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P06815

- CAN1_RABIT

UniProt

P06815 - CAN1_RABIT

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Protein

Calpain-1 catalytic subunit

Gene
CAPN1
Organism
Oryctolagus cuniculus (Rabbit)
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.

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 – 1971211 PublicationAdd
BLAST
Calcium bindingi216 – 2271221 PublicationAdd
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
Complete GO annotation...

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
Complete GO annotation...

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.

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini173 – 20634EF-hand 1Add
BLAST
Domaini203 – 23836EF-hand 2Add
BLAST
Domaini268 – 30235EF-hand 3Add
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.
Contains 3 EF-hand domains.

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

Non-terminal residue

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: February 19, 2014
This is version 113 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

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