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Calpain-3 (EC 3.4.22.54) (Calcium-activated neutral proteinase 3) (CANP 3) (Calpain L3) (Calpain p94) (Cn94) (Muscle-specific calcium-activated neutral protease 3)

 CAN3_MACFA              Reviewed;         815 AA.
Q9GLG7;
19-JUL-2003, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
30-AUG-2017, entry version 103.
RecName: Full=Calpain-3;
EC=3.4.22.54;
AltName: Full=Calcium-activated neutral proteinase 3;
Short=CANP 3;
AltName: Full=Calpain L3;
AltName: Full=Calpain p94;
AltName: Full=Cn94;
AltName: Full=Muscle-specific calcium-activated neutral protease 3;
Name=CAPN3;
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
NCBI_TaxID=9541;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Corneal epithelium;
PubMed=11406271; DOI=10.1016/S0167-4781(01)00212-3;
Nakajima T., Fukiage C., Azuma M., Ma H., Shearer T.R.;
"Different expression patterns for ubiquitous calpains and Capn3
splice variants in monkey ocular tissues.";
Biochim. Biophys. Acta 1519:55-64(2001).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
-!- CATALYTIC ACTIVITY: Broad endopeptidase activity.
-!- ENZYME REGULATION: Activated by micromolar concentrations of
calcium and inhibited by calpastatin. {ECO:0000250}.
-!- SUBUNIT: Homodimer; via EF-hand domain 4. Interacts with
TTN/titin. Interacts with CMYA5; this interaction, which results
in CMYA5 proteolysis, may protect CAPN3 from autolysis.
{ECO:0000250|UniProtKB:P20807}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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EMBL; AF277376; AAG27599.1; -; mRNA.
RefSeq; NP_001274630.1; NM_001287701.1.
UniGene; Mfa.5713; -.
ProteinModelPortal; Q9GLG7; -.
SMR; Q9GLG7; -.
MEROPS; C02.004; -.
PRIDE; Q9GLG7; -.
GeneID; 102115794; -.
KEGG; mcf:102115794; -.
CTD; 825; -.
HOVERGEN; HBG012645; -.
KO; K08573; -.
BRENDA; 3.4.22.54; 1793.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030016; C:myofibril; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0030315; C:T-tubule; ISS:UniProtKB.
GO; GO:0030018; C:Z disc; ISS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; ISS:UniProtKB.
GO; GO:0003824; F:catalytic activity; ISS:UniProtKB.
GO; GO:0055103; F:ligase regulator activity; ISS:UniProtKB.
GO; GO:0008233; F:peptidase activity; ISS:UniProtKB.
GO; GO:0032947; F:protein complex scaffold activity; ISS:UniProtKB.
GO; GO:0031402; F:sodium ion binding; ISS:UniProtKB.
GO; GO:0008307; F:structural constituent of muscle; ISS:UniProtKB.
GO; GO:0031432; F:titin binding; ISS:UniProtKB.
GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
GO; GO:0071472; P:cellular response to salt stress; ISS:UniProtKB.
GO; GO:0061061; P:muscle structure development; ISS:UniProtKB.
GO; GO:0030239; P:myofibril assembly; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
GO; GO:0033234; P:negative regulation of protein sumoylation; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; ISS:UniProtKB.
GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; ISS:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006461; P:protein complex assembly; ISS:UniProtKB.
GO; GO:0072657; P:protein localization to membrane; ISS:UniProtKB.
GO; GO:0006508; P:proteolysis; ISS:UniProtKB.
GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
GO; GO:0051592; P:response to calcium ion; ISS:UniProtKB.
GO; GO:0014850; P:response to muscle activity; ISS:UniProtKB.
GO; GO:0045214; P:sarcomere organization; ISS:UniProtKB.
GO; GO:0097264; P:self proteolysis; ISS:UniProtKB.
CDD; cd00214; Calpain_III; 1.
CDD; cd00044; CysPc; 1.
InterPro; IPR033883; C2_III.
InterPro; IPR022684; Calpain_cysteine_protease.
InterPro; IPR022682; Calpain_domain_III.
InterPro; IPR022683; Calpain_III.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR000169; Pept_cys_AS.
InterPro; IPR001300; Peptidase_C2_calpain_cat.
Pfam; PF01067; Calpain_III; 1.
Pfam; PF13202; EF-hand_5; 1.
Pfam; PF13833; EF-hand_8; 1.
Pfam; PF00648; Peptidase_C2; 1.
PRINTS; PR00704; CALPAIN.
SMART; SM00720; calpain_III; 1.
SMART; SM00230; CysPc; 1.
SMART; SM00054; EFh; 3.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF49758; SSF49758; 1.
PROSITE; PS50203; CALPAIN_CAT; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS50222; EF_HAND_2; 4.
PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
2: Evidence at transcript level;
Calcium; Cytoplasm; Hydrolase; Metal-binding; Protease; Repeat;
Thiol protease.
CHAIN 1 815 Calpain-3.
/FTId=PRO_0000207707.
DOMAIN 74 417 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 643 677 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 686 719 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 716 751 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 781 815 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 656 666 1. {ECO:0000250|UniProtKB:P20807}.
CA_BIND 699 710 2. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 729 735 3. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 794 800 4. {ECO:0000250|UniProtKB:P20807}.
REGION 418 586 Domain III.
REGION 587 649 Linker.
REGION 650 815 Domain IV.
ACT_SITE 129 129 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 334 334 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 358 358 {ECO:0000255|PROSITE-ProRule:PRU00239}.
SEQUENCE 815 AA; 93556 MW; 994A930F0223CCF4 CRC64;
MPTVISASVA PRTAAEPRSP GPVPHPAQSK ATEAGGGNAS GIYSAIISRN FPIIGVKEKT
FEQLHKKCLE KKVLYVDPEF PPDETSLFYS QKFPIQFIWK RPPEICENPR FIIDGANRTD
ICQGDLGDCW FLAAIACLTL NQRLLFRVIP HDQSFIENYA GIFHFQFWRY GEWVDVVIDD
CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVTEFFE
IRDAPSDMHK IMKKAIERGS LMGCSIDDGT NMTYGTSPSG LNMGELIARM VRNMDNSLFR
DSDLDPRASV ERPTRTIVPV QYETRMACGL VRGHAYSVTG LDEVLFKGEK VKLVRLRNPW
GQVEWNGSWS DGWKDWSFVD KDEKARLQHQ VTEDGEFWMS YEDFIYHFTK LEICNLTADA
LQSDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PDDSEVICSF
LVALMQKNRR KDRKLGANLF TIGFAIYEVP KEMHGNRQHL QKDFFLYNAS RARSKTYINM
REVSQRFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEVENTISV DRPVPIIFVS
DRANSNKELG VDQESEEGKG KTSPDKQEQS PQPQPGSSDQ ESEEQQQFRN IFKQIAGDDM
EICADELKKV LNTVVNKHKD LKTHGFTLES CRSMIALMDT DGSGKLNLQE FHHLWNKIKA
WQKIFKHYDT DQSGTINSYE MRNAVNDAGF HLNNQLYDII TMRYADKHMN IDFDSFICCF
VRLEGMFRAF HAFDKDGDGI IKLNVLEWLQ LTMYA


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