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P97571 (CAN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
Synonyms:Cls1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length713 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

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

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 713712Calpain-1 catalytic subunit
PRO_0000207700

Regions

Domain55 – 354300Calpain catalytic
Domain540 – 57536EF-hand 1
Domain584 – 61734EF-hand 2
Domain614 – 64936EF-hand 3
Domain679 – 71335EF-hand 4
Calcium binding99 – 10681 Ref.3 Ref.5
Calcium binding302 – 333322 Ref.3 Ref.5
Calcium binding597 – 608123 By similarity
Calcium binding627 – 638124 By similarity
Region355 – 525171Domain III
Region526 – 54116Linker
Region542 – 712171Domain 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

Secondary structure

........................................................................................................... 713
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P97571 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 6E664600B0EFAEBB

FASTA71382,119
        10         20         30         40         50         60 
MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL QNGVLFQDDA 

        70         80         90        100        110        120 
FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA 

       130        140        150        160        170        180 
IASLTLNETI LHRVVPYGQS FQEGYAGIFH FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS 

       190        200        210        220        230        240 
AQGNEFWSAL LEKAYAKVNG SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK 

       250        260        270        280        290        300 
ALERGSLLGC SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE 

       310        320        330        340        350        360 
VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI CNLTPDALKS 

       370        380        390        400        410        420 
RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEEVDDADDY DSRESGCSFL 

       430        440        450        460        470        480 
LALMQKHRRR ERRFGRDMET IGFAVYQVPR ELAGQPVHLK RDFFLANASR AQSEHFINLR 

       490        500        510        520        530        540 
EVSNRIRLPP GEYIVVPSTF EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE 

       550        560        570        580        590        600 
EIDDNFKTLF SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG 

       610        620        630        640        650        660 
NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL NKKLHELIIT 

       670        680        690        700        710 
RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT FDLFKWLQLT MFA 

« Hide

References

« Hide 'large scale' references
[1]"Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human."
Sorimachi H., Amano S., Ishiura S., Suzuki K.
Biochim. Biophys. Acta 1309:37-41(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Prostate.
[3]"A Ca(2+) switch aligns the active site of calpain."
Moldoveanu T., Hosfield C.M., Lim D., Elce J.S., Jia Z., Davies P.L.
Cell 108:649-660(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 27-356, CALCIUM-BINDING REGIONS.
[4]"Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement."
Pal G.P., De Veyra T., Elce J.S., Jia Z.
Structure 11:1521-1526(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-647.
[5]"Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site."
Moldoveanu T., Campbell R.L., Cuerrier D., Davies P.L.
J. Mol. Biol. 343:1313-1326(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-356 IN COMPLEX WITH INHIBITORS, CALCIUM-BINDING REGIONS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U53858 mRNA. Translation: AAC53001.1.
BC061880 mRNA. Translation: AAH61880.1.
RefSeqNP_062025.1. NM_019152.2.
UniGeneRn.6037.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KXRX-ray2.07A/B27-356[»]
1QXPX-ray2.80A/B60-647[»]
1TL9X-ray1.80A27-356[»]
1TLOX-ray1.90A27-356[»]
2G8EX-ray2.25A27-356[»]
2G8JX-ray1.61A27-356[»]
2NQGX-ray2.04A27-356[»]
2NQIX-ray2.04A27-356[»]
2R9CX-ray1.80A27-356[»]
2R9FX-ray1.60A27-356[»]
ProteinModelPortalP97571.
SMRP97571. Positions 13-712.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000028431.

Chemistry

BindingDBP97571.
ChEMBLCHEMBL3747.

Protein family/group databases

MEROPSC02.001.

PTM databases

PhosphoSiteP97571.

Proteomic databases

PaxDbP97571.
PRIDEP97571.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID29153.
KEGGrno:29153.
UCSCRGD:2267. rat.

Organism-specific databases

CTD823.
RGD2267. Capn1.

Phylogenomic databases

eggNOGNOG327523.
HOGENOMHOG000232035.
HOVERGENHBG012645.
InParanoidP97571.
KOK01367.
PhylomeDBP97571.

Enzyme and pathway databases

BRENDA3.4.22.52. 5301.

Gene expression databases

GenevestigatorP97571.

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.
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

EvolutionaryTraceP97571.
NextBio608167.
PROP97571.

Entry information

Entry nameCAN1_RAT
AccessionPrimary (citable) accession number: P97571
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: April 16, 2014
This is version 131 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references