Calpain-1 catalytic subunit - Sus scrofa (Pig)

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P35750 (CAN1_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 113. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended 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

Organism

Sus scrofa (Pig) [Reference proteome]

Taxonomic identifier

9823 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Suina › Suidae › Sus

Protein attributes

Sequence length	714 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Domain	Repeat
Ligand	Calcium Metal-binding
Molecular function	Hydrolase Protease Thiol protease
PTM	Autocatalytic cleavage
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW receptor catabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent cysteine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 714

714

Calpain-1 catalytic subunit

PRO_0000207697

Regions

Domain

55 – 354

300

Calpain catalytic

Domain

585 – 618

EF-hand 1

Domain

615 – 650

EF-hand 2

Domain

680 – 714

EF-hand 3

Calcium binding

99 – 106

1 By similarity

Calcium binding

302 – 333

2 By similarity

Calcium binding

598 – 609

3 By similarity

Calcium binding

628 – 639

4 By similarity

Region

355 – 526

172

Domain III

Region

527 – 542

Linker

Region

543 – 713

171

Domain IV

Sites

Active site

115

By similarity

Active site

272

By similarity

Active site

296

By similarity

Site

15 – 16

Cleavage; for 78 kDa form By similarity

Site

27 – 28

Cleavage; for 75 kDa form By similarity

Experimental info

Sequence conflict

528

V → I in AAA65125. Ref.3

Sequence conflict

531

I → N in AAA65125. Ref.3

Sequence conflict

541

E → G in AAA65125. Ref.3

Sequence conflict

622

S → A in AAA65125. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P35750 [UniParc].

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

714

81,739

        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' referencesShow '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.
UniGene	Ssc.42541.
3D structure databases
ProteinModelPortal	P35750.
SMR	P35750. Positions 13-713.
ModBase	Search...
Protein family/group databases
MEROPS	C02.001.
Proteomic databases
PaxDb	P35750.
PRIDE	P35750.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSSSCT00000014210; ENSSSCP00000013824; ENSSSCG00000012999.
Phylogenomic databases
eggNOG	NOG327523.
GeneTree	ENSGT00700000104379.
HOGENOM	HOG000232035.
HOVERGEN	HBG012645.
OMA	DFLREFS.
OrthoDB	EOG4RR6GS.
Enzyme and pathway databases
BRENDA	3.4.22.52. 6170.
Gene expression databases
ArrayExpress	P35750.
Family and domain databases
Gene3D	1.10.238.10. 1 hit.
InterPro	IPR022684. Calpain_cysteine_protease. IPR022682. Calpain_domain_III. IPR022683. Calpain_III. IPR011992. EF-hand-like_dom. IPR018247. EF_Hand_1_Ca_BS. IPR002048. EF_hand_dom. IPR000169. Pept_cys_AS. IPR001300. Peptidase_C2_calpain_cat. [Graphical view]
Pfam	PF01067. Calpain_III. 1 hit. PF13405. EF_hand_4. 1 hit. PF00648. Peptidase_C2. 1 hit. [Graphical view]
PRINTS	PR00704. CALPAIN.
SMART	SM00720. calpain_III. 1 hit. SM00230. CysPc. 1 hit. SM00054. EFh. 3 hits. [Graphical view]
SUPFAM	SSF49758. Peptidase_C2. 1 hit.
PROSITE	PS50203. CALPAIN_CAT. 1 hit. PS00018. EF_HAND_1. 2 hits. PS50222. EF_HAND_2. 3 hits. PS00640. THIOL_PROTEASE_ASN. False negative. PS00139. THIOL_PROTEASE_CYS. 1 hit. PS00639. THIOL_PROTEASE_HIS. False negative. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P35750.
ChEMBL	CHEMBL4062.

Entry information

Entry name

CAN1_PIG

Accession

Primary (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 1, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents