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O08736 (CASPC_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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-12
Short name=CASP-12
EC=3.4.22.-
Gene names
Name:Casp12
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length419 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 By similarity.

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by two subunits Potential. Interacts with TRAF2 under resting conditions; this interaction is reduced in ER stress conditions. Ref.4

Tissue specificity

Mainly expressed in skeletal muscle and lung.

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Ontologies

Keywords
   Biological processApoptosis
   Molecular functionHydrolase
Protease
Thiol protease
   PTMZymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processendoplasmic reticulum unfolded protein response

Inferred from direct assay. Source: MGI

virus-infected cell apoptosis

Inferred from direct assay. Source: MGI

   Cellular componentendoplasmic reticulum

Traceable author statement. Source: MGI

   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 – ? PotentialPRO_0000004647
Chain? – 419Caspase-12PRO_0000004648

Regions

Domain1 – 9292CARD

Sites

Active site2501 By similarity
Active site2981 By similarity

Sequences

Sequence LengthMass (Da)Tools
O08736 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B94B0FED16B1CB40

FASTA41947,854
        10         20         30         40         50         60 
MAARRTHERD PIYKIKGLAK DMLDGVFDDL VEKNVLNGDE LLKIGESASF ILNKAENLVE 

        70         80         90        100        110        120 
NFLEKTDMAG KIFAGHIANS QEQLSLQFSN DEDDGPQKIC TPSSPSESKR KVEDDEMEVN 

       130        140        150        160        170        180 
AGLAHESHLM LTAPHGLQSS EVQDTLKLCP RDQFCKIKTE RAKEIYPVME KEGRTRLALI 

       190        200        210        220        230        240 
ICNKKFDYLF DRDNADTDIL NMQELLENLG YSVVLKENLT AQEMETELMQ FAGRPEHQSS 

       250        260        270        280        290        300 
DSTFLVFMSH GILEGICGVK HRNKKPDVLH DDTIFKIFNN SNCRSLRNKP KILIMQACRG 

       310        320        330        340        350        360 
RYNGTIWVST NKGIATADTD EERVLSCKWN NSITKAHVET DFIAFKSSTP HNISWKVGKT 

       370        380        390        400        410 
GSLFISKLID CFKKYCWCYH LEEIFRKVQH SFEVPGELTQ MPTIERVSMT RYFYLFPGN

« Hide

References

« Hide 'large scale' references
[1]"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.
[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. 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.
Tissue: Ovary and Uterus.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N-3.
Tissue: Mammary gland.
[4]"Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress."
Yoneda T., Imaizumi K., Oono K., Yui D., Gomi F., Katayama T., Tohyama M.
J. Biol. Chem. 276:13935-13940(2001) [PubMed: 11278723] [Abstract]
Cited for: INTERACTION WITH TRAF2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		Y13090 mRNA. Translation: CAA73532.1.
AK077256 mRNA. Translation: BAC36712.1.
AK161525 mRNA. Translation: BAE36443.1.
BC028979 mRNA. Translation: AAH28979.1.
IPIIPI00115537.
RefSeqNP_033938.3. NM_009808.4.
UniGeneMm.42163.

3D structure databases

ProteinModelPortalO08736.
SMRO08736. Positions 140-419.
ModBaseSearch...

Protein-protein interaction databases

STRINGO08736.

Protein family/group databases

MEROPSC14.013.

Proteomic databases

PRIDEO08736.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027009; ENSMUSP00000027009; ENSMUSG00000025887.
GeneID12364.
KEGGmmu:12364.
UCSCuc009obx.2. mouse.

Organism-specific databases

CTD100506742.
MGIMGI:1312922. Casp12.

Phylogenomic databases

eggNOGroNOG12982.
HOGENOMHBG505276.
HOVERGENHBG076981.
InParanoidO08736.
OMASWSHHLE.
PhylomeDBO08736.

Gene expression databases

ArrayExpressO08736.
BgeeO08736.
CleanExMM_CASP12.
GenevestigatorO08736.
GermOnlineENSMUSG00000025887. 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.
KOK04741.
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

NextBio457709.
SOURCESearch...

Entry information

Entry nameCASPC_MOUSE
AccessionPrimary (citable) accession number: O08736
Secondary accession number(s): Q3TT82
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 1, 1997
Last modified: November 16, 2011
This is version 109 of the entry and version 1 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents