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P06815 (CAN1_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 113. 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
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length302 AA.
Sequence statusFragment.
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

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.

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 3 EF-hand domains.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – 302›302Calpain-1 catalytic subunit
PRO_0000207699

Regions

Domain173 – 20634EF-hand 1
Domain203 – 23836EF-hand 2
Domain268 – 30235EF-hand 3
Calcium binding186 – 197121 Ref.3
Calcium binding216 – 227122 Ref.3
Region‹1 – 114›114Domain III
Region115 – 13016Linker
Region131 – 301171Domain IV

Experimental info

Non-terminal residue11

Sequences

Sequence LengthMass (Da)Tools
P06815 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 178BFEF4216C6EAB

FASTA30235,275
        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 

« Hide

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING DATA.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13363 mRNA. Translation: AAA31456.1.
PIRA24815.
UniGeneOcu.1955.

3D structure databases

ProteinModelPortalP06815.
SMRP06815. Positions 1-301.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC02.001.

Proteomic databases

PRIDEP06815.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG012645.

Enzyme and pathway databases

BRENDA3.4.22.52. 1749.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR011992. EF-hand-dom_pair.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
[Graphical view]
PfamPF01067. Calpain_III. 1 hit.
PF13405. EF-hand_6. 1 hit.
[Graphical view]
SMARTSM00720. calpain_III. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
SUPFAMSSF49758. SSF49758. 1 hit.
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN1_RABIT
AccessionPrimary (citable) accession number: P06815
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 19, 2014
This is version 113 of the entry and version 1 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