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Reviewed, UniProtKB/Swiss-Prot P06815 (CAN1_RABIT)

Last modified June 16, 2009. Version 88. 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

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 1
      Short name=CANP 1
    Calpain mu-type
    muCANP
    Micromolar-calpain
Gene names
Name: CAPN1
OrganismOryctolagus cuniculus (Rabbit)
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length302 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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 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.

Sequence similarities

Belongs to the peptidase C2 family.

Contains 3 EF-hand domains.

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...

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
P06815-1 [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: 2424911] [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: 3667575] [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: 3038855] [Abstract]
Cited for: CALCIUM-BINDING DATA.

Cross-references

Sequence databases

M13363 mRNA. Translation: AAA31456.1.
PIRA24815.
UniGeneOcu.1955

3D structure databases

HSSPHSSP built from PDB template 1KFX based on UniProtKB P17655.
ModBaseSearch...

Protein family/group databases

MEROPSC02.001.

Phylogenomic databases

HOVERGENP06815.

Enzyme and pathway databases

BRENDA3.4.22.52. 255.

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.
[Graphical view]
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00720. calpain_III. 1 hit.
SM00054. EFh. 3 hits.
[Graphical view]
PROSITEPS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00640. THIOL_PROTEASE_ASN. Partial match.
PS00139. THIOL_PROTEASE_CYS. Partial match.
PS00639. THIOL_PROTEASE_HIS. Partial match.
[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: June 16, 2009
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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