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Q07009

- CAN2_RAT

UniProt

Q07009 - CAN2_RAT

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Protein

Calpain-2 catalytic subunit

Gene
Capn2
Organism
Rattus norvegicus (Rat)
Status
Reviewed - 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' By similarity.

Catalytic activityi

Broad endopeptidase specificity.

Cofactori

Binds 7 calcium ions.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi89 – 891Calcium 3; via carbonyl oxygen
Metal bindingi91 – 911Calcium 3; via carbonyl oxygen
Metal bindingi96 – 961Calcium 3
Active sitei105 – 1051
Metal bindingi175 – 1751Calcium 3
Metal bindingi229 – 2291Calcium 2
Metal bindingi230 – 2301Calcium 2
Active sitei262 – 2621
Active sitei286 – 2861
Metal bindingi292 – 2921Calcium 4
Metal bindingi299 – 2991Calcium 4
Metal bindingi319 – 3191Calcium 4; via carbonyl oxygen
Metal bindingi323 – 3231Calcium 4; via carbonyl oxygen
Metal bindingi542 – 5421Calcium 5; via carbonyl oxygen
Metal bindingi545 – 5451Calcium 5
Metal bindingi547 – 5471Calcium 5; via carbonyl oxygen
Metal bindingi552 – 5521Calcium 5
Metal bindingi585 – 5851Calcium 6
Metal bindingi587 – 5871Calcium 6
Metal bindingi589 – 5891Calcium 6; via carbonyl oxygen
Metal bindingi591 – 5911Calcium 6; via carbonyl oxygen
Metal bindingi596 – 5961Calcium 6
Metal bindingi615 – 6151Calcium 7
Metal bindingi617 – 6171Calcium 7
Metal bindingi619 – 6191Calcium 7; via carbonyl oxygen
Metal bindingi621 – 6211Calcium 7; via carbonyl oxygen
Metal bindingi626 – 6261Calcium 7
Metal bindingi658 – 6581Calcium 1
Metal bindingi661 – 6611Calcium 1

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi585 – 5961212 PublicationsAdd
BLAST
Calcium bindingi615 – 6261222 PublicationsAdd
BLAST

GO - Molecular functioni

  1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
  2. calcium ion binding Source: RGD
  3. cytoskeletal protein binding Source: RGD
  4. protein binding Source: IntAct
  5. protein heterodimerization activity Source: RGD

GO - Biological processi

  1. blastocyst development Source: Ensembl
  2. cellular response to amino acid stimulus Source: UniProtKB
  3. myoblast fusion Source: Ensembl
  4. protein autoprocessing Source: RGD
  5. proteolysis Source: UniProtKB
  6. 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.

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
ProteomesiUP000002494: 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

  1. chromatin Source: Ensembl
  2. cytoplasm Source: UniProtKB
  3. cytosol Source: BHF-UCL
  4. dendrite Source: UniProtKB
  5. nucleus Source: Ensembl
  6. plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi105 – 1051C → S: Loss of activity. 1 Publication
Mutagenesisi226 – 2261K → S: 12% decrease in activity.
Mutagenesisi230 – 2301K → E: 84% decrease in activity. 1 Publication
Mutagenesisi230 – 2301K → S: No effect. 1 Publication
Mutagenesisi234 – 2341K → E: 85% decrease in activity. 1 Publication
Mutagenesisi234 – 2341K → S: 20% decrease in activity. 1 Publication
Mutagenesisi262 – 2621H → A: Loss of activity. 1 Publication
Mutagenesisi286 – 2861N → A: Loss of activity. 1 Publication
Mutagenesisi288 – 2881W → Y: 95% decrease in activity. 1 Publication
Mutagenesisi417 – 4171R → A: Decreases catalytic activity. 1 Publication
Mutagenesisi420 – 4201R → A: Decreases catalytic activity. 1 Publication
Mutagenesisi469 – 4691R → A: Decreases catalytic activity. 1 Publication
Mutagenesisi504 – 5041E → S: 10% decrease in activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Propeptidei2 – 1918Anchors to the small subunit Reviewed predictionPRO_0000026493Add
BLAST
Chaini20 – 700681Calpain-2 catalytic subunitPRO_0000026494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ07009.
PRIDEiQ07009.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

GenevestigatoriQ07009.

Interactioni

Subunit structurei

Forms a heterodimer with a small (regulatory) subunit (CAPNS1).2 Publications

Binary interactionsi

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

Protein-protein interaction databases

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

Structurei

Secondary structure

1
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1411
Turni15 – 195
Helixi21 – 233
Helixi27 – 293
Helixi32 – 4211
Beta strandi49 – 513
Helixi55 – 584
Helixi68 – 703
Beta strandi74 – 763
Helixi78 – 814
Beta strandi82 – 843
Helixi94 – 963
Beta strandi101 – 1033
Helixi105 – 11410
Helixi118 – 1247
Beta strandi131 – 1344
Beta strandi136 – 14510
Beta strandi148 – 1569
Beta strandi158 – 1614
Beta strandi164 – 1674
Beta strandi171 – 1755
Helixi177 – 18812
Helixi192 – 1954
Beta strandi196 – 1983
Helixi205 – 2073
Beta strandi210 – 2167
Helixi224 – 23310
Beta strandi237 – 2415
Helixi247 – 2493
Turni255 – 2573
Beta strandi264 – 27411
Beta strandi277 – 2859
Beta strandi295 – 3006
Helixi302 – 3065
Helixi309 – 3157
Beta strandi321 – 3277
Helixi328 – 3347
Beta strandi337 – 3426
Beta strandi348 – 3503
Beta strandi355 – 36511
Turni367 – 3704
Helixi378 – 3814
Beta strandi387 – 3915
Helixi393 – 3953
Helixi399 – 4013
Beta strandi404 – 41512
Helixi417 – 4226
Beta strandi429 – 4357
Helixi438 – 4403
Helixi450 – 4556
Beta strandi459 – 4613
Beta strandi465 – 47713
Beta strandi479 – 49012
Beta strandi495 – 50713
Beta strandi508 – 5114
Helixi527 – 5293
Helixi532 – 54211
Helixi543 – 5453
Beta strandi546 – 5494
Helixi550 – 56112
Helixi574 – 58411
Beta strandi590 – 5923
Helixi594 – 61421
Beta strandi620 – 6234
Helixi624 – 63310
Helixi640 – 65011
Helixi653 – 6553
Helixi659 – 67618
Beta strandi677 – 6793
Beta strandi685 – 6906
Helixi691 – 70010

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 2-700.

Miscellaneous databases

EvolutionaryTraceiQ07009.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 344300Calpain catalyticAdd
BLAST
Domaini572 – 60534EF-hand 1Add
BLAST
Domaini602 – 63736EF-hand 2Add
BLAST
Domaini667 – 70034EF-hand 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni345 – 514170Domain IIIAdd
BLAST
Regioni515 – 52915LinkerAdd
BLAST
Regioni530 – 700171Domain IVAdd
BLAST

Sequence similaritiesi

Belongs to the peptidase C2 family.
Contains 3 EF-hand domains.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG327523.
GeneTreeiENSGT00750000117643.
HOGENOMiHOG000232035.
HOVERGENiHBG012645.
InParanoidiQ07009.
KOiK03853.
OMAiDTYKKWK.
OrthoDBiEOG7RV9FM.
PhylomeDBiQ07009.
TreeFamiTF314748.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR022684. 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.
PF00648. Peptidase_C2. 1 hit.
[Graphical view]
PRINTSiPR00704. CALPAIN.
SMARTiSM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view]
SUPFAMiSSF49758. 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

MAGIAMKLAK DREAAEGLGS HERAIKYLNQ DYETLRNECL EAGALFQDPS    50
FPALPSSLGF KELGPYSSKT RGIEWKRPTE ICADPQFIIG GATRTDICQG 100
ALGDCWLLAA IASLTLNEEI LARVVPLDQS FQENYAGIFH FQFWQYGEWV 150
EVVVDDRLPT KDGELLFVHS AEGSEFWSAL LEKAYAKING CYEALSGGAT 200
TEGFEDFTGG IAEWYELRKP PPNLFKIIQK ALEKGSLLGC SIDITSAADS 250
EAVTYQKLVK GHAYSVTGAE EVESSGSLQK LIRIRNPWGQ VEWTGKWNDN 300
CPSWNTVDPE VRANLTERQE DGEFWMSFSD FLRHYSRLEI CNLTPDTLTC 350
DSYKKWKLTK MDGNWRRGST AGGCRNYPNT FWMNPQYLIK LEEEDEDDED 400
GERGCTFLVG LIQKHRRRQR KMGEDMHTIG FGIYEVPEEL TGQTNIHLSK 450
NFFLTTRARE RSDTFINLRE VLNRFKLPPG EYVLVPSTFE PHKNGDFCIR 500
VFSEKKADYQ TVDDEIEANI EEIEANEEDI GDGFRRLFAQ LAGEDAEISA 550
FELQTILRRV LAKREDIKSD GFSIETCKIM VDMLDEDGSG KLGLKEFYIL 600
WTKIQKYQKI YREIDVDRSG TMNSYEMRKA LEEAGFKLPC QLHQVIVARF 650
ADDELIIDFD NFVRCLVRLE ILFKIFKQLD PENTGTIQLD LISWLSFSVL 700
Length:700
Mass (Da):79,919
Last modified:January 23, 2007 - v3
Checksum:i296B0DC3BEEF5B90
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
L09120 mRNA. Translation: AAA16327.1 .
BC065306 mRNA. Translation: AAH65306.1 .
PIRi S38361.
RefSeqi NP_058812.1. NM_017116.2.
UniGenei Rn.6822.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DF0 X-ray 2.60 A 1-700 [» ]
1MDW X-ray 1.95 A/B 19-346 [» ]
1QXP X-ray 2.80 A/B 1-700 [» ]
1U5I X-ray 2.86 A 1-700 [» ]
3BOW X-ray 2.40 A 1-700 [» ]
3DF0 X-ray 2.95 A 1-700 [» ]
ProteinModelPortali Q07009.
SMRi Q07009. Positions 2-700.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-6139N.
IntActi Q07009. 4 interactions.
MINTi MINT-112911.
STRINGi 10116.ENSRNOP00000046509.

Protein family/group databases

MEROPSi C02.002.

Proteomic databases

PaxDbi Q07009.
PRIDEi Q07009.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000045326 ; ENSRNOP00000046509 ; ENSRNOG00000034015 .
GeneIDi 29154.
KEGGi rno:29154.
UCSCi RGD:2268. rat.

Organism-specific databases

CTDi 824.
RGDi 2268. Capn2.

Phylogenomic databases

eggNOGi NOG327523.
GeneTreei ENSGT00750000117643.
HOGENOMi HOG000232035.
HOVERGENi HBG012645.
InParanoidi Q07009.
KOi K03853.
OMAi DTYKKWK.
OrthoDBi EOG7RV9FM.
PhylomeDBi Q07009.
TreeFami TF314748.

Enzyme and pathway databases

BRENDAi 3.4.22.53. 5301.

Miscellaneous databases

EvolutionaryTracei Q07009.
NextBioi 608171.
PROi Q07009.

Gene expression databases

Genevestigatori Q07009.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
InterProi 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 ]
PANTHERi PTHR10183:SF268. PTHR10183:SF268. 1 hit.
Pfami PF01067. Calpain_III. 1 hit.
PF00648. Peptidase_C2. 1 hit.
[Graphical view ]
PRINTSi PR00704. CALPAIN.
SMARTi SM00720. calpain_III. 1 hit.
SM00230. CysPc. 1 hit.
SM00054. EFh. 2 hits.
[Graphical view ]
SUPFAMi SSF49758. SSF49758. 1 hit.
PROSITEi PS50203. CALPAIN_CAT. 1 hit.
PS00018. EF_HAND_1. 2 hits.
PS50222. EF_HAND_2. 3 hits.
PS00139. THIOL_PROTEASE_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and bacterial expression of cDNA for rat calpain II 80 kDa subunit."
    Deluca C.I., Davies P.L., Samis J.A., Elce J.S.
    Biochim. Biophys. Acta 1216:81-93(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Ca(2+)-induced structural changes in rat m-calpain revealed by partial proteolysis."
    Moldoveanu T., Hosfield C.M., Jia Z., Elce J.S., Davies P.L.
    Biochim. Biophys. Acta 1545:245-254(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
  4. "Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C(2)-like domain."
    Hosfield C.M., Moldoveanu T., Davies P.L., Elce J.S., Jia Z.
    J. Biol. Chem. 276:7404-7407(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-230; LYS-234 AND GLU-504.
  5. "Active site residues in m-calpain: identification by site-directed mutagenesis."
    Arthur J.S., Gauthier S., Elce J.S.
    FEBS Lett. 368:397-400(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-105; HIS-262; ASN-286 AND TRP-288.
  6. "Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation."
    Hosfield C.M., Elce J.S., Davies P.L., Jia Z.
    EMBO J. 18:6880-6889(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  7. "Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains."
    Moldoveanu T., Gehring K., Green D.R.
    Nature 456:404-408(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH CAPNS1 AND CALPASTATIN, CALCIUM-BINDING SITES, SUBUNIT, MUTAGENESIS OF ARG-417; ARG-420 AND ARG-469.
  8. "Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin."
    Hanna R.A., Campbell R.L., Davies P.L.
    Nature 456:409-412(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT SER-105 IN COMPLEX WITH CAPNS1 AND CALPASTATIN, CALCIUM-BINDING SITES, SUBUNIT.

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: September 3, 2014
This is version 145 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

External Data

Dasty 3

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