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P00789 (CANX_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus

Protein attributes

Sequence length705 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

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

Sequences

Sequence LengthMass (Da)Tools
P00789 [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

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.
PIRCICHH. A00979.
RefSeqNP_990634.1. NM_205303.1.
UniGeneGga.1707.

3D structure databases

ProteinModelPortalP00789.
SMRP00789. Positions 5-703.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP00789.
ChEMBLCHEMBL3147.

Protein family/group databases

MEROPSC02.003.

Proteomic databases

PaxDbP00789.
PRIDEP00789.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSGALT00000016557; ENSGALP00000016538; ENSGALG00000010186.
GeneID396240.
KEGGgga:396240.

Organism-specific databases

CTD823.

Phylogenomic databases

eggNOGNOG327523.
GeneTreeENSGT00750000117643.
HOGENOMHOG000232035.
HOVERGENHBG012645.
InParanoidP00789.
KOK01367.
OMAHTIGFAV.
OrthoDBEOG7RV9FM.
PhylomeDBP00789.
TreeFamTF314748.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR000169. Pept_cys_AS.
IPR001300. Peptidase_C2_calpain_cat.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
PF13405. EF-hand_6. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSPR00704. CALPAIN.
SMARTSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMSSF49758. SSF49758. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20816292.

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: May 14, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries