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P55215 (CASP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Caspase-2

Short name=CASP-2
EC=3.4.22.55
Alternative name(s):
Protease ICH-1
Gene names
Name:Casp2
Synonyms:Ich1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length452 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival By similarity.

Catalytic activity

Strict requirement for an Asp residue at P1, with 316-asp being essential for proteolytic activity and has a preferred cleavage sequence of Val-Asp-Val-Ala-Asp-|-.

Subunit structure

Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a p18 subunit and a p12 subunit. Interacts with LRDD By similarity.

Post-translational modification

The mature protease can process its own propeptide, but not that of other caspases By similarity.

Sequence similarities

Belongs to the peptidase C14A family.

Contains 1 CARD domain.

Sequence caution

The sequence AAB82567.1 differs from that shown. Reason: Frameshift at positions 137 and 189.

Ontologies

Keywords
   Biological processApoptosis
   Coding sequence diversityAlternative splicing
   Molecular functionHydrolase
Protease
Thiol protease
   PTMAcetylation
Phosphoprotein
Zymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Inferred from electronic annotation. Source: Ensembl

aging

Inferred from expression pattern PubMed 12175478. Source: RGD

apoptotic process

Inferred from mutant phenotype PubMed 18614702. Source: RGD

brain development

Inferred from expression pattern PubMed 11741299. Source: RGD

cellular response to mechanical stimulus

Inferred from electronic annotation. Source: Ensembl

ectopic germ cell programmed cell death

Inferred from electronic annotation. Source: Ensembl

extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

luteolysis

Inferred from expression pattern PubMed 16940287. Source: RGD

neural retina development

Inferred from expression pattern PubMed 9809666. Source: RGD

positive regulation of apoptotic signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron apoptotic process

Inferred from mutant phenotype Ref.2. Source: RGD

programmed cell death

Traceable author statement Ref.1. Source: RGD

protein processing

Inferred from electronic annotation. Source: Ensembl

proteolysis

Traceable author statement Ref.1. Source: RGD

   Cellular_componentmembrane

Inferred from direct assay PubMed 16123172. Source: RGD

mitochondrion

Inferred from direct assay PubMed 11716979. Source: RGD

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncysteine-type endopeptidase activity involved in apoptotic process

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P55215-1)

Also known as: caspase-2L;

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.
Isoform 2 (identifier: P55215-2)

Also known as: caspase-2S;

The sequence of this isoform differs from the canonical sequence as follows:
     323-343: DETDRGVDQQDGKNHAQSPGC → GAIGSLGPLLLFTAATASLAL
     344-452: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 169168
PRO_0000043403
Chain170 – 325156Caspase-2 subunit p18 By similarity
PRO_0000044573
Propeptide326 – 3338
PRO_0000044574
Chain334 – 452119Caspase-2 subunit p13 By similarity
PRO_0000004551
Chain348 – 452105Caspase-2 subunit p12 By similarity
PRO_0000004552

Regions

Domain32 – 12190CARD

Sites

Active site2771 By similarity
Active site3201 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3401Phosphoserine By similarity

Natural variations

Alternative sequence323 – 34321DETDR…QSPGC → GAIGSLGPLLLFTAATASLA L in isoform 2.
VSP_016555
Alternative sequence344 – 452109Missing in isoform 2.
VSP_016556

Experimental info

Sequence conflict1451C → Y in AAB82567. Ref.3
Sequence conflict1661D → H in AAB82567. Ref.3
Sequence conflict1771K → E in AAB82567. Ref.3
Sequence conflict1971Q → R in AAB82567. Ref.3
Sequence conflict3401S → P in AAC52260. Ref.4
Sequence conflict348 – 3492AG → TV in AAC52260. Ref.4
Sequence conflict3671G → V in AAC52260. Ref.4
Sequence conflict3731G → D in AAC52260. Ref.4
Sequence conflict376 – 3772AM → PI in AAC52260. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (caspase-2L) [UniParc].

Last modified December 6, 2005. Version 3.
Checksum: 03F9D096BB741CE3

FASTA45250,728
        10         20         30         40         50         60 
MAASSGRSQS SLHRKGLMAA DRRSRILAVC GMHPDHQETL KKNRVVLAKQ LLLSELLEHL 

        70         80         90        100        110        120 
LEKDIITLEM RELIQAKGGS FSQNVELLNL LPKRGPQAFD AFCEALRETR QGHLEDLLLT 

       130        140        150        160        170        180 
TLSDIQHILP PLSCDYDSSL PFSVCESCPP HKQSRLSTDT MEHSLDNGDG PPCLQVKPCT 

       190        200        210        220        230        240 
PEFYQAHYQL AYRLQSQPRG LALVMSNVHF TGEKDLEFRS GGDVDHTTLV TLFKLLGYNV 

       250        260        270        280        290        300 
HVLYDQTAQE MQEKLQNFAQ LPAHRVTDSC IVALLSHGVE GGIYGVDGKL LQLQEVFRLF 

       310        320        330        340        350        360 
DNANCPSLQN KPKMFFIQAC RGDETDRGVD QQDGKNHAQS PGCEESDAGK EELMKMRLPT 

       370        380        390        400        410        420 
RSDMICGYAC LKGNAAMRNT KRGSWYIEAL TQVFSERACD MHVADMLVKV NALIKEREGY 

       430        440        450 
APGTEFHRCK EMSEYCSTLC QQLYLFPGYP PT 

« Hide

Isoform 2 (caspase-2S) [UniParc].

Checksum: 0292D6130C63F641
Show »

FASTA34338,004

References

[1]"Cloning and expression of the cDNA encoding rat caspase-2."
Sato N., Milligan C.E., Uchiyama Y., Oppenheim R.W.
Gene 202:127-132(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Two caspase-2 transcripts are expressed in rat hippocampus after global cerebral ischemia."
Jin K., Nagayama T., Mao X., Kawaguchi K., Hickey R.W., Greenberg D.A., Simon R.P., Graham S.H.
J. Neurochem. 81:25-35(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Strain: Sprague-Dawley.
Tissue: Brain.
[3]"Identification of gene family of caspases in rat kidney and altered expression in ischemia-reperfusion injury."
Kaushal G.P., Singh A.B., Shah S.V.
Am. J. Physiol. 274:F587-F595(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 67-324.
Strain: Sprague-Dawley.
Tissue: Kidney cortex.
[4]"Interleukin-1 beta-converting enzyme-related proteases (IRPs) and mammalian cell death: dissociation of IRP-induced oligonucleosomal endonuclease activity from morphological apoptosis in granulosa cells of the ovarian follicle."
Flaws J.A., Kugu K., Trbovich A.M., Desanti A., Tilly K.I., Hirshfield A.N., Tilly J.L.
Endocrinology 136:5042-5053(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 198-379.
Tissue: Ovary.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U77933 mRNA. Translation: AAB96379.1.
AF136231 mRNA. Translation: AAD33684.1.
AF136232 mRNA. Translation: AAD33685.1.
AF025671 mRNA. Translation: AAB82567.1. Frameshift.
U34684 mRNA. Translation: AAC52260.1.
PIRI67436.
JC6507.
RefSeqNP_071967.2. NM_022522.2.
UniGeneRn.1438.

3D structure databases

ProteinModelPortalP55215.
SMRP55215. Positions 173-333, 355-452.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-48602N.
STRING10116.ENSRNOP00000022672.

Protein family/group databases

MEROPSC14.006.

PTM databases

PhosphoSiteP55215.

Proteomic databases

PaxDbP55215.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000022672; ENSRNOP00000022672; ENSRNOG00000016707. [P55215-1]
GeneID64314.
KEGGrno:64314.
UCSCRGD:69274. rat. [P55215-1]

Organism-specific databases

CTD835.
RGD69274. Casp2.

Phylogenomic databases

eggNOGNOG305976.
GeneTreeENSGT00700000104134.
HOGENOMHOG000290714.
HOVERGENHBG103962.
InParanoidP55215.
KOK02186.
OMAPCLQVKP.
OrthoDBEOG7TTQ7K.
PhylomeDBP55215.
TreeFamTF102023.

Enzyme and pathway databases

BRENDA3.4.22.55. 5301.

Gene expression databases

ArrayExpressP55215.
GenevestigatorP55215.

Family and domain databases

Gene3D1.10.533.10. 1 hit.
InterProIPR001315. CARD.
IPR017350. Caspase_IL-1_beta.
IPR011029. DEATH-like_dom.
IPR011600. Pept_C14_caspase.
IPR001309. Pept_C14_ICE_p20.
IPR016129. Pept_C14_ICE_p20_AS.
IPR002138. Pept_C14_p10.
IPR015917. Pept_C14A_p45_core.
[Graphical view]
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. SSF47986. 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

NextBio612988.
PROP55215.

Entry information

Entry nameCASP2_RAT
AccessionPrimary (citable) accession number: P55215
Secondary accession number(s): O35398, O55194, Q9WUI6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries