
GenevestigatorP70343.
GermOnlineENSMUSG00000033538. Mus musculus.

Family and domain databases

InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
IPR011029. DEATH-like.
IPR011600. Pept_C14_cat.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR002398. Pept_C14_p45.
IPR015917. Pept_C14_p45_core.
[Graphical view]
Gene3DG3DSA:1.10.533.10. DEATH_like. 1 hit.
KOK12808.
PANTHERPTHR10454. Pept_C14_p45. 1 hit.
PfamPF00619. CARD. 1 hit.
PF00656. Peptidase_C14. 1 hit.
[Graphical view]
PIRSFPIRSF038001. Caspase_ICE. 1 hit.
PRINTSPR00376. IL1BCENZYME.
SMARTSM00114. CARD. 1 hit.
SM00115. CASc. 1 hit.
[Graphical view]
SUPFAMSSF47986. DEATH_like. 1 hit.
PROSITEPS50209. CARD. 1 hit.
PS01122. CASPASE_CYS. 1 hit.
PS01121. CASPASE_HIS. 1 hit.
PS50207. CASPASE_P10. 1 hit.
PS50208. CASPASE_P20. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio457710.
PMAP-CutDBQ3TAF3.
SOURCESearch...

Entry information

Entry nameCASP4_MOUSE
AccessionPrimary (citable) accession number: P70343
Secondary accession number(s): O08735, Q3TAF3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: December 14, 2011
This is version 98 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families