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Q9GLG1 (CAN2_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 94. 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-2 catalytic subunit

EC=3.4.22.53
Alternative name(s):
Calcium-activated neutral proteinase 2
Short name=CANP 2
Calpain M-type
Calpain-2 large subunit
Millimolar-calpain
Short name=M-calpain
Gene names
Name:CAPN2
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

Protein attributes

Sequence length700 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. Proteolytically cleaves MYOC at 'Arg-226' By similarity.

Catalytic activity

Broad endopeptidase specificity.

Cofactor

Binds 7 calcium ions By similarity.

Enzyme regulation

Activated by 200-1000 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.

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
Propeptide2 – 1918Anchors to the small subunit Potential
PRO_0000026489
Chain20 – 700681Calpain-2 catalytic subunit
PRO_0000026490

Regions

Domain45 – 344300Calpain catalytic
Domain572 – 60534EF-hand 1
Domain602 – 63736EF-hand 2
Domain667 – 70034EF-hand 3
Calcium binding585 – 596121
Calcium binding615 – 626122
Region345 – 514170Domain III
Region515 – 52915Linker
Region530 – 700171Domain IV

Sites

Active site1051 By similarity
Active site2621 By similarity
Active site2861 By similarity
Metal binding891Calcium 3; via carbonyl oxygen By similarity
Metal binding911Calcium 3; via carbonyl oxygen By similarity
Metal binding961Calcium 3 By similarity
Metal binding1751Calcium 3 By similarity
Metal binding2291Calcium 2 By similarity
Metal binding2301Calcium 2 By similarity
Metal binding2921Calcium 4 By similarity
Metal binding2991Calcium 4 By similarity
Metal binding3231Calcium 4; via carbonyl oxygen By similarity
Metal binding5421Calcium 5; via carbonyl oxygen By similarity
Metal binding5451Calcium 5 By similarity
Metal binding5471Calcium 5; via carbonyl oxygen By similarity
Metal binding5521Calcium 5 By similarity
Metal binding5851Calcium 6 By similarity
Metal binding5871Calcium 6 By similarity
Metal binding5891Calcium 6; via carbonyl oxygen By similarity
Metal binding5911Calcium 6; via carbonyl oxygen By similarity
Metal binding5961Calcium 6 By similarity
Metal binding6151Calcium 7 By similarity
Metal binding6171Calcium 7 By similarity
Metal binding6191Calcium 7; via carbonyl oxygen By similarity
Metal binding6211Calcium 7; via carbonyl oxygen By similarity
Metal binding6261Calcium 7 By similarity
Metal binding6581Calcium 1 By similarity
Metal binding6611Calcium 1 By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9GLG1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: DCEE16214F05057C

FASTA70080,026
        10         20         30         40         50         60 
MAGIAAKLVK DREAAEGLGS HERAIKYLNQ DYEALRNECL EAGTLFQDPS FPAIPSALGF 

        70         80         90        100        110        120 
KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG ALGDCWLLAA IASLTLNEEI 

       130        140        150        160        170        180 
LARVVPLNQS FQENYAGIFH FQFWQYGEWV EVVVDDRLPT KDGELLFVHS AEGSEFWSAL 

       190        200        210        220        230        240 
LEKAYAKING CYEALSGGAT TEGFEDFTGG IAEWYELKKP PPNLFKIIQK ALQKGSLLGC 

       250        260        270        280        290        300 
SIDITSAADS EAITYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGE VEWTGRWNDN 

       310        320        330        340        350        360 
CPSWNTIDPE ERERLTRRHE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTS DTYKKWKLTK 

       370        380        390        400        410        420 
MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDEED GESGCTFLVG LIQKHRRRQR 

       430        440        450        460        470        480 
KMGEDMHTIG FGIYEVPEEL SGQTNIHLSK NFFLTNRARE RSDTFINLRE VLNRFKLPPG 

       490        500        510        520        530        540 
EYILVPSTFE PNKDGDFCIR VFSEKKADYQ AVDDEIEANL EEFDISEDDI DDGFRRLFAQ 

       550        560        570        580        590        600 
LAGEDAEISA FELQTILRRV LAKRQDIKSD GFSIETCKIM VDMLDSDGSG KLGLKEFYIL 

       610        620        630        640        650        660 
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKMPC QLHQVIVARF ADDQLIIDFD 

       670        680        690        700 
NFVRCLVRLE TLFKIFKQLD PENTGTIELD LISWLCFSVL 

« Hide

References

[1]"Different expression patterns for ubiquitous calpains and Capn3 splice variants in monkey ocular tissues."
Nakajima T., Fukiage C., Azuma M., Ma H., Shearer T.R.
Biochim. Biophys. Acta 1519:55-64(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Retina.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF284441 mRNA. Translation: AAG22771.1.
RefSeqNP_001274615.1. NM_001287686.1.
UniGeneMfa.5652.

3D structure databases

ProteinModelPortalQ9GLG1.
SMRQ9GLG1. Positions 2-700.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC02.002.

Proteomic databases

PRIDEQ9GLG1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID102122692.
KEGGmcf:102122692.

Organism-specific databases

CTD824.

Phylogenomic databases

HOVERGENHBG012645.
KOK03853.

Enzyme and pathway databases

BRENDA3.4.22.53. 3121.

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

Entry information

Entry nameCAN2_MACFA
AccessionPrimary (citable) accession number: Q9GLG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 94 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