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Q07009

- CAN2_RAT

UniProt

Q07009 - CAN2_RAT

Protein

Calpain-2 catalytic subunit

Gene

Capn2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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.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 – 596121Add
    BLAST
    Calcium bindingi615 – 626122Add
    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

    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

    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 – 11RemovedBy similarity
    Propeptidei2 – 1918Anchors to the small subunitSequence AnalysisPRO_0000026493Add
    BLAST
    Chaini20 – 700681Calpain-2 catalytic subunitPRO_0000026494Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ07009.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini45 – 344300Calpain catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini572 – 60534EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini602 – 63736EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini667 – 70034EF-hand 3PROSITE-ProRule annotationAdd
    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.Curated
    Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
    Contains 3 EF-hand domains.PROSITE-ProRule annotation

    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

    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: October 1, 2014
    This is version 146 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