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Q9GLG2 (CAN1_MACFA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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
Synonyms:CANPL1
ORF Names:QccE-12457
OrganismMacaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Taxonomic identifier9541 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMacaca

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 By similarity.

Catalytic activity

Broad endopeptidase specificity.

Cofactor

Binds 4 calcium ions By similarity.

Enzyme regulation

Activated by micromolar concentrations of calcium and inhibited by calpastatin By similarity.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 714713Calpain-1 catalytic subunit
PRO_0000207695

Regions

Domain55 – 354300Calpain catalytic
Domain541 – 57636EF-hand 1
Domain585 – 61834EF-hand 2
Domain615 – 65036EF-hand 3
Domain680 – 71435EF-hand 4
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

Sequences

Sequence LengthMass (Da)Tools
Q9GLG2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 834690C214DE7AD8

FASTA71481,850
        10         20         30         40         50         60 
MAEEIITPVY CTGVSAQVQK QRAKELGLGR HENAIKYLGQ DYEQLRARCL QSGTLFRDEA 

        70         80         90        100        110        120 
FPPVPQSLGF KDLGPNSSKT YGIKWKRPTE LLSNPQFIVD GATRTDICQG ALGDCWLLAA 

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

       190        200        210        220        230        240 
AEGNEFWSAL LEKAYAKVNG SYESLSGGST SEGFEDFTGG VTEWYELRKA PSDLYQIILK 

       250        260        270        280        290        300 
ALERGSLLGC SIDISSVLDM EAITFKKLVK GHAYSVTGAK QVNYRGQMVN LIRMRNPWGE 

       310        320        330        340        350        360 
VEWTGAWSDS SSEWNSVDPY EREQLRVKME DGEFWMSFRD FMREFTRLEI CNLTPDALKS 

       370        380        390        400        410        420 
RTIRKWNTTL YEGTWRRGST AGGCRNYPAT FWVNPQFKIR LDETDDPDDY GDRESGCSFV 

       430        440        450        460        470        480 
LALMQKHRRR ERRFGRDMET IGFAVYEVPP ELVGQPALHL KRDFFLANAS RARSEQFINL 

       490        500        510        520        530        540 
REVSTRFRLP PGEYVVVPST FEPNKEGDFV LRFFSEKSAG TAELDDQIQA NLPDEQVLSE 

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

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

       670        680        690        700        710 
TRYSEPDLAV DFDNFVCCLV RLETMFRFFK TLDTDLDGVV TFDLFKWLQL TMFA 

« Hide

References

« Hide 'large scale' 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.
[2]"DNA sequences of macaque genes expressed in brain or testis and its evolutionary implications."
International consortium for macaque cDNA sequencing and analysis
Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF284440 mRNA. Translation: AAG22770.1.
AB169651 mRNA. Translation: BAE01732.1.
RefSeqNP_001272270.1. NM_001285341.1.
XP_005577364.1. XM_005577307.1.
XP_005577365.1. XM_005577308.1.
UniGeneMfa.867.

3D structure databases

ProteinModelPortalQ9GLG2.
SMRQ9GLG2. Positions 13-713.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSC02.001.

Proteomic databases

PRIDEQ9GLG2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID101867512.
KEGGmcf:101867512.

Phylogenomic databases

HOVERGENHBG012645.
KOK01367.

Enzyme and pathway databases

BRENDA3.4.22.52. 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.
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. 4 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCAN1_MACFA
AccessionPrimary (citable) accession number: Q9GLG2
Secondary accession number(s): Q4R593
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2003
Last sequence update: March 1, 2001
Last modified: April 16, 2014
This is version 85 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