Reviewed, UniProtKB/Swiss-Prot P06815 (CAN1_RABIT)

Names and origin

Protein names

Recommended name:
    Calpain-1 catalytic subunit
    EC=3.4.22.52
Alternative name(s):
    Calpain-1 large subunit
    Calcium-activated neutral proteinase 1
      Short name=CANP 1
    Calpain mu-type
    muCANP
    Micromolar-calpain

Gene names

Name:

CAPN1

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	302 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.
Catalytic activity	Broad endopeptidase specificity.
Cofactor	Binds 3 calcium ions By similarity.
Enzyme regulation	Activated by 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.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the peptidase C2 family. 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 – 302	›302	Calpain-1 catalytic subunit		PRO_0000207699
Regions
	Domain	173 – 206	34	EF-hand 1
	Domain	203 – 238	36	EF-hand 2
	Domain	268 – 302	35	EF-hand 3
	Calcium binding	186 – 197	12	1 Ref.3
	Calcium binding	216 – 227	12	2 Ref.3
	Region	‹1 – 114	›114	Domain III
	Region	115 – 130	16	Linker
	Region	131 – 301	171	Domain IV
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	P06815-1 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 178BFEF4216C6EAB	FASTA	302	35,275
	10 20 30 40 50 60 RESGCSFVLA LMQKHRRRER RFGRDMETIG FAVYEVPREL VGQPALHLKR DFFLANASRA 70 80 90 100 110 120 RSEQFINLRE VSTRFRLPPG EYVVVPSTFE PNKEGDFVLR FFSEKRAGTQ ELDDQIQANL 130 140 150 160 170 180 PDEQVLSAEE IDENFKALFR QLAGEDLEIS VRELQTILNR ITSKHKDLRT KGFSMESCRS 190 200 210 220 230 240 MVNLMDRDGN GKLGLVEFNI LWNRIRNYLA IFRKFDLDKS GSMSAYEMRM AIESAGFKLN 250 260 270 280 290 300 KKLYELIITR YSEPDLAVDF DNFVCCLVRL ETMFRFFKTL DTDLDGVVTF DLFKWLQLTM FA

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]	"Separation of peptides on the basis of the difference in positive charge: simultaneous isolation of C-terminal and blocked N-terminal peptides from tryptic digests." Kawasaki H., Imajoh S., Suzuki K. J. Biochem. 102:393-400(1987) [PubMed: 3667575] [Abstract] Cited for: AMINO-ACID COMPOSITION.
[3]	"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	M13363 mRNA. Translation: AAA31456.1.
PIR	A24815.
UniGene	Ocu.1955
3D structure databases
HSSP	HSSP built from PDB template 1KFX based on UniProtKB P17655.
ModBase	Search...
Protein family/group databases
MEROPS	C02.001.
Phylogenomic databases
HOVERGEN	P06815.
Enzyme and pathway databases
BRENDA	3.4.22.52. 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. [Graphical view]
ProDom	PD000012. EF-hand. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00720. calpain_III. 1 hit. SM00054. EFh. 3 hits. [Graphical view]
PROSITE	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

CAN1_RABIT

Accession

Primary (citable) accession number: P06815

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1988
Last sequence update:	January 1, 1988
Last modified:	June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)