P00789 (CANX_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: Calpain-1 catalytic subunit EC=3.4.22.52 Alternative name(s): Calcium-activated neutral proteinase Short name=CANP Calpain-1 large subunit Mu/M-type
Organism	Gallus gallus (Chicken) [Reference proteome]
Taxonomic identifier	9031 [NCBI]
Taxonomic lineage	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	705 AA.
Sequence status	Complete.
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 micromolar concentrations of calcium and inhibited by calpastatin.
Subunit structure	Heterodimer of large (catalytic) and a small (regulatory) subunit.
Subcellular location	Cytoplasm By similarity. Cell membrane By similarity. Note: Translocates to the plasma membrane upon Ca2+ binding By similarity.
Tissue specificity	Ubiquitously expressed.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the peptidase C2 family. Contains 1 calpain catalytic domain. Contains 3 EF-hand domains.
Caution	This protein was previously thought to be M-calpain but has since been found to be an intermediate form between the M and Mu types.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Thiol protease
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
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: InterPro 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 – 705	705	Calpain-1 catalytic subunit		PRO_0000207701
Regions
	Domain	48 – 347	300	Calpain catalytic
	Domain	530 – 565	36	EF-hand 1
	Domain	606 – 641	36	EF-hand 2
	Domain	671 – 705	35	EF-hand 3
	Calcium binding	545 – 556	12	1 Ref.3
	Calcium binding	589 – 600	12	2 Ref.3
	Calcium binding	619 – 630	12	3 Ref.3
	Region	348 – 517	170	Domain III
	Region	518 – 533	16	Linker
	Region	534 – 704	171	Domain IV
Sites
	Active site	108	1	By similarity
	Active site	265	1	By similarity
	Active site	289	1	By similarity

Sequences

	Sequence		Length	Mass (Da)
	P00789 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: ABCDDC56298E48AA	FASTA	705	80,352
	10 20 30 40 50 60 MMPFGGIAAR LQRDRLRAEG VGEHNNAVKY LNQDYEALKQ ECIESGTLFR DPQFPAGPTA 70 80 90 100 110 120 LGFKELGPYS SKTRGVEWKR PSELVDDPQF IVGGATRTDI CQGALGDCWL LAAIGSLTLN 130 140 150 160 170 180 EELLHRVVPH GQSFQEDYAG IFHFQIWQFG EWVDVVVDDL LPTKDGELLF VHSAECTEFW 190 200 210 220 230 240 SALLEKAYAK LNGCYESLSG GSTTEGFEDF TGGVAEMYDL KRAPRNMGHI IRKALERGSL 250 260 270 280 290 300 LGCSIDITSA FDMEAVTFKK LVKGHAYSVT AFKDVNYRGQ QEQLIRIRNP WGQVEWTGAW 310 320 330 340 350 360 SDGSSEWDNI DPSDREELQL KMEDGEFWMS FRDFMREFSR LEICNLTPDA LTKDELSRWH 370 380 390 400 410 420 TQVFEGTWRR GSTAGGCRNN PATFWINPQF KIKLLEEDDD PGDDEVACSF LVALMQKHRR 430 440 450 460 470 480 RERRVGGDMH TIGFAVYEVP EEAQGSQNVH LKKDFFLRNQ SRARSETFIN LREVSNQIRL 490 500 510 520 530 540 PPGEYIVVPS TFEPHKEADF ILRVFTEKQS DTAELDEEIS ADLADEEEIT EDDIEDGFKN 550 560 570 580 590 600 MFQQLAGEDM EISVFELKTI LNRVIARHKD LKTDGFSLDS CRNMVNLMDK DGSARLGLVE 610 620 630 640 650 660 FQILWNKIRS WLTIFRQYDL DKSGTMSSYE MRMALESAGF KLNNKLHQVV VARYADAETG 670 680 690 700 VDFDNFVCCL VKLETMFRFF HSMDRDGTGT AVMNLAEWLL LTMCG

References

[1]	"Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?" Ohno S., Emori Y., Imajoh S., Kawasaki H., Kisaragi M., Suzuki K. Nature 312:566-570(1984) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Gene structure of calcium-dependent protease retains the ancestral organization of the calcium-binding protein gene." Emori Y., Ohno S., Tobita M., Suzuki K. FEBS Lett. 194:249-252(1986) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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] [Europe PMC] [Abstract] Cited for: CALCIUM-BINDING DATA.
[4]	"Identification of a third ubiquitous calpain species -- chicken muscle expresses four distinct calpains." Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., Suzuki K. Biochim. Biophys. Acta 1261:381-393(1995) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X01415 mRNA. Translation: CAA25658.1.
IPI	IPI00599609.
PIR	CICHH. A00979.
RefSeq	NP_990634.1. NM_205303.1.
UniGene	Gga.1707.
3D structure databases
ProteinModelPortal	P00789.
SMR	P00789. Positions 5-703.
ModBase	Search...
Protein family/group databases
MEROPS	C02.003.
Proteomic databases
PaxDb	P00789.
PRIDE	P00789.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSGALT00000016557; ENSGALP00000016538; ENSGALG00000010186.
GeneID	396240.
KEGG	gga:396240.
Organism-specific databases
CTD	823.
Phylogenomic databases
eggNOG	NOG327523.
GeneTree	ENSGT00700000104379.
HOGENOM	HOG000232035.
HOVERGEN	HBG012645.
InParanoid	P00789.
KO	K01367.
OMA	HTIGFAV.
OrthoDB	EOG4RR6GS.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR022684. Calpain_cysteine_protease. IPR022682. Calpain_domain_III. IPR022683. Calpain_III. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000169. Pept_cys_AS. IPR001300. Peptidase_C2_calpain_cat. [Graphical view]
Pfam	PF01067. Calpain_III. 1 hit. PF13405. EF_hand_4. 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. 1 hit. PS50222. EF_HAND_2. 2 hits. PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P00789.
ChEMBL	CHEMBL3147.
NextBio	20816292.

Entry information

Entry name

CANX_CHICK

Accession

Primary (citable) accession number: P00789

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program