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P97571

- CAN1_RAT

UniProt

P97571 - CAN1_RAT

Protein

Calpain-1 catalytic subunit

Gene

Capn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      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.

    Catalytic activityi

    Broad endopeptidase specificity.

    Cofactori

    Binds 4 calcium ions.By similarity

    Enzyme regulationi

    Activated by micromolar concentrations of calcium and inhibited by calpastatin.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei15 – 162Cleavage; for 78 kDa formBy similarity
    Sitei27 – 282Cleavage; for 75 kDa formBy similarity
    Active sitei115 – 1151By similarity
    Active sitei272 – 2721By similarity
    Active sitei296 – 2961By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi99 – 10681
    Calcium bindingi302 – 333322Add
    BLAST
    Calcium bindingi597 – 608123PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi627 – 638124PROSITE-ProRule annotationAdd
    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: UniProtKB

    GO - Biological processi

    1. protein autoprocessing Source: RGD
    2. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.52. 5301.

    Protein family/group databases

    MEROPSiC02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:Capn1
    Synonyms:Cls1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2267. Capn1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: RefGenome
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 713712Calpain-1 catalytic subunitPRO_0000207700Add
    BLAST

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Autocatalytic cleavage

    Proteomic databases

    PaxDbiP97571.
    PRIDEiP97571.

    PTM databases

    PhosphoSiteiP97571.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    GenevestigatoriP97571.

    Interactioni

    Subunit structurei

    Forms a heterodimer with a small (regulatory) subunit (CAPNS1).1 Publication

    Protein-protein interaction databases

    STRINGi10116.ENSRNOP00000028431.

    Structurei

    Secondary structure

    1
    713
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi37 – 393
    Helixi42 – 5110
    Helixi65 – 684
    Beta strandi70 – 767
    Helixi78 – 825
    Beta strandi84 – 863
    Helixi88 – 914
    Beta strandi99 – 1024
    Helixi104 – 1063
    Beta strandi111 – 1133
    Helixi115 – 12410
    Helixi128 – 1347
    Beta strandi147 – 1559
    Beta strandi158 – 1669
    Beta strandi168 – 1714
    Beta strandi174 – 1774
    Beta strandi181 – 1833
    Helixi187 – 19913
    Beta strandi200 – 2023
    Helixi203 – 2053
    Beta strandi206 – 2083
    Helixi210 – 2167
    Beta strandi221 – 2266
    Helixi227 – 2293
    Helixi234 – 24411
    Beta strandi247 – 2515
    Beta strandi255 – 2584
    Beta strandi261 – 2633
    Beta strandi269 – 2713
    Beta strandi274 – 28411
    Beta strandi287 – 2959
    Helixi312 – 3165
    Helixi319 – 3257
    Beta strandi331 – 3377
    Helixi338 – 3447
    Beta strandi347 – 3526
    Beta strandi370 – 3756
    Turni377 – 3793
    Turni388 – 3903
    Helixi391 – 3933
    Beta strandi398 – 4014
    Beta strandi418 – 4258
    Beta strandi441 – 4477
    Helixi461 – 4644
    Beta strandi477 – 4804
    Beta strandi482 – 4876
    Beta strandi490 – 50314
    Beta strandi506 – 51611
    Beta strandi518 – 5203
    Beta strandi528 – 5303
    Beta strandi556 – 5594
    Turni565 – 5695
    Helixi586 – 59611
    Beta strandi606 – 6083
    Helixi609 – 62315
    Helixi624 – 6263
    Helixi636 – 64510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KXRX-ray2.07A/B27-356[»]
    1QXPX-ray2.80A/B60-647[»]
    1TL9X-ray1.80A27-356[»]
    1TLOX-ray1.90A27-356[»]
    2G8EX-ray2.25A27-356[»]
    2G8JX-ray1.61A27-356[»]
    2NQGX-ray2.04A27-356[»]
    2NQIX-ray2.04A27-356[»]
    2R9CX-ray1.80A27-356[»]
    2R9FX-ray1.60A27-356[»]
    ProteinModelPortaliP97571.
    SMRiP97571. Positions 13-712.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP97571.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini55 – 354300Calpain catalyticPROSITE-ProRule annotationAdd
    BLAST
    Domaini540 – 57536EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini584 – 61734EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini614 – 64936EF-hand 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini679 – 71335EF-hand 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni355 – 525171Domain IIIAdd
    BLAST
    Regioni526 – 54116LinkerAdd
    BLAST
    Regioni542 – 712171Domain IVAdd
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase C2 family.Curated
    Contains 1 calpain catalytic domain.PROSITE-ProRule annotation
    Contains 4 EF-hand domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG327523.
    HOGENOMiHOG000232035.
    HOVERGENiHBG012645.
    InParanoidiP97571.
    KOiK01367.
    PhylomeDBiP97571.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR022684. 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]
    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. 3 hits.
    [Graphical view]
    SUPFAMiSSF49758. SSF49758. 1 hit.
    PROSITEiPS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 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.

    P97571-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAEELITPVY CTGVSAQVQK QRDKELGLGR HENAIKYLGQ DYENLRARCL    50
    QNGVLFQDDA FPPVSHSLGF KELGPNSSKT YGIKWKRPTE LLSNPQFIVD 100
    GATRTDICQG ALGDCWLLAA IASLTLNETI LHRVVPYGQS FQEGYAGIFH 150
    FQLWQFGEWV DVVVDDLLPT KDGKLVFVHS AQGNEFWSAL LEKAYAKVNG 200
    SYEALSGGCT SEAFEDFTGG VTEWYDLQKA PSDLYQIILK ALERGSLLGC 250
    SINISDIRDL EAITFKNLVR GHAYSVTDAK QVTYQGQRVN LIRMRNPWGE 300
    VEWKGPWSDN SYEWNKVDPY EREQLRVKME DGEFWMSFRD FIREFTKLEI 350
    CNLTPDALKS RTLRNWNTTF YEGTWRRGST AGGCRNYPAT FWVNPQFKIR 400
    LEEVDDADDY DSRESGCSFL LALMQKHRRR ERRFGRDMET IGFAVYQVPR 450
    ELAGQPVHLK RDFFLANASR AQSEHFINLR EVSNRIRLPP GEYIVVPSTF 500
    EPNKEGDFLL RFFSEKKAGT QELDDQIQAN LPDEKVLSEE EIDDNFKTLF 550
    SKLAGDDMEI SVKELQTILN RIISKHKDLR TNGFSLESCR SMVNLMDRDG 600
    NGKLGLVEFN ILWNRIRNYL TIFRKFDLDK SGSMSAYEMR MAIEAAGFKL 650
    NKKLHELIIT RYSEPDLAVD FDNFVCCLVR LETMFRFFKI LDTDLDGVVT 700
    FDLFKWLQLT MFA 713
    Length:713
    Mass (Da):82,119
    Last modified:May 1, 1997 - v1
    Checksum:i6E664600B0EFAEBB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53858 mRNA. Translation: AAC53001.1.
    BC061880 mRNA. Translation: AAH61880.1.
    RefSeqiNP_062025.1. NM_019152.2.
    UniGeneiRn.6037.

    Genome annotation databases

    GeneIDi29153.
    KEGGirno:29153.
    UCSCiRGD:2267. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U53858 mRNA. Translation: AAC53001.1 .
    BC061880 mRNA. Translation: AAH61880.1 .
    RefSeqi NP_062025.1. NM_019152.2.
    UniGenei Rn.6037.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KXR X-ray 2.07 A/B 27-356 [» ]
    1QXP X-ray 2.80 A/B 60-647 [» ]
    1TL9 X-ray 1.80 A 27-356 [» ]
    1TLO X-ray 1.90 A 27-356 [» ]
    2G8E X-ray 2.25 A 27-356 [» ]
    2G8J X-ray 1.61 A 27-356 [» ]
    2NQG X-ray 2.04 A 27-356 [» ]
    2NQI X-ray 2.04 A 27-356 [» ]
    2R9C X-ray 1.80 A 27-356 [» ]
    2R9F X-ray 1.60 A 27-356 [» ]
    ProteinModelPortali P97571.
    SMRi P97571. Positions 13-712.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10116.ENSRNOP00000028431.

    Chemistry

    BindingDBi P97571.
    ChEMBLi CHEMBL3747.

    Protein family/group databases

    MEROPSi C02.001.

    PTM databases

    PhosphoSitei P97571.

    Proteomic databases

    PaxDbi P97571.
    PRIDEi P97571.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 29153.
    KEGGi rno:29153.
    UCSCi RGD:2267. rat.

    Organism-specific databases

    CTDi 823.
    RGDi 2267. Capn1.

    Phylogenomic databases

    eggNOGi NOG327523.
    HOGENOMi HOG000232035.
    HOVERGENi HBG012645.
    InParanoidi P97571.
    KOi K01367.
    PhylomeDBi P97571.

    Enzyme and pathway databases

    BRENDAi 3.4.22.52. 5301.

    Miscellaneous databases

    EvolutionaryTracei P97571.
    NextBioi 608167.
    PROi P97571.

    Gene expression databases

    Genevestigatori P97571.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR022684. 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 ]
    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. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49758. SSF49758. 1 hit.
    PROSITEi PS50203. CALPAIN_CAT. 1 hit.
    PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 4 hits.
    PS00139. THIOL_PROTEASE_CYS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary sequences of rat mu-calpain large and small subunits are, respectively, moderately and highly similar to those of human."
      Sorimachi H., Amano S., Ishiura S., Suzuki K.
      Biochim. Biophys. Acta 1309:37-41(1996) [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. "A Ca(2+) switch aligns the active site of calpain."
      Moldoveanu T., Hosfield C.M., Lim D., Elce J.S., Jia Z., Davies P.L.
      Cell 108:649-660(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.07 ANGSTROMS) OF 27-356, CALCIUM-BINDING REGIONS.
    4. "Crystal structure of a micro-like calpain reveals a partially activated conformation with low Ca2+ requirement."
      Pal G.P., De Veyra T., Elce J.S., Jia Z.
      Structure 11:1521-1526(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 60-647.
    5. "Crystal structures of calpain-E64 and -leupeptin inhibitor complexes reveal mobile loops gating the active site."
      Moldoveanu T., Campbell R.L., Cuerrier D., Davies P.L.
      J. Mol. Biol. 343:1313-1326(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-356 IN COMPLEX WITH INHIBITORS, CALCIUM-BINDING REGIONS.

    Entry informationi

    Entry nameiCAN1_RAT
    AccessioniPrimary (citable) accession number: P97571
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 18, 2001
    Last sequence update: May 1, 1997
    Last modified: October 1, 2014
    This is version 134 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, 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