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Protein

Calpain-2 catalytic subunit

Gene

Capn2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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'. Proteolytically cleaves CPEB3 following neuronal stimulation which abolishes CPEB3 translational repressor activity, leading to translation of CPEB3 target mRNAs.By similarity

Catalytic activityi

Broad endopeptidase specificity.

Cofactori

Ca2+Note: Binds 7 Ca2+ ions.

Enzyme regulationi

Activated by 200-1000 micromolar concentrations of calcium and inhibited by calpastatin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi89Calcium 3; via carbonyl oxygen1
Metal bindingi91Calcium 3; via carbonyl oxygen1
Metal bindingi96Calcium 31
Active sitei1051
Metal bindingi175Calcium 31
Metal bindingi229Calcium 21
Metal bindingi230Calcium 21
Active sitei2621
Active sitei2861
Metal bindingi292Calcium 41
Metal bindingi299Calcium 41
Metal bindingi319Calcium 4; via carbonyl oxygen1
Metal bindingi323Calcium 4; via carbonyl oxygen1
Metal bindingi542Calcium 5; via carbonyl oxygen1
Metal bindingi545Calcium 51
Metal bindingi547Calcium 5; via carbonyl oxygen1
Metal bindingi552Calcium 51
Metal bindingi585Calcium 61
Metal bindingi587Calcium 61
Metal bindingi589Calcium 6; via carbonyl oxygen1
Metal bindingi591Calcium 6; via carbonyl oxygen1
Metal bindingi596Calcium 61
Metal bindingi615Calcium 71
Metal bindingi617Calcium 71
Metal bindingi619Calcium 7; via carbonyl oxygen1
Metal bindingi621Calcium 7; via carbonyl oxygen1
Metal bindingi626Calcium 71
Metal bindingi658Calcium 11
Metal bindingi661Calcium 11

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi585 – 5961Add BLAST12
Calcium bindingi615 – 6262Add BLAST12

GO - Molecular functioni

  • calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  • calcium ion binding Source: RGD
  • cytoskeletal protein binding Source: RGD
  • protein heterodimerization activity Source: RGD

GO - Biological processi

  • blastocyst development Source: Ensembl
  • cellular response to amino acid stimulus Source: UniProtKB
  • myoblast fusion Source: Ensembl
  • protein autoprocessing Source: RGD
  • proteolysis Source: UniProtKB
  • proteolysis involved in cellular protein catabolic process Source: Ensembl
  • regulation of cytoskeleton organization Source: InterPro
  • response to hypoxia Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease

Keywords - Ligandi

Calcium, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.22.53. 5301.
ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.

Protein family/group databases

MEROPSiC02.002.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Capn2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 13

Organism-specific databases

RGDi2268. Capn2.

Subcellular locationi

  • Cytoplasm By similarity
  • Cell membrane By similarity

  • Note: Translocates to the plasma membrane upon Ca2+ binding.By similarity

GO - Cellular componenti

  • chromatin Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: BHF-UCL
  • dendrite Source: UniProtKB
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • lysosome Source: Ensembl
  • membrane raft Source: Ensembl
  • nucleus Source: Ensembl
  • perinuclear endoplasmic reticulum Source: Ensembl
  • plasma membrane Source: BHF-UCL
  • pseudopodium Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi105C → S: Loss of activity. 1 Publication1
Mutagenesisi226K → S: 12% decrease in activity. 1
Mutagenesisi230K → E: 84% decrease in activity. 1 Publication1
Mutagenesisi230K → S: No effect. 1 Publication1
Mutagenesisi234K → E: 85% decrease in activity. 1 Publication1
Mutagenesisi234K → S: 20% decrease in activity. 1 Publication1
Mutagenesisi262H → A: Loss of activity. 1 Publication1
Mutagenesisi286N → A: Loss of activity. 1 Publication1
Mutagenesisi288W → Y: 95% decrease in activity. 1 Publication1
Mutagenesisi417R → A: Decreases catalytic activity. 1 Publication1
Mutagenesisi420R → A: Decreases catalytic activity. 1 Publication1
Mutagenesisi469R → A: Decreases catalytic activity. 1 Publication1
Mutagenesisi504E → S: 10% decrease in activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
PropeptideiPRO_00000264932 – 19Anchors to the small subunitSequence analysisAdd BLAST18
ChainiPRO_000002649420 – 700Calpain-2 catalytic subunitAdd BLAST681

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ07009.
PRIDEiQ07009.

PTM databases

iPTMnetiQ07009.
PhosphoSitePlusiQ07009.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSRNOG00000034015.
GenevisibleiQ07009. RN.

Interactioni

Subunit structurei

Forms a heterodimer with a small (regulatory) subunit (CAPNS1) (PubMed:19020622, PubMed:19020623). Interacts with CPEB3; this leads to cleavage of CPEB3 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CastP273215EBI-1040438,EBI-7441624
srp-6G5EFH42EBI-1040438,EBI-1549936From a different organism.

GO - Molecular functioni

  • cytoskeletal protein binding Source: RGD
  • protein heterodimerization activity Source: RGD

Protein-protein interaction databases

DIPiDIP-6139N.
IntActiQ07009. 4 interactors.
MINTiMINT-112911.
STRINGi10116.ENSRNOP00000046509.

Structurei

Secondary structure

1700
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 14Combined sources11
Turni15 – 19Combined sources5
Helixi21 – 23Combined sources3
Helixi27 – 29Combined sources3
Helixi32 – 42Combined sources11
Beta strandi49 – 51Combined sources3
Helixi55 – 58Combined sources4
Helixi68 – 70Combined sources3
Beta strandi74 – 76Combined sources3
Helixi78 – 81Combined sources4
Beta strandi82 – 84Combined sources3
Helixi94 – 96Combined sources3
Beta strandi101 – 103Combined sources3
Helixi105 – 114Combined sources10
Helixi118 – 124Combined sources7
Beta strandi131 – 134Combined sources4
Beta strandi136 – 145Combined sources10
Beta strandi148 – 156Combined sources9
Beta strandi158 – 161Combined sources4
Beta strandi164 – 167Combined sources4
Beta strandi171 – 175Combined sources5
Helixi177 – 188Combined sources12
Helixi192 – 195Combined sources4
Beta strandi196 – 198Combined sources3
Helixi205 – 207Combined sources3
Beta strandi210 – 216Combined sources7
Helixi224 – 233Combined sources10
Beta strandi237 – 241Combined sources5
Helixi247 – 249Combined sources3
Turni255 – 257Combined sources3
Beta strandi264 – 274Combined sources11
Beta strandi277 – 285Combined sources9
Beta strandi295 – 300Combined sources6
Helixi302 – 306Combined sources5
Helixi309 – 315Combined sources7
Beta strandi321 – 327Combined sources7
Helixi328 – 334Combined sources7
Beta strandi337 – 342Combined sources6
Beta strandi348 – 350Combined sources3
Beta strandi355 – 365Combined sources11
Turni367 – 370Combined sources4
Helixi378 – 381Combined sources4
Beta strandi387 – 391Combined sources5
Helixi393 – 395Combined sources3
Helixi399 – 401Combined sources3
Beta strandi404 – 415Combined sources12
Helixi417 – 422Combined sources6
Beta strandi429 – 435Combined sources7
Helixi438 – 440Combined sources3
Helixi450 – 455Combined sources6
Beta strandi459 – 461Combined sources3
Beta strandi465 – 477Combined sources13
Beta strandi479 – 490Combined sources12
Beta strandi495 – 507Combined sources13
Beta strandi508 – 511Combined sources4
Helixi527 – 529Combined sources3
Helixi532 – 542Combined sources11
Helixi543 – 545Combined sources3
Beta strandi546 – 549Combined sources4
Helixi550 – 561Combined sources12
Helixi574 – 584Combined sources11
Beta strandi590 – 592Combined sources3
Helixi594 – 614Combined sources21
Beta strandi620 – 623Combined sources4
Helixi624 – 633Combined sources10
Helixi640 – 650Combined sources11
Helixi653 – 655Combined sources3
Helixi659 – 676Combined sources18
Beta strandi677 – 679Combined sources3
Beta strandi685 – 690Combined sources6
Helixi691 – 700Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DF0X-ray2.60A1-700[»]
1MDWX-ray1.95A/B19-346[»]
1QXPX-ray2.80A/B1-700[»]
1U5IX-ray2.86A1-700[»]
3BOWX-ray2.40A1-700[»]
3DF0X-ray2.95A1-700[»]
ProteinModelPortaliQ07009.
SMRiQ07009.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ07009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini45 – 344Calpain catalyticPROSITE-ProRule annotationAdd BLAST300
Domaini572 – 605EF-hand 1PROSITE-ProRule annotationAdd BLAST34
Domaini602 – 637EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini667 – 700EF-hand 3PROSITE-ProRule annotationAdd BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni345 – 514Domain IIIAdd BLAST170
Regioni515 – 529LinkerAdd BLAST15
Regioni530 – 700Domain IVAdd BLAST171

Sequence similaritiesi

Belongs to the peptidase C2 family.Curated
Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
Contains 3 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiQ07009.
KOiK03853.
OMAiDTYKKWK.
OrthoDBiEOG091G049E.
PhylomeDBiQ07009.
TreeFamiTF314748.

Family and domain databases

CDDicd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029539. CAPN2.
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]
PANTHERiPTHR10183:SF268. PTHR10183:SF268. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF13833. EF-hand_8. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q07009-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGIAMKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS
60 70 80 90 100
FPALPSSLGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG
110 120 130 140 150
ALGDCWLLAA IASLTLNEEI LARVVPLDQS FQENYAGIFH FQFWQYGEWV
160 170 180 190 200
EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT
210 220 230 240 250
TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC SIDITSAADS
260 270 280 290 300
EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN
310 320 330 340 350
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC
360 370 380 390 400
DSYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDDED
410 420 430 440 450
GERGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK
460 470 480 490 500
NFFLTTRARE RSDTFINLRE VLNRFKLPPG EYVLVPSTFE PHKNGDFCIR
510 520 530 540 550
VFSEKKADYQ TVDDEIEANI EEIEANEEDI GDGFRRLFAQ LAGEDAEISA
560 570 580 590 600
FELQTILRRV LAKREDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL
610 620 630 640 650
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF
660 670 680 690 700
ADDELIIDFD NFVRCLVRLE ILFKIFKQLD PENTGTIQLD LISWLSFSVL
Length:700
Mass (Da):79,919
Last modified:January 23, 2007 - v3
Checksum:i296B0DC3BEEF5B90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09120 mRNA. Translation: AAA16327.1.
BC065306 mRNA. Translation: AAH65306.1.
PIRiS38361.
RefSeqiNP_058812.1. NM_017116.2.
UniGeneiRn.6822.

Genome annotation databases

EnsembliENSRNOT00000045326; ENSRNOP00000046509; ENSRNOG00000034015.
GeneIDi29154.
KEGGirno:29154.
UCSCiRGD:2268. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09120 mRNA. Translation: AAA16327.1.
BC065306 mRNA. Translation: AAH65306.1.
PIRiS38361.
RefSeqiNP_058812.1. NM_017116.2.
UniGeneiRn.6822.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DF0X-ray2.60A1-700[»]
1MDWX-ray1.95A/B19-346[»]
1QXPX-ray2.80A/B1-700[»]
1U5IX-ray2.86A1-700[»]
3BOWX-ray2.40A1-700[»]
3DF0X-ray2.95A1-700[»]
ProteinModelPortaliQ07009.
SMRiQ07009.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-6139N.
IntActiQ07009. 4 interactors.
MINTiMINT-112911.
STRINGi10116.ENSRNOP00000046509.

Protein family/group databases

MEROPSiC02.002.

PTM databases

iPTMnetiQ07009.
PhosphoSitePlusiQ07009.

Proteomic databases

PaxDbiQ07009.
PRIDEiQ07009.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000045326; ENSRNOP00000046509; ENSRNOG00000034015.
GeneIDi29154.
KEGGirno:29154.
UCSCiRGD:2268. rat.

Organism-specific databases

CTDi824.
RGDi2268. Capn2.

Phylogenomic databases

eggNOGiKOG0045. Eukaryota.
ENOG410XP0B. LUCA.
GeneTreeiENSGT00760000118971.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiQ07009.
KOiK03853.
OMAiDTYKKWK.
OrthoDBiEOG091G049E.
PhylomeDBiQ07009.
TreeFamiTF314748.

Enzyme and pathway databases

BRENDAi3.4.22.53. 5301.
ReactomeiR-RNO-1474228. Degradation of the extracellular matrix.

Miscellaneous databases

EvolutionaryTraceiQ07009.
PROiQ07009.

Gene expression databases

BgeeiENSRNOG00000034015.
GenevisibleiQ07009. RN.

Family and domain databases

CDDicd00214. Calpain_III. 1 hit.
cd00044. CysPc. 1 hit.
cd00051. EFh. 1 hit.
Gene3Di1.10.238.10. 1 hit.
InterProiIPR033883. C2_III.
IPR022684. Calpain_cysteine_protease.
IPR022682. Calpain_domain_III.
IPR022683. Calpain_III.
IPR029539. CAPN2.
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]
PANTHERiPTHR10183:SF268. PTHR10183:SF268. 1 hit.
PfamiPF01067. Calpain_III. 1 hit.
PF13833. EF-hand_8. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF49758. SSF49758. 1 hit.
PROSITEiPS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCAN2_RAT
AccessioniPrimary (citable) accession number: Q07009
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 165 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.