CAN1_RABIT
ID CAN1_RABIT Reviewed; 302 AA.
AC P06815;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Calpain-1 catalytic subunit {ECO:0000305};
DE EC=3.4.22.52 {ECO:0000250|UniProtKB:P07384};
DE AltName: Full=Calcium-activated neutral proteinase 1 {ECO:0000250|UniProtKB:P07384};
DE Short=CANP 1 {ECO:0000250|UniProtKB:P07384};
DE AltName: Full=Calpain mu-type {ECO:0000250|UniProtKB:P07384};
DE AltName: Full=Calpain-1 large subunit {ECO:0000250|UniProtKB:P07384};
DE AltName: Full=Micromolar-calpain {ECO:0000250|UniProtKB:P07384};
DE Short=muCANP {ECO:0000250|UniProtKB:P07384};
DE Flags: Fragment;
GN Name=CAPN1 {ECO:0000250|UniProtKB:P07384};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=2424911; DOI=10.1016/s0021-9258(18)67679-3;
RA Emori Y., Kawasaki H., Sugihara H., Imajoh S., Kawashima S., Suzuki K.;
RT "Isolation and sequence analyses of cDNA clones for the large subunits of
RT two isozymes of rabbit calcium-dependent protease.";
RL J. Biol. Chem. 261:9465-9471(1986).
RN [2]
RP AMINO-ACID COMPOSITION.
RX PubMed=3667575; DOI=10.1093/oxfordjournals.jbchem.a122066;
RA Kawasaki H., Imajoh S., Suzuki K.;
RT "Separation of peptides on the basis of the difference in positive charge:
RT simultaneous isolation of C-terminal and blocked N-terminal peptides from
RT tryptic digests.";
RL J. Biochem. 102:393-400(1987).
RN [3]
RP CALCIUM-BINDING DATA.
RX PubMed=3038855; DOI=10.1093/oxfordjournals.jbchem.a121956;
RA Minami Y., Emori Y., Kawasaki H., Suzuki K.;
RT "E-F hand structure-domain of calcium-activated neutral protease (CANP) can
RT bind Ca2+ ions.";
RL J. Biochem. 101:889-895(1987).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease which
CC catalyzes limited proteolysis of substrates involved in cytoskeletal
CC remodeling and signal transduction. Proteolytically cleaves CTBP1.
CC {ECO:0000250|UniProtKB:P07384}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
CC Evidence={ECO:0000250|UniProtKB:P07384};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P07384, ECO:0000269|PubMed:3038855};
CC Note=Binds 4 Ca(2+) ions. {ECO:0000250|UniProtKB:P07384,
CC ECO:0000269|PubMed:3038855};
CC -!- ACTIVITY REGULATION: Activated by micromolar concentrations of calcium
CC and inhibited by calpastatin. {ECO:0000250|UniProtKB:P07384}.
CC -!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit CAPNS1.
CC {ECO:0000250|UniProtKB:P97571}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07384}. Cell
CC membrane {ECO:0000250|UniProtKB:P07384}. Note=Translocates to the
CC plasma membrane upon Ca(2+) binding. {ECO:0000250|UniProtKB:P07384}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:2424911}.
CC -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:3667575}.
CC -!- PTM: Undergoes calcium-induced successive autoproteolytic cleavages
CC that generate a membrane-bound 78 kDa active form and an intracellular
CC 75 kDa active form. Calpastatin reduces with high efficiency the
CC transition from 78 kDa to 75 kDa calpain forms (By similarity).
CC {ECO:0000250|UniProtKB:P07384}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; M13363; AAA31456.1; -; mRNA.
DR PIR; A24815; A24815.
DR AlphaFoldDB; P06815; -.
DR SMR; P06815; -.
DR STRING; 9986.ENSOCUP00000002711; -.
DR InParanoid; P06815; -.
DR BRENDA; 3.4.22.52; 1749.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
DR CDD; cd00214; Calpain_III; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029643; CAPN1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR PANTHER; PTHR10183:SF284; PTHR10183:SF284; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00720; calpain_III; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Calcium; Cell membrane; Cytoplasm; Hydrolase;
KW Membrane; Metal-binding; Protease; Reference proteome; Repeat;
KW Thiol protease.
FT CHAIN <1..302
FT /note="Calpain-1 catalytic subunit"
FT /id="PRO_0000207699"
FT DOMAIN 173..206
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 203..238
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 268..302
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION <1..114
FT /note="Domain III"
FT REGION 115..130
FT /note="Linker"
FT REGION 131..301
FT /note="Domain IV"
FT BINDING 186
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 188
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 192
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 197
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 216
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 220
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 222
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT BINDING 227
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448,
FT ECO:0000269|PubMed:3038855"
FT NON_TER 1
SQ SEQUENCE 302 AA; 35275 MW; 178BFEF4216C6EAB CRC64;
RESGCSFVLA LMQKHRRRER RFGRDMETIG FAVYEVPREL VGQPALHLKR DFFLANASRA
RSEQFINLRE VSTRFRLPPG EYVVVPSTFE PNKEGDFVLR FFSEKRAGTQ ELDDQIQANL
PDEQVLSAEE IDENFKALFR QLAGEDLEIS VRELQTILNR ITSKHKDLRT KGFSMESCRS
MVNLMDRDGN GKLGLVEFNI LWNRIRNYLA IFRKFDLDKS GSMSAYEMRM AIESAGFKLN
KKLYELIITR YSEPDLAVDF DNFVCCLVRL ETMFRFFKTL DTDLDGVVTF DLFKWLQLTM
FA
