Reviewed, UniProtKB/Swiss-Prot P06814 (CAN2_RABIT)

Names and origin

Protein names

Recommended 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

Organism

Oryctolagus cuniculus (Rabbit)

Taxonomic identifier

9986 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus

Protein attributes

Sequence length	422 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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 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. 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 component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium
Molecular function	Hydrolase Protease Thiol protease
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	‹1 – 422	›422	Calpain-2 catalytic subunit		PRO_0000207704
Regions
	Domain	‹1 – 66	›66	Calpain catalytic
	Domain	294 – 327	34	EF-hand 1
	Domain	324 – 359	36	EF-hand 2
	Domain	389 – 422	34	EF-hand 3
	Calcium binding	307 – 318	12	1 Ref.2
	Calcium binding	337 – 348	12	2 Ref.2
	Region	67 – 236	170	Domain III
	Region	237 – 251	15	Linker
	Region	252 – 422	171	Domain IV
Sites
	Active site	8	1	By similarity
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P06814-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: AE4FA3C48A333C41	FASTA	422	49,494
	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

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: 2424911] [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: 3038855] [Abstract] Cited for: CALCIUM-BINDING DATA.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M13797 mRNA. Translation: AAA31455.1.
PIR	B24815.
UniGene	Ocu.1954
3D structure databases
HSSP	HSSP built from PDB template 1KFX based on UniProtKB P17655.
SMR	P06814. Positions 1-422.
ModBase	Search...
Protein family/group databases
MEROPS	C02.002.
Phylogenomic databases
HOVERGEN	P06814.
Enzyme and pathway databases
BRENDA	3.4.22.53. 255.
Family and domain databases
InterPro	IPR011992. 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]
Gene3D	G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
Pfam	PF01067. Calpain_III. 1 hit. PF00648. Peptidase_C2. 1 hit. [Graphical view]
PRINTS	PR00704. CALPAIN.
SMART	SM00720. calpain_III. 1 hit. SM00054. EFh. 3 hits. [Graphical view]
PROSITE	PS50203. 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]
ProtoNet	Search...

Entry information

Entry name

CAN2_RABIT

Accession

Primary (citable) accession number: P06814

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)