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P06814 (CAN2_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Calpain-2 catalytic subunit
EC=3.4.22.53
Alternative name(s):
Calcium-activated neutral proteinase 2
Short name=CANP 2
Calpain M-type
Calpain-2 large subunit
Millimolar-calpain
Short name=M-calpain
Gene names
Name:CAPN2
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length422 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Calcium-regulated non-lysosomal thiol-protease which catalyze limited proteolysis of substrates involved in cytoskeletal remodeling and signal transduction By similarity.

Catalytic activity

Broad endopeptidase specificity.

Cofactor

Binds 7 calcium ions By similarity.

Enzyme regulation

Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.

Subunit structure

Forms a heterodimer with a small (regulatory) subunit (CAPNS1).

Subcellular location

Cytoplasm. Cell membrane. Note: Translocates to the plasma membrane upon Ca2+ binding.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase C2 family.

Contains 1 calpain catalytic domain.

Contains 3 EF-hand domains.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandCalcium
Metal-binding
   Molecular functionHydrolase
Protease
Thiol protease
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processproteolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 422›422Calpain-2 catalytic subunit
PRO_0000207704

Regions

Domain‹1 – 66›66Calpain catalytic
Domain294 – 32734EF-hand 1
Domain324 – 35936EF-hand 2
Domain389 – 42234EF-hand 3
Calcium binding307 – 318121 Ref.2
Calcium binding337 – 348122 Ref.2
Region67 – 236170Domain III
Region237 – 25115Linker
Region252 – 422171Domain IV

Sites

Active site81 By similarity
Metal binding141Calcium 4 By similarity
Metal binding211Calcium 4 By similarity
Metal binding451Calcium 4; via carbonyl oxygen By similarity
Metal binding2641Calcium 5; via carbonyl oxygen By similarity
Metal binding2671Calcium 5 By similarity
Metal binding2691Calcium 5; via carbonyl oxygen By similarity
Metal binding2741Calcium 5 By similarity
Metal binding3071Calcium 6 By similarity
Metal binding3091Calcium 6 By similarity
Metal binding3111Calcium 6; via carbonyl oxygen By similarity
Metal binding3131Calcium 6; via carbonyl oxygen By similarity
Metal binding3181Calcium 6 By similarity
Metal binding3371Calcium 7 By similarity
Metal binding3391Calcium 7 By similarity
Metal binding3411Calcium 7; via carbonyl oxygen By similarity
Metal binding3431Calcium 7; via carbonyl oxygen By similarity
Metal binding3481Calcium 7 By similarity
Metal binding3801Calcium 1 By similarity
Metal binding3831Calcium 1 By similarity

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P06814 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: AE4FA3C48A333C41

FASTA42249,494
        10         20         30         40         50         60 
QKLIRIRNPW GEVEWTGRWN DNCPNWNTVD PEVRERLAER HEDGEFWMSF SDFLRHYSRL 

        70         80         90        100        110        120 
EICNLTPDTL TSDTYKKWKL TKMDGNWRRG STAGGCRNYP NTFWMNPQYV IKLEEEDEDQ 

       130        140        150        160        170        180 
EDGESGCTFL VGLIQKHRRR QRKMGEDMHT IGFGIYEVPE ELRGQTNIHL GKNFFLTTRA 

       190        200        210        220        230        240 
RERSDTFINL REVLNRFKLP PGEYILVPST FEPNKNGDFC VRVFSEKKAD YQAVDDEIEA 

       250        260        270        280        290        300 
DLEEADVSED DIDDGFRRLF AQLAGEDAEI SAFELQNILR RVLAKRQDIK TDGLSIETCK 

       310        320        330        340        350        360 
IMVDMLDSDG TGKLGLKEFY VLWTKIQKYQ KIYREIDVDR SGTMNSYEMR KALEEAGFKL 

       370        380        390        400        410        420 
PCQLHEVIVA RFADDQLIID FDNFVRCLVR LETLFKIFKQ LDPDNTGMIQ LDLISWLCFS 


VL

« Hide

References

[1]"Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease."
Emori Y., Kawasaki H., Sugihara H., Imajoh S., Kawashima S., Suzuki K.
J. Biol. Chem. 261:9465-9471(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions."
Minami Y., Emori Y., Kawasaki H., Suzuki K.
J. Biochem. 101:889-895(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING DATA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M13797 mRNA. Translation: AAA31455.1.
PIRB24815.
UniGeneOcu.1954.

3D structure databases

ProteinModelPortalP06814.
SMRP06814. Positions 1-422.
ModBaseSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000017627.

Protein family/group databases

MEROPSC02.019.

Proteomic databases

PRIDEP06814.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG327523.
HOGENOMHOG000232035.
HOVERGENHBG012645.
OrthoDBEOG4RR6GS.

Enzyme and pathway databases

BRENDA3.4.22.53. 1749.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00720. calpain_III. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMSSF49758. Peptidase_C2. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00640. THIOL_PROTEASE_ASN. Partial match.
PS00139. THIOL_PROTEASE_CYS. Partial match.
PS00639. THIOL_PROTEASE_HIS. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN2_RABIT
AccessionPrimary (citable) accession number: P06814
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 1, 2013
This is version 115 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

SIMILARITY comments

Index of protein domains and families

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