Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q27971 (CAN2_BOVIN)

Last modified June 16, 2009. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Calpain-2 catalytic subunit
    EC=3.4.22.53
Alternative name(s):
    Calpain-2 large subunit
    Calcium-activated neutral proteinase 2
      Short name=CANP 2
    Calpain M-type
    M-calpain
    Millimolar-calpain
Gene names
Name: CAPN2
OrganismBos taurus (Bovine)
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 3 calcium ions.

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 1 calpain catalytic domain.

Contains 3 EF-hand domains.

Sequence caution

The sequence AAA18455.1 differs from that shown. Reason: Frameshift at positions 470 and 480.

Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandCalcium
   Molecular functionHydrolase
Protease
Thiol protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   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: UniProtKB-KW

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

Initiator methionine11Removed By similarity
Propeptide2 – 1918Anchors to the small subunit Potential
PRO_0000317423
Chain20 – 700681Calpain-2 catalytic subunit
PRO_0000207702

Regions

Domain45 – 344300Calpain catalytic
Domain572 – 60534EF-hand 1
Domain602 – 63736EF-hand 2
Domain667 – 70034EF-hand 3
Calcium binding585 – 596121 By similarity
Calcium binding615 – 626122 By similarity
Region345 – 514170Domain III By similarity
Region515 – 52915Linker By similarity
Region530 – 700171Domain IV By similarity

Sites

Active site1051 By similarity
Active site2621 By similarity
Active site2861 By similarity

Experimental info

Sequence conflict4171R → Q in AAA18455. Ref.2
Sequence conflict460 – 4623ERS → DV in AAA18455. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q27971-1 [UniParc].

Last modified February 5, 2008. Version 2.
Checksum: 00FD932E9C6AB268

FASTA70079,935
        10         20         30         40         50         60 
MAGIAAKLAK DREAAEGLGS HERAVKYLNQ DYAALRDECL EAGALFQDPS FPALPSSLGF 

        70         80         90        100        110        120 
KELGPYSSKT RGIEWKRPTE ICDNPQFITG GATRTDICQG ALGDCWLLAA IASLTLNEEI 

       130        140        150        160        170        180 
LARVVPLDQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL 

       190        200        210        220        230        240 
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKA PPNLFRIIQK ALQKGSLLGC 

       250        260        270        280        290        300 
SIDITSAADS EAITFQKLVK GHAYSVTGAE EVESRGSLQK LIRIRNPWGE VEWTGQWNDN 

       310        320        330        340        350        360 
CPNWNTVDPE VRETLTRQHE DGEFWMSFND FLRHYSRLEI CNLTPDTLTS DSYKKWKLTK 

       370        380        390        400        410        420 
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDQED GESGCTFLVG LIQKHRRRQR 

       430        440        450        460        470        480 
KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK KFFLTTRARE RSDTFINLRE VLNRFKLPPG 

       490        500        510        520        530        540 
EYIVVPSTFE PNKDGDFCIR VFSEKKADYQ VVDDEIEANI DEIDISEDDI DDGFRRLFAQ 

       550        560        570        580        590        600 
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL 

       610        620        630        640        650        660 
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDDLIIDFD 

       670        680        690        700 
NFVRCLIRLE TLFRIFKQLD PENTGMIQLD LISWLSFSVL 

« Hide

References

« Hide 'large scale' references
[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[2]"Cloning the partial cDNA's for the calpain family of protease genes from bovine muscle."
Sun W., Bidwell C.A., Ji S., Hancock D.L.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 377-585.
Tissue: Skeletal muscle.

Cross-references

Sequence databases

BC134526 mRNA. Translation: AAI34527.1.
U07850 mRNA. Translation: AAA18455.1. Frameshift.
IPIIPI00695673.
RefSeqNP_001096556.1.
UniGeneBt.60825

3D structure databases

HSSPHSSP built from PDB template 1KFX based on UniProtKB P17655.
ModBaseSearch...

Protein family/group databases

MEROPSC02.002.

Genome annotation databases

EnsemblENSBTAG00000012778. Bos taurus. [Contig view]
GeneID281662.
KEGGbta:281662.

Phylogenomic databases

HOVERGENQ27971.
OMAQ27971. LTKMDGN.

Enzyme and pathway databases

BRENDA3.4.22.53. 251.

Family and domain databases

InterProIPR011992. EF-Hand_type.
IPR018247. EF_HAND_1.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2.
[Graphical view]
Gene3DG3DSA:1.10.238.10. EF-Hand_type. 1 hit.
PfamPF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
PS00639. THIOL_PROTEASE_HIS. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN2_BOVIN
AccessionPrimary (citable) accession number: Q27971
Secondary accession number(s): A4IFD3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: June 16, 2009
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents