CAN3_CHICK
ID CAN3_CHICK Reviewed; 810 AA.
AC Q92177;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Calpain-3;
DE EC=3.4.22.54;
DE AltName: Full=Calcium-activated neutral proteinase 3;
DE Short=CANP 3;
DE AltName: Full=Calpain L3;
DE AltName: Full=Calpain p94;
DE AltName: Full=Muscle-specific calcium-activated neutral protease 3;
GN Name=CAPN3;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lung;
RX PubMed=7742367; DOI=10.1016/0167-4781(95)00027-e;
RA Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., Suzuki K.;
RT "Identification of a third ubiquitous calpain species -- chicken muscle
RT expresses four distinct calpains.";
RL Biochim. Biophys. Acta 1261:381-393(1995).
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC Proteolytically cleaves CTBP1. Mediates, with UTP25, the proteasome-
CC independent degradation of p53/TP53. {ECO:0000250|UniProtKB:P20807}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase activity.; EC=3.4.22.54;
CC -!- ACTIVITY REGULATION: Activated by micromolar concentrations of calcium
CC and inhibited by calpastatin.
CC -!- SUBUNIT: Homodimer; via EF-hand domain 4. Interacts with TTN/titin.
CC Interacts with CMYA5; this interaction, which results in CMYA5
CC proteolysis, may protect CAPN3 from autolysis. Interacts with SIMC1.
CC Interacts with UTP25; the interaction is required for CAPN3
CC translocation to the nucleolus. {ECO:0000250|UniProtKB:P20807}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20807}.
CC Nucleus, nucleolus {ECO:0000250|UniProtKB:P20807}.
CC -!- TISSUE SPECIFICITY: Skeletal muscle. Low levels in spleen, intestine
CC and bone.
CC -!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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DR EMBL; D38028; BAA07230.1; -; mRNA.
DR PIR; S57196; S57196.
DR AlphaFoldDB; Q92177; -.
DR SMR; Q92177; -.
DR STRING; 9031.ENSGALP00000031999; -.
DR MEROPS; C02.004; -.
DR PaxDb; Q92177; -.
DR VEuPathDB; HostDB:geneid_423233; -.
DR eggNOG; KOG0045; Eukaryota.
DR InParanoid; Q92177; -.
DR PhylomeDB; Q92177; -.
DR BRENDA; 3.4.22.54; 1306.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030016; C:myofibril; ISS:UniProtKB.
DR GO; GO:0005730; C:nucleolus; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
DR GO; GO:0030018; C:Z disc; 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:0003824; F:catalytic activity; ISS:UniProtKB.
DR GO; GO:0055103; F:ligase regulator activity; ISS:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
DR GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
DR GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
DR GO; GO:0031432; F:titin binding; ISS:UniProtKB.
DR GO; GO:1990092; P:calcium-dependent self proteolysis; ISS:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
DR GO; GO:0061061; P:muscle structure development; ISS:UniProtKB.
DR GO; GO:0030239; P:myofibril assembly; ISS:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
DR GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0030163; P:protein catabolic process; ISS:UniProtKB.
DR GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
DR GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
DR GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
DR GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
DR GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR InterPro; IPR033883; C2_III.
DR InterPro; IPR022684; Calpain_cysteine_protease.
DR InterPro; IPR022682; Calpain_domain_III.
DR InterPro; IPR022683; Calpain_III.
DR InterPro; IPR036213; Calpain_III_sf.
DR InterPro; IPR029531; CAPN3.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR000169; Pept_cys_AS.
DR InterPro; IPR001300; Peptidase_C2_calpain_cat.
DR PANTHER; PTHR10183:SF329; PTHR10183:SF329; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF00036; EF-hand_1; 1.
DR Pfam; PF00648; Peptidase_C2; 1.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF49758; SSF49758; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 2.
DR PROSITE; PS50222; EF_HAND_2; 4.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 2: Evidence at transcript level;
KW Calcium; Cytoplasm; Hydrolase; Metal-binding; Nucleus; Protease;
KW Reference proteome; Repeat; Thiol protease.
FT CHAIN 1..810
FT /note="Calpain-3"
FT /id="PRO_0000207712"
FT DOMAIN 68..410
FT /note="Calpain catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT DOMAIN 638..672
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 681..714
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 711..746
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 776..810
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 9..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..579
FT /note="Domain III"
FT REGION 578..639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..638
FT /note="Linker"
FT REGION 639..809
FT /note="Domain IV"
FT COMPBIAS 578..596
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..639
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 327
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT ACT_SITE 351
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00239"
FT BINDING 651
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 654
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 656
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 661
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 694
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 696
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 698
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 700
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 705
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 724
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 726
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 728
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 730
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 735
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 789
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 791
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 793
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P20807"
FT BINDING 795
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000250|UniProtKB:P20807"
SQ SEQUENCE 810 AA; 93561 MW; E8DE99411C51041E CRC64;
MPSAINAAVA QQTAAGSVPS TTSTTTEGTG GGTGGIYSAI ISRNQPIIKV KEKTYEELHK
KCLEENILYE DPDFPPNETS LFYSQKVPIK FEWKRPREIC ENPRFIIGGA NRTDICQGEL
GDCWFLAAIA CLTLNKKLLC RVIPHDQSFI QNYAGIFHFQ FWRYGDWVDV IIDDCLPTYN
NQLVFTKSSQ RNEFWSALLE KAYAKLHGSY EALKGGNTTE AMEDFTGGVI EFYEIKDAPK
DIYKIMKHAI ARGSLMASSI DDNLGFHYGA APRSDIGELI ARMVKNLENA QMTYSTVDYQ
GTDERPAWTI MPMQYETRMS CGLVKGHAYS VTAVEETTYK GEKMRLVRLR NPWGQVEWNG
PWSDKSEEWN FIDEEEKIRL QHKIAEDGEF WISLEDFMRH FTKLEICNLT PDTLEADKLQ
TWTVSVNEGR WVRGCSAGGC RNYPDTFWTN PQYRLKLLEE DDDPEDEEVI CSFLVALMQK
NRRKERKLGA NLYTIGFAIY EVPKEMHGTK HHLQKDFFLY NASKARSKTY INMREISERF
RLPPSEYVII PSTYEPHQEG EFILRVFSEK RSLSEEVENM IEADRPSKKK KGKPIIFVSD
RANSNKELTT DEDAGKDGEK THVDEKKRSS AKAREKSEEE TQFRNIFRQI AGDDMEICRE
ELRNVLNNVV KKHKDLKTEG FELESSRSMI ALMDTDGSGK INFDEFRHLW DKIKSWQKIF
KHYDADHSGT INSYEMRNAV KDAGFRLNNQ LYDIITMRYA DKNMNIDFDS FICCFVRLDA
MFRAFHAFDK DGDGIIKLNV LEWLQLTMYA
