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Reviewed, UniProtKB/Swiss-Prot Q07009 (CAN2_RAT)

Last modified June 16, 2009. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

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Protein attributes

Sequence length700 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

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

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.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

Capns1Q645371EBI-1040438,EBI-918712
srp-6O014621EBI-1040438,EBI-1549936From a different organism.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Propeptide2 – 1918Anchors to the small subunit Potential
PRO_0000026493
Chain20 – 700681Calpain-2 catalytic subunit
PRO_0000026494

Regions

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

Sites

Active site1051
Active site2621
Active site2861

Experimental info

Mutagenesis1051C → S: Loss of activity. Ref.5
Mutagenesis2261K → S: 12% decrease in activity.
Mutagenesis2301K → E: 84% decrease in activity. Ref.4
Mutagenesis2301K → S: No effect. Ref.4
Mutagenesis2341K → E: 85% decrease in activity. Ref.4
Mutagenesis2341K → S: 20% decrease in activity. Ref.4
Mutagenesis2621H → A: Loss of activity. Ref.5
Mutagenesis2861N → A: Loss of activity. Ref.5
Mutagenesis2881W → Y: 95% decrease in activity. Ref.5
Mutagenesis5041E → S: 10% decrease in activity. Ref.4

Secondary structure

1 .................................................................................................... 700
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q07009-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 296B0DC3BEEF5B90

FASTA70079,919
        10         20         30         40         50         60 
MAGIAMKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS FPALPSSLGF 

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

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

       190        200        210        220        230        240 
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC 

       250        260        270        280        290        300 
SIDITSAADS EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN 

       310        320        330        340        350        360 
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC DSYKKWKLTK 

       370        380        390        400        410        420 
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDDED GERGCTFLVG LIQKHRRRQR 

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

       490        500        510        520        530        540 
EYVLVPSTFE PHKNGDFCIR VFSEKKADYQ TVDDEIEANI EEIEANEEDI GDGFRRLFAQ 

       550        560        570        580        590        600 
LAGEDAEISA FELQTILRRV LAKREDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL 

       610        620        630        640        650        660 
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF ADDELIIDFD 

       670        680        690        700 
NFVRCLVRLE ILFKIFKQLD PENTGTIQLD LISWLSFSVL

« Hide

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References

« Hide 'large scale' references
[1]"Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit."
Deluca C.I., Davies P.L., Samis J.A., Elce J.S.
Biochim. Biophys. Acta 1216:81-93(1993) [PubMed: 8218419] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Prostate.
[3]"Ca(2+)-induced structural changes in rat m-calpain revealed by partial proteolysis."
Moldoveanu T., Hosfield C.M., Jia Z., Elce J.S., Davies P.L.
Biochim. Biophys. Acta 1545:245-254(2001) [PubMed: 11342050] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
[4]"Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain."
Hosfield C.M., Moldoveanu T., Davies P.L., Elce J.S., Jia Z.
J. Biol. Chem. 276:7404-7407(2001) [PubMed: 11102442] [Abstract]
Cited for: MUTAGENESIS OF LYS-230; LYS-234 AND GLU-504.
[5]"Active site residues in m-calpain: identification by site-directed mutagenesis."
Arthur J.S., Gauthier S., Elce J.S.
FEBS Lett. 368:397-400(1995) [PubMed: 7635186] [Abstract]
Cited for: MUTAGENESIS OF CYS-105; HIS-262; ASN-286 AND TRP-288.
[6]"Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation."
Hosfield C.M., Elce J.S., Davies P.L., Jia Z.
EMBO J. 18:6880-6889(1999) [PubMed: 10601010] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

L09120 mRNA. Translation: AAA16327.1.
BC065306 mRNA. Translation: AAH65306.1.
IPIIPI00388249.
PIRS38361.
RefSeqNP_058812.1.
UniGeneRn.6822

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1DF0X-ray2.60A1-700[»]
1MDWX-ray1.95A/B19-346[»]
1QXPX-ray2.80A/B1-700[»]
1U5IX-ray2.86A1-700[»]
3BOWX-ray2.40A1-700[»]
3DF0X-ray2.95A1-700[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:6139N.
IntActQ07009. 2 interactions.

Protein family/group databases

MEROPSC02.002.

Proteomic databases

PRIDEQ07009.

Genome annotation databases

EnsemblENSRNOG00000034015. Rattus norvegicus. [Contig view]
GeneID29154.
KEGGrno:29154.

Organism-specific databases

RGD2268. Capn2.

Phylogenomic databases

HOVERGENQ07009.

Enzyme and pathway databases

BRENDA3.4.22.53. 248.

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...

Other Resources

NextBio608171.

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Entry information

Entry nameCAN2_RAT
AccessionPrimary (citable) accession number: Q07009
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents