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Reviewed, UniProtKB/Swiss-Prot P00789 (CANX_CHICK)

Last modified June 16, 2009. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Calpain-1 catalytic subunit
    EC=3.4.22.52
Alternative name(s):
    Calpain-1 large subunit
    Calcium-activated neutral proteinase
      Short name=CANP
    Mu/M-type
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 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.

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Ontologies

Keywords
   Cellular componentCell membrane
Cytoplasm
Membrane
   DomainRepeat
   LigandCalcium
   Molecular functionHydrolase
Protease
Thiol protease
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

calcium-dependent cysteine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 705705Calpain-1 catalytic subunit
PRO_0000207701

Regions

Domain48 – 347300Calpain catalytic
Domain530 – 56536EF-hand 1
Domain606 – 64136EF-hand 2
Domain671 – 70535EF-hand 3
Calcium binding545 – 556121 Ref.3
Calcium binding589 – 600122 Ref.3
Calcium binding619 – 630123 Ref.3
Region348 – 517170Domain III
Region518 – 53316Linker
Region534 – 704171Domain IV

Sites

Active site1081 By similarity
Active site2651 By similarity
Active site2891 By similarity

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Sequences

Sequence LengthMass (Da)Tools
P00789-1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: ABCDDC56298E48AA

FASTA70580,352
        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

« Hide

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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: 6095110] [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: 3000828] [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: 3038855] [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: 7742367] [Abstract]
Cited for: CHARACTERIZATION.

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Cross-references

Sequence databases

X01415 mRNA. Translation: CAA25658.1.
IPIIPI00599609.
PIRCICHH. A00979.
RefSeqNP_990634.1.
UniGeneGga.1707

3D structure databases

HSSPHSSP built from PDB template 1MDW based on UniProtKB Q07009.
ModBaseSearch...

Protein family/group databases

MEROPSC02.003.

Genome annotation databases

EnsemblENSGALG00000010186. Gallus gallus. [Contig view]
GeneID396240.
KEGGgga:396240.

Phylogenomic databases

HOVERGENP00789.
OMAP00789. IRKWNTT.

Enzyme and pathway databases

BRENDA3.4.22.52. 4.

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.
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
PROSITEPS50203. 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]
ProtoNetSearch...

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Entry information

Entry nameCANX_CHICK
AccessionPrimary (citable) accession number: P00789
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: December 1, 2000
Last modified: June 16, 2009
This is version 94 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

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