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CAN2_PIG
ID   CAN2_PIG                Reviewed;         324 AA.
AC   P43367;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Calpain-2 catalytic subunit;
DE            EC=3.4.22.53;
DE   AltName: Full=Calcium-activated neutral proteinase 2;
DE            Short=CANP 2;
DE   AltName: Full=Calpain M-type;
DE   AltName: Full=Calpain-2 large subunit;
DE   AltName: Full=Millimolar-calpain;
DE            Short=M-calpain;
DE   Flags: Fragment;
GN   Name=CAPN2;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-209.
RC   TISSUE=Skeletal muscle;
RX   PubMed=8312396; DOI=10.1016/0300-9084(93)90051-s;
RA   Sun W., Ji S.Q., Ebert P.J., Bidwell C.A., Hancock D.L.;
RT   "Cloning the partial cDNAs of mu-calpain and m-calpain from porcine
RT   skeletal muscle.";
RL   Biochimie 75:931-936(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 122-324.
RC   TISSUE=Pulmonary artery;
RX   PubMed=9728040; DOI=10.1152/ajplung.1998.275.3.l461;
RA   Zhang J.L., Patel J.M., Block E.R.;
RT   "Hypoxia-specific upregulation of calpain activity and gene expression in
RT   pulmonary artery endothelial cells.";
RL   Am. J. Physiol. 275:L461-L468(1998).
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 MYOC at
CC       'Arg-226'. Proteolytically cleaves CPEB3 following neuronal stimulation
CC       which abolishes CPEB3 translational repressor activity, leading to
CC       translation of CPEB3 target mRNAs. {ECO:0000250|UniProtKB:O08529,
CC       ECO:0000250|UniProtKB:P17655}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Broad endopeptidase specificity.; EC=3.4.22.53;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 7 Ca(2+) ions. {ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by 200-1000 micromolar concentrations of
CC       calcium and inhibited by calpastatin.
CC   -!- SUBUNIT: Forms a heterodimer with a small (regulatory) subunit
CC       (CAPNS1). Interacts with CPEB3; this leads to cleavage of CPEB3.
CC       {ECO:0000250|UniProtKB:O08529, ECO:0000250|UniProtKB:Q07009}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane
CC       {ECO:0000250}. Note=Translocates to the plasma membrane upon Ca(2+)
CC       binding. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR   EMBL; U01181; AAC48401.1; -; mRNA.
DR   EMBL; U71320; AAB17381.1; -; mRNA.
DR   AlphaFoldDB; P43367; -.
DR   SMR; P43367; -.
DR   STRING; 9823.ENSSSCP00000026311; -.
DR   BindingDB; P43367; -.
DR   ChEMBL; CHEMBL4143; -.
DR   MEROPS; C95.001; -.
DR   PeptideAtlas; P43367; -.
DR   PRIDE; P43367; -.
DR   eggNOG; KOG0045; Eukaryota.
DR   InParanoid; P43367; -.
DR   BRENDA; 3.4.22.53; 6170.
DR   Proteomes; UP000008227; Unplaced.
DR   Proteomes; UP000314985; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR   GO; GO:0051493; P:regulation of cytoskeleton organization; IEA:InterPro.
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; IPR029539; CAPN2.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   PANTHER; PTHR10183:SF268; PTHR10183:SF268; 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; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   2: Evidence at transcript level;
KW   Calcium; Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW   Protease; Reference proteome; Repeat; Thiol protease.
FT   CHAIN           <1..324
FT                   /note="Calpain-2 catalytic subunit"
FT                   /id="PRO_0000207703"
FT   DOMAIN          190..224
FT                   /note="EF-hand 1"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          226..261
FT                   /note="EF-hand 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   REGION          <1..138
FT                   /note="Domain III"
FT   REGION          139..153
FT                   /note="Linker"
FT   REGION          158..324
FT                   /note="Domain IV"
FT   BINDING         166
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         169
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         176
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="5"
FT                   /evidence="ECO:0000250"
FT   BINDING         209
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         211
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         213
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         215
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         220
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="6"
FT                   /evidence="ECO:0000250"
FT   BINDING         239
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         241
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         243
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         245
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         250
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   BINDING         282
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        202
FT                   /note="R -> K (in Ref. 2; AAB17381)"
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
SQ   SEQUENCE   324 AA;  37809 MW;  3929553239E123CF CRC64;
     YPNTFWMNPQ YLIKLEEEDE DQEDGESGCT FLVGLIQKHR RRQRKMGEDM HTIGFGIYEV
     PEELTGQTNI HLSKNFFLTH RARERSDTFI NLREVLNRFK LPPGEYILVP STFEPNKDGD
     FCIRVFSEKK ADYQVVDDEI EADLEENDAS EDDIDDGFRR LFAQLAGEDA EISAFELQTI
     LRRVLAKRQD IKSDGFSIET CRIMVDMLDS DGSAKLGLKE FYILWTKIQK YQKIYREIDV
     DRSGTMNSYE MRKALEEAGF KLPCQLHQVI VARFADDQLI IDFDNFVRCL VRLETLFRIS
     KQLDSENTGT IELDLISWLC FSVL
 
 
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