Calpain-2 catalytic subunit precursor - Rattus norvegicus (Rat)

Contribute

Send feedback

Read comments (?) or add your own

Q07009 (CAN2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 124. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.
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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium
Molecular function	Hydrolase Protease Thiol protease
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	protein autoprocessing Inferred from direct assay. Source: RGD proteolysis Inferred from direct assay. Source: RGD response to hypoxia Inferred from expression pattern. Source: RGD
Cellular component	cytoplasm Traceable author statement. Source: RGD insoluble fraction Inferred from direct assay. Source: RGD plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from direct assay. Source: RGD
Molecular function	calcium ion binding Inferred from direct assay. Source: RGD calcium-dependent cysteine-type endopeptidase activity Inferred from direct assay. Source: RGD cytoskeletal protein binding Inferred from direct assay. Source: RGD protein heterodimerization activity Inferred from physical interaction. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
srp-6	O01462	2	EBI-1040438,EBI-1549936	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Propeptide

2 – 19

Anchors to the small subunit Potential

PRO_0000026493

Chain

20 – 700

681

Calpain-2 catalytic subunit

PRO_0000026494

Regions

Domain

45 – 344

300

Calpain catalytic

Domain

572 – 605

EF-hand 1

Domain

602 – 637

EF-hand 2

Domain

667 – 700

EF-hand 3

Calcium binding

585 – 596

Calcium binding

615 – 626

Region

345 – 514

170

Domain III

Region

515 – 529

Linker

Region

530 – 700

171

Domain IV

Sites

Active site

105

Active site

262

Active site

286

Experimental info

Mutagenesis

105

C → S: Loss of activity. Ref.5

Mutagenesis

226

K → S: 12% decrease in activity.

Mutagenesis

230

K → E: 84% decrease in activity. Ref.4

Mutagenesis

230

K → S: No effect. Ref.4

Mutagenesis

234

K → E: 85% decrease in activity. Ref.4

Mutagenesis

234

K → S: 20% decrease in activity. Ref.4

Mutagenesis

262

H → A: Loss of activity. Ref.5

Mutagenesis

286

N → A: Loss of activity. Ref.5

Mutagenesis

288

W → Y: 95% decrease in activity. Ref.5

Mutagenesis

504

E → S: 10% decrease in activity. Ref.4

Secondary structure

700

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q07009 [UniParc].

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

FASTA

700

79,919

        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

References

	« Hide 'large scale' referencesShow '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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L09120 mRNA. Translation: AAA16327.1.
BC065306 mRNA. Translation: AAH65306.1.

IPI

IPI00388249.

PIR

S38361.

RefSeq

NP_058812.1. NM_017116.2.

UniGene

Rn.6822.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DF0	X-ray	2.60	A	1-700	[»]
1MDW	X-ray	1.95	A/B	19-346	[»]
1QXP	X-ray	2.80	A/B	1-700	[»]
1U5I	X-ray	2.86	A	1-700	[»]
3BOW	X-ray	2.40	A	1-700	[»]
3DF0	X-ray	2.95	A	1-700	[»]

ProteinModelPortal

Q07009.

SMR

Q07009. Positions 2-700.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6139N.

IntAct

Q07009. 2 interactions.

MINT

MINT-112911.

STRING

Q07009.

Protein family/group databases

MEROPS

C02.002.

Proteomic databases

PRIDE

Q07009.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSRNOT00000045326; ENSRNOP00000046509; ENSRNOG00000034015.

GeneID

29154.

KEGG

rno:29154.

UCSC

NM_017116. rat.

Organism-specific databases

CTD

824.

RGD

2268. Capn2.

Phylogenomic databases

eggNOG

roNOG08857.

HOVERGEN

HBG012645.

InParanoid

Q07009.

OrthoDB

EOG4RR6GS.

Enzyme and pathway databases

BRENDA

3.4.22.53. 5301.

Gene expression databases

Genevestigator

Q07009.

Family and domain databases

InterPro

IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-like_dom.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]

Gene3D

G3DSA:1.10.238.10. EF-Hand_type. 1 hit.

K03853.

Pfam

PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]

PRINTS

PR00704. CALPAIN.

SMART

SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]

SUPFAM

SSF49758. Peptidase_C2. 1 hit.

PROSITE

PS50203. 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]

ProtoNet

Search...

Other

NextBio

608171.

Entry information

Entry name

CAN2_RAT

Accession

Primary (citable) accession number: Q07009

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	November 16, 2011
This is version 124 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents