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Calpain-3 (EC 3.4.22.54) (Calcium-activated neutral proteinase 3) (CANP 3) (Calpain L3) (Calpain p94) (Muscle-specific calcium-activated neutral protease 3) (New calpain 1) (nCL-1)

 CAN3_PIG                Reviewed;         821 AA.
P43368; O46596; Q28961;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
30-AUG-2017, entry version 127.
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=Muscle-specific calcium-activated neutral protease 3;
AltName: Full=New calpain 1;
Short=nCL-1;
Name=CAPN3; Synonyms=NCL1;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE.
Sun W., Muir M.W., Hancock D.L., Stuart J.J.;
"Cloning the full length cDNA of pig skeletal muscle specific calpain
by Polymerase Chain Reaction.";
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE OF 277-651.
TISSUE=Skeletal muscle;
Ji S.Q., Hancock D.L., Bidwell C.A., Anderson D.B.;
Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 372-509.
TISSUE=Blood;
PubMed=8833248; DOI=10.1007/s003359900062;
Briley G.P., Riggs P.K., Womack J.E., Hancock D.L., Bidwell C.A.;
"Chromosomal localization of the porcine skeletal muscle calpain
gene.";
Mamm. Genome 7:226-228(1996).
-!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
-!- CATALYTIC ACTIVITY: Broad endopeptidase activity.
-!- ENZYME REGULATION: Activated by micromolar concentrations of
calcium and inhibited by calpastatin.
-!- 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.
-!- TISSUE SPECIFICITY: Skeletal muscle.
-!- SIMILARITY: Belongs to the peptidase C2 family. {ECO:0000305}.
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EMBL; AF043295; AAB99847.1; -; mRNA.
EMBL; U05678; AAA17032.1; -; mRNA.
EMBL; U23954; AAA67685.1; -; Genomic_DNA.
RefSeq; NP_999336.1; NM_214171.1.
UniGene; Ssc.16057; -.
ProteinModelPortal; P43368; -.
SMR; P43368; -.
STRING; 9823.ENSSSCP00000005095; -.
MEROPS; C02.004; -.
PaxDb; P43368; -.
PeptideAtlas; P43368; -.
PRIDE; P43368; -.
GeneID; 397349; -.
KEGG; ssc:397349; -.
CTD; 825; -.
eggNOG; KOG0045; Eukaryota.
eggNOG; ENOG410XP0B; LUCA.
HOGENOM; HOG000232035; -.
HOVERGEN; HBG012645; -.
InParanoid; P43368; -.
KO; K08573; -.
BRENDA; 3.4.22.54; 6170.
Proteomes; UP000008227; Unplaced.
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; Complete proteome; Cytoplasm; Hydrolase; Metal-binding;
Protease; Reference proteome; Repeat; Thiol protease.
CHAIN 1 821 Calpain-3.
/FTId=PRO_0000207709.
DOMAIN 73 417 Calpain catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00239}.
DOMAIN 649 683 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 692 725 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 722 757 EF-hand 3. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 787 821 EF-hand 4. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 662 672 1. {ECO:0000250|UniProtKB:P20807}.
CA_BIND 705 716 2. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 735 741 3. {ECO:0000250|UniProtKB:P20807,
ECO:0000255|PROSITE-ProRule:PRU00448}.
CA_BIND 800 806 4. {ECO:0000250|UniProtKB:P20807}.
REGION 418 586 Domain III.
REGION 587 649 Linker.
REGION 650 821 Domain IV.
ACT_SITE 128 128 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 334 334 {ECO:0000255|PROSITE-ProRule:PRU00239}.
ACT_SITE 358 358 {ECO:0000255|PROSITE-ProRule:PRU00239}.
CONFLICT 281 281 K -> N (in Ref. 2; AAA17032).
{ECO:0000305}.
CONFLICT 307 308 GC -> V (in Ref. 2; AAA17032).
{ECO:0000305}.
CONFLICT 446 447 GC -> TG (in Ref. 2; AAA17032).
{ECO:0000305}.
CONFLICT 446 446 G -> A (in Ref. 3; AAA67685).
{ECO:0000305}.
CONFLICT 487 487 K -> R (in Ref. 2; AAA17032).
{ECO:0000305}.
CONFLICT 570 570 I -> M (in Ref. 2; AAA17032).
{ECO:0000305}.
CONFLICT 579 579 N -> K (in Ref. 2; AAA17032).
{ECO:0000305}.
SEQUENCE 821 AA; 94551 MW; 868E2769AD3AAFDF CRC64;
MPTVISASMA PRTGASQVPR TMPQAAQGKG TEAGVGNPGG KYSAIISRNF PIIGVKEKTF
EQLHKKCLEK KVLYLDPEFP PDETSLFYSQ KFPIQFVWKR PPEICENPRF IIGGANRTDI
CQGDLGDCWF LAAIACLTLN KRLLFRVIPH DQSFTENYAG IFHFQFWRYG DWVDVVIDDC
LPTYNNQLVF TKSNHRNEFW SALLEKAYAK LHGSYEALKG GNTTEAMEDF TGGVTEFFEI
KDAPRDMYKI MKKAIERGSL MGCSIDDGTN MTYGTSPSGL KMGDLIARMV RNMDESRLRD
SDLIPEGCSD DRPTRTIVPV QFETRMACGL VKGHAYSVTG LEEALFKGEK VKLVRLRNPW
GQVEWNGSWS DSWKDWSFVD KDEKARLQHQ VTEDGEFWMS YDDFIYHFTK LEICNLTADA
LESDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PDDSEVICSF
LVALMQKNRR KDRKLGANLF TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSRTYINM
REVSERFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEVENTISV DRPVRKKKTK
PIIFVSDRAN SNKELGVDQE SEEGQDKTSP DKQEKSPKPE PSNTDQESEE QQQFRNIFRQ
IAGDDMEICA DELKNVLNRV VNKHKDLKTE GFTLESCRSM IALMDTDGSG RLNLQEFHHL
WKKIKSWQKI FKHYDTDQSG TINSYEMRNA VNDAGFHLNN QLYDIITMRY ADKYMNIDFD
SFICCFVRLE GMFRAFNAFD KDGDGIIKLN VLEWLQLTMY A


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