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Q27970 (CAN1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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 1
Short name=CANP 1
Calpain mu-type
Calpain-1 large subunit
Micromolar-calpain
Short name=muCANP
Gene names
Name:CAPN1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length716 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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 4 calcium ions By similarity.

Enzyme regulation

Activated by micromolar concentrations of calcium and inhibited by calpastatin.

Subunit structure

Heterodimer of a 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.

Post-translational modification

Undergoes calcium-induced successive autoproteolytic cleavages that generate a membrane-bound 78 kDa active form and an intracellular 75 kDa active form. Calpastatin reduces with high efficiency the transition from 78 kDa to 75 kDa calpain forms By similarity.

Sequence similarities

Belongs to the peptidase C2 family.

Contains 1 calpain catalytic domain.

Contains 4 EF-hand domains.

Sequence caution

The sequence AAA18454.1 differs from that shown. Reason: Frameshift at positions 582 and 617.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 716715Calpain-1 catalytic subunit
PRO_0000207693

Regions

Domain55 – 354300Calpain catalytic
Domain543 – 57836EF-hand 1
Domain587 – 62034EF-hand 2
Domain617 – 65236EF-hand 3
Domain682 – 71635EF-hand 4
Calcium binding101 – 10881 By similarity
Calcium binding304 – 335322 By similarity
Calcium binding600 – 611123 By similarity
Calcium binding630 – 641124 By similarity
Region355 – 528174Domain III
Region529 – 54416Linker
Region545 – 715171Domain IV

Sites

Active site1151 By similarity
Active site2721 By similarity
Active site2961 By similarity
Site15 – 162Cleavage; for 78 kDa form By similarity
Site27 – 282Cleavage; for 75 kDa form By similarity

Experimental info

Sequence conflict211Q → T AA sequence Ref.5
Sequence conflict3161G → A in AAF64504. Ref.1
Sequence conflict3811A → V in AAF64504. Ref.1
Sequence conflict5301V → I in AAA18454. Ref.4
Sequence conflict6241S → A in AAA18454. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Q27970 [UniParc].

Last modified December 12, 2006. Version 3.
Checksum: A7F55C197BD5DF23

FASTA71682,207
        10         20         30         40         50         60 
MAEEFITPVY CTGVSAQVQK QRAKELGLGR HENAIKYLGQ DYEQLRVHCL QRGALFRDEA 

        70         80         90        100        110        120 
FPPVPQSLGF KELGPNSSKT YGIKWKRPTE LFSNPQFIVD GATRTDICQG ALGDCWLLAA 

       130        140        150        160        170        180 
IASLTLNDTL LHRVVPHGQS FQDGYAGIFH FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS 

       190        200        210        220        230        240 
AQGNEFWSAL LEKAYAKVNG SYEALSGGST SEGFEDFTGG VTEWYELRKA PSDLYNIILK 

       250        260        270        280        290        300 
ALERGSLLGC SIDISSILDM EAVTFKKLVK GHAYSVTGAK QVNYQGQMVN LIRMRNPWGE 

       310        320        330        340        350        360 
VEWTGAWSDG SSEWNGVDPY MREQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS 

       370        380        390        400        410        420 
QRFRNWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEETDDPDPD DYGGRESGCS 

       430        440        450        460        470        480 
FLLALMQKHR RRERRFGRDM ETIGFAVYEV PPELMGQPAV HLKRDFFLSN ASRARSEQFI 

       490        500        510        520        530        540 
NLREVSTRFR LPPGEYVVVP STFEPNKEGD FVLRFFSEKS AGTQELDDQV QANLPDEQVL 

       550        560        570        580        590        600 
SEEEIDENFK SLFRQLAGED MEISVKELRT ILNRIISKHK DLRTTGFSLE SCRSMVNLMD 

       610        620        630        640        650        660 
RDGNGKLGLV EFNILWNRIR NYLSIFRKFD LDKSGSMSAY EMRMAIEFAG FKLNKKLYEL 

       670        680        690        700        710 
IITRYSEPDL AVDFDNFVCC LVRLETMFRF FKTLDTDLDG VVTFDLFKWL QLTMFA 

« Hide

References

« Hide 'large scale' references
[1]"Bovine CAPN1 maps to a region of BTA29 containing a quantitative trait locus for meat tenderness."
Smith T.P.L., Casas E., Rexroad C.E. III, Kappes S.M., Keele J.W.
J. Anim. Sci. 78:2589-2594(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Bovine CAPN1 maps to a region containing a QTL for meat tenderness."
Smith T.P.L., Casas E., Rexroad C.E., Kappes S.M., Keele J.W.
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]NIH - Mammalian Gene Collection (MGC) project
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.
[4]Sun W., Bidwell C.A., Ji S., Hancock D.L.
Submitted (APR-1994) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 530-625.
Tissue: Skeletal muscle.
[5]"Two-stage autolysis of the catalytic subunit initiates activation of calpain I."
Zimmerman U.J., Schlaepfer W.W.
Biochim. Biophys. Acta 1078:192-198(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 16-41.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF248054, AF252504 Genomic DNA. Translation: AAF64504.2.
AF221129 mRNA. Translation: AAF32364.1.
BC123635 mRNA. Translation: AAI23636.1.
U07849 mRNA. Translation: AAA18454.1. Frameshift.
PIRS16181.
RefSeqNP_776684.1. NM_174259.2.
UniGeneBt.252.

3D structure databases

ProteinModelPortalQ27970.
SMRQ27970. Positions 13-715.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ27970. 1 interaction.

Protein family/group databases

MEROPSC02.001.

Proteomic databases

PaxDbQ27970.
PRIDEQ27970.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000011678; ENSBTAP00000011678; ENSBTAG00000010230.
GeneID281661.
KEGGbta:281661.

Organism-specific databases

CTD823.

Phylogenomic databases

eggNOGNOG327523.
GeneTreeENSGT00750000117643.
HOGENOMHOG000232035.
HOVERGENHBG012645.
InParanoidQ27970.
KOK01367.
OMAPQSLGYK.
OrthoDBEOG7RV9FM.
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. 3 hits.
[Graphical view]
SUPFAMSSF49758. SSF49758. 1 hit.
PROSITEPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20805592.

Entry information

Entry nameCAN1_BOVIN
AccessionPrimary (citable) accession number: Q27970
Secondary accession number(s): Q9N0U3, Q9N0V6, Q9N185
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 12, 2006
Last modified: April 16, 2014
This is version 115 of the entry and version 3 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