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P06815

- CAN1_RABIT

UniProt

P06815 - CAN1_RABIT

Protein

Calpain-1 catalytic subunit

Gene

CAPN1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi186 – 197121Add
    BLAST
    Calcium bindingi216 – 227122Add
    BLAST

    GO - Molecular functioni

    1. calcium-dependent cysteine-type endopeptidase activity Source: UniProtKB
    2. calcium ion binding Source: InterPro

    GO - Biological processi

    1. proteolysis Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protease, Thiol protease

    Keywords - Ligandi

    Calcium, Metal-binding

    Enzyme and pathway databases

    BRENDAi3.4.22.52. 1749.

    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
    OrganismiOryctolagus cuniculus (Rabbit)
    Taxonomic identifieri9986 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
    ProteomesiUP000001811: Unplaced

    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: UniProtKB-SubCell
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini‹1 – 302›302Calpain-1 catalytic subunitPRO_0000207699Add
    BLAST

    Post-translational modificationi

    The N-terminus is blocked.
    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

    PRIDEiP06815.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Interactioni

    Subunit structurei

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

    Structurei

    3D structure databases

    ProteinModelPortaliP06815.
    SMRiP06815. Positions 1-301.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini173 – 20634EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini203 – 23836EF-hand 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini268 – 30235EF-hand 3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni‹1 – 114›114Domain IIIAdd
    BLAST
    Regioni115 – 13016LinkerAdd
    BLAST
    Regioni131 – 301171Domain IVAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    HOVERGENiHBG012645.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view]
    PfamiPF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view]
    SMARTiSM00720. calpain_III. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view]
    SUPFAMiSSF49758. SSF49758. 1 hit.
    PROSITEiPS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Fragment.

    P06815-1 [UniParc]FASTAAdd to Basket

    « Hide

    RESGCSFVLA LMQKHRRRER RFGRDMETIG FAVYEVPREL VGQPALHLKR    50
    DFFLANASRA RSEQFINLRE VSTRFRLPPG EYVVVPSTFE PNKEGDFVLR 100
    FFSEKRAGTQ ELDDQIQANL PDEQVLSAEE IDENFKALFR QLAGEDLEIS 150
    VRELQTILNR ITSKHKDLRT KGFSMESCRS MVNLMDRDGN GKLGLVEFNI 200
    LWNRIRNYLA IFRKFDLDKS GSMSAYEMRM AIESAGFKLN KKLYELIITR 250
    YSEPDLAVDF DNFVCCLVRL ETMFRFFKTL DTDLDGVVTF DLFKWLQLTM 300
    FA 302
    Length:302
    Mass (Da):35,275
    Last modified:January 1, 1988 - v1
    Checksum:i178BFEF4216C6EAB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Non-terminal residuei1 – 11

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13363 mRNA. Translation: AAA31456.1.
    PIRiA24815.
    UniGeneiOcu.1955.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M13363 mRNA. Translation: AAA31456.1 .
    PIRi A24815.
    UniGenei Ocu.1955.

    3D structure databases

    ProteinModelPortali P06815.
    SMRi P06815. Positions 1-301.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi C02.001.

    Proteomic databases

    PRIDEi P06815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG012645.

    Enzyme and pathway databases

    BRENDAi 3.4.22.52. 1749.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR022682. Calpain_domain_III.
    IPR022683. Calpain_III.
    IPR011992. EF-hand-dom_pair.
    IPR018247. EF_Hand_1_Ca_BS.
    IPR002048. EF_hand_dom.
    [Graphical view ]
    Pfami PF01067. Calpain_III. 1 hit.
    PF13405. EF-hand_6. 1 hit.
    [Graphical view ]
    SMARTi SM00720. calpain_III. 1 hit.
    SM00054. EFh. 3 hits.
    [Graphical view ]
    SUPFAMi SSF49758. SSF49758. 1 hit.
    PROSITEi PS00018. EF_HAND_1. 2 hits.
    PS50222. EF_HAND_2. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and sequence analyses of cDNA clones for the large subunits of two isozymes of rabbit calcium-dependent protease."
      Emori Y., Kawasaki H., Sugihara H., Imajoh S., Kawashima S., Suzuki K.
      J. Biol. Chem. 261:9465-9471(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Separation of peptides on the basis of the difference in positive charge: simultaneous isolation of C-terminal and blocked N-terminal peptides from tryptic digests."
      Kawasaki H., Imajoh S., Suzuki K.
      J. Biochem. 102:393-400(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: AMINO-ACID COMPOSITION.
    3. "E-F hand structure-domain of calcium-activated neutral protease (CANP) can bind Ca2+ ions."
      Minami Y., Emori Y., Kawasaki H., Suzuki K.
      J. Biochem. 101:889-895(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CALCIUM-BINDING DATA.

    Entry informationi

    Entry nameiCAN1_RABIT
    AccessioniPrimary (citable) accession number: P06815
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 114 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

    Complete proteome, Reference proteome

    Documents

    1. Peptidase families
      Classification of peptidase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3