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P35750 (CAN1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 123. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length714 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 3 EF-hand domains.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 714713Calpain-1 catalytic subunit
PRO_0000207697

Regions

Domain55 – 354300Calpain catalytic
Domain585 – 61834EF-hand 1
Domain615 – 65036EF-hand 2
Domain680 – 71435EF-hand 3
Calcium binding99 – 10681 By similarity
Calcium binding302 – 333322 By similarity
Calcium binding598 – 609123 By similarity
Calcium binding628 – 639124 By similarity
Region355 – 526172Domain III
Region527 – 54216Linker
Region543 – 713171Domain 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 conflict5281V → I in AAA65125. Ref.3
Sequence conflict5311I → N in AAA65125. Ref.3
Sequence conflict5411E → G in AAA65125. Ref.3
Sequence conflict6221S → A in AAA65125. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P35750 [UniParc].

Last modified January 11, 2001. Version 3.
Checksum: 0BB31DE4FC56363A

FASTA71481,739
        10         20         30         40         50         60 
MAEEVITPVY CTGVSAQVQK LRAKELGLGR HENAIKYLGQ DYEQLRAHCL QSGSLFRDEA 

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

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

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

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

       310        320        330        340        350        360 
VEWTGAWSDG SSEWNGVDPY QRDQLRVRME DGEFWMSFRD FLREFTRLEI CNLTPDALKS 

       370        380        390        400        410        420 
QRVRNWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LEETDDPEDD YGGRESGCSF 

       430        440        450        460        470        480 
VLALMQKHRR RERRFGRDME TIGFAVYEVP PELVGQPVHL KRDFFLANAS RARSEQFINL 

       490        500        510        520        530        540 
REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKKAG TQELDDQVQA ILPDEQVLSE 

       550        560        570        580        590        600 
EEIDENFKAL FRQLAGEDME ISVRELRTIL NRIISKHKDL RTKGFSLESC RSMVNLMDRD 

       610        620        630        640        650        660 
GNGKLGLVEF NILWNRIRNY LSIFRKFDLD KSGSMSAYEM RMAIESAGFK LNKKLFELII 

       670        680        690        700        710 
TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA 

« Hide

References

« Hide 'large scale' references
[1]"Rapid communication: nucleotide sequences of two isoforms of porcine micromolar calcium-activated neutral protease 1 cDNA."
Smith T.P.L., Simmen F.A., Zhao G., Vallet J.L.
J. Anim. Sci. 79:552-553(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Evaluation and characterization of a porcine small intestine cDNA library: analysis of 839 clones."
Winteroe A.K., Fredholm M., Davies W.
Mamm. Genome 7:509-517(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 326-415.
Tissue: Small intestine.
[3]"Cloning the partial cDNAs of mu-calpain and m-calpain from porcine skeletal muscle."
Sun W., Ji S.Q., Ebert P.J., Bidwell C.A., Hancock D.L.
Biochimie 75:931-936(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 528-623.
Tissue: Skeletal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF263610 mRNA. Translation: AAF73444.1.
F14611 mRNA. Translation: CAA23154.1.
U01180 mRNA. Translation: AAA65125.1.
RefSeqXP_005660758.1. XM_005660701.1.
XP_005660759.1. XM_005660702.1.
UniGeneSsc.42541.

3D structure databases

ProteinModelPortalP35750.
SMRP35750. Positions 13-713.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP35750.
ChEMBLCHEMBL4062.

Protein family/group databases

MEROPSC02.001.

Proteomic databases

PaxDbP35750.
PRIDEP35750.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
GeneID397027.
KEGGssc:397027.

Organism-specific databases

CTD823.

Phylogenomic databases

eggNOGNOG327523.
GeneTreeENSGT00750000117643.
HOGENOMHOG000232035.
HOVERGENHBG012645.
KOK01367.
OMAPQSLGYK.
OrthoDBEOG7RV9FM.
TreeFamTF314748.

Enzyme and pathway databases

BRENDA3.4.22.52. 6170.

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. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN1_PIG
AccessionPrimary (citable) accession number: P35750
Secondary accession number(s): Q29600, Q9N0M6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 11, 2001
Last modified: May 14, 2014
This is version 123 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