Skip Header

Contribute Send feedback
Read comments (?) or add your own

P43367 (CAN2_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 106. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length324 AA.
Sequence statusFragment.
Protein existenceEvidence at transcript 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 By similarity. Cell membrane By similarity. Note: Translocates to the plasma membrane upon Ca2+ binding By similarity.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the peptidase C2 family.

Contains at least 2 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

cysteine-type peptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 324›324Calpain-2 catalytic subunit
PRO_0000207703

Regions

Domain190 – 22435EF-hand 1
Domain226 – 26136EF-hand 2
Calcium binding209 – 220121
Calcium binding239 – 250122
Region‹1 – 138›138Domain III
Region139 – 15315Linker
Region158 – 324167Domain IV

Sites

Metal binding1661Calcium 5; via carbonyl oxygen By similarity
Metal binding1691Calcium 5 By similarity
Metal binding1711Calcium 5; via carbonyl oxygen By similarity
Metal binding1761Calcium 5 By similarity
Metal binding2091Calcium 6 By similarity
Metal binding2111Calcium 6 By similarity
Metal binding2131Calcium 6; via carbonyl oxygen By similarity
Metal binding2151Calcium 6; via carbonyl oxygen By similarity
Metal binding2201Calcium 6 By similarity
Metal binding2391Calcium 7 By similarity
Metal binding2411Calcium 7 By similarity
Metal binding2431Calcium 7; via carbonyl oxygen By similarity
Metal binding2451Calcium 7; via carbonyl oxygen By similarity
Metal binding2501Calcium 7 By similarity
Metal binding2821Calcium 1 By similarity
Metal binding2851Calcium 1 By similarity

Experimental info

Sequence conflict2021R → K in AAB17381. Ref.2
Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P43367 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 3929553239E123CF

FASTA32437,809
        10         20         30         40         50         60 
YPNTFWMNPQ YLIKLEEEDE DQEDGESGCT FLVGLIQKHR RRQRKMGEDM HTIGFGIYEV 

        70         80         90        100        110        120 
PEELTGQTNI HLSKNFFLTH RARERSDTFI NLREVLNRFK LPPGEYILVP STFEPNKDGD 

       130        140        150        160        170        180 
FCIRVFSEKK ADYQVVDDEI EADLEENDAS EDDIDDGFRR LFAQLAGEDA EISAFELQTI 

       190        200        210        220        230        240 
LRRVLAKRQD IKSDGFSIET CRIMVDMLDS DGSAKLGLKE FYILWTKIQK YQKIYREIDV 

       250        260        270        280        290        300 
DRSGTMNSYE MRKALEEAGF KLPCQLHQVI VARFADDQLI IDFDNFVRCL VRLETLFRIS 

       310        320 
KQLDSENTGT IELDLISWLC FSVL

« Hide

References

[1]"Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle."
Sun W., Ji S.Q., Ebert P.J., Bidwell C.A., Hancock D.L.
Biochimie 75:931-936(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-209.
Tissue: Skeletal muscle.
[2]"Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells."
Zhang J.L., Patel J.M., Block E.R.
Am. J. Physiol. 275:L461-L468(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 122-324.
Tissue: Pulmonary artery.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U01181 mRNA. Translation: AAC48401.1.
U71320 mRNA. Translation: AAB17381.1.
UniGeneSsc.49836.

3D structure databases

ProteinModelPortalP43367.
SMRP43367. Positions 1-324.
ModBaseSearch...

Protein family/group databases

MEROPSC02.002.

Proteomic databases

PRIDEP43367.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG012645.

Enzyme and pathway databases

BRENDA3.4.22.53. 6170.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
[Graphical view]
SMARTSM00720. calpain_III. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF49758. Peptidase_C2. 1 hit.
PROSITEPS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 1 hit.
PS00640. THIOL_PROTEASE_ASN. Partial match.
PS00139. THIOL_PROTEASE_CYS. Partial match.
PS00639. THIOL_PROTEASE_HIS. Partial match.
[Graphical view]
ProtoNetSearch...

Other

BindingDBP43367.
ChEMBLCHEMBL4143.

Entry information

Entry nameCAN2_PIG
AccessionPrimary (citable) accession number: P43367
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1997
Last modified: May 1, 2013
This is version 106 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

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