ID M3YEJ8_MUSPF Unreviewed; 821 AA.
AC M3YEJ8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Calpain-3 {ECO:0000256|ARBA:ARBA00023844, ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|ARBA:ARBA00023801, ECO:0000256|RuleBase:RU367132};
GN Name=CAPN3 {ECO:0000313|Ensembl:ENSMPUP00000009755.1,
GN ECO:0000313|RefSeq:XP_004751248.1};
OS Mustela putorius furo (European domestic ferret) (Mustela furo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Mustelinae; Mustela.
OX NCBI_TaxID=9669 {ECO:0000313|Ensembl:ENSMPUP00000009755.1};
RN [1] {ECO:0000313|Ensembl:ENSMPUP00000009755.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2023) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_004751248.1}
RP IDENTIFICATION.
RC TISSUE=Brain {ECO:0000313|RefSeq:XP_004751248.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Calcium-regulated non-lysosomal thiol-protease.
CC {ECO:0000256|RuleBase:RU367132}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase activity.; EC=3.4.22.54;
CC Evidence={ECO:0000256|ARBA:ARBA00023702,
CC ECO:0000256|RuleBase:RU367132};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|RuleBase:RU367132}. Nucleus, nucleolus
CC {ECO:0000256|ARBA:ARBA00004604}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623, ECO:0000256|RuleBase:RU367132}.
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DR EMBL; AEYP01028319; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AEYP01028320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_004751248.1; XM_004751191.3.
DR STRING; 9669.ENSMPUP00000009755; -.
DR MEROPS; C02.004; -.
DR Ensembl; ENSMPUT00000009912.1; ENSMPUP00000009755.1; ENSMPUG00000009829.1.
DR GeneID; 101675191; -.
DR KEGG; mpuf:101675191; -.
DR CTD; 825; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000156092; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR OMA; DMDGEFW; -.
DR OrthoDB; 142935at2759; -.
DR Proteomes; UP000000715; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0055103; F:ligase regulator activity; IEA:Ensembl.
DR GO; GO:0060090; F:molecular adaptor activity; IEA:Ensembl.
DR GO; GO:0031402; F:sodium ion binding; IEA:Ensembl.
DR GO; GO:0008307; F:structural constituent of muscle; IEA:Ensembl.
DR GO; GO:0031432; F:titin binding; IEA:Ensembl.
DR GO; GO:1990092; P:calcium-dependent self proteolysis; IEA:Ensembl.
DR GO; GO:0071277; P:cellular response to calcium ion; IEA:Ensembl.
DR GO; GO:0071472; P:cellular response to salt stress; IEA:Ensembl.
DR GO; GO:0070315; P:G1 to G0 transition involved in cell differentiation; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0033234; P:negative regulation of protein sumoylation; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0045862; P:positive regulation of proteolysis; IEA:Ensembl.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR GO; GO:0014718; P:positive regulation of satellite cell activation involved in skeletal muscle regeneration; IEA:Ensembl.
DR GO; GO:0012501; P:programmed cell death; IEA:Ensembl.
DR GO; GO:0030163; P:protein catabolic process; IEA:Ensembl.
DR GO; GO:0031648; P:protein destabilization; IEA:Ensembl.
DR GO; GO:0072657; P:protein localization to membrane; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:Ensembl.
DR GO; GO:0043122; P:regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0045661; P:regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0045214; P:sarcomere organization; IEA:Ensembl.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16190; EFh_PEF_CAPN3; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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_PEF.
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; CALPAIN; 1.
DR PANTHER; PTHR10183:SF329; CALPAIN-3; 1.
DR Pfam; PF01067; Calpain_III; 1.
DR Pfam; PF16648; Calpain_u2; 1.
DR Pfam; PF13405; EF-hand_6; 1.
DR Pfam; PF13833; EF-hand_8; 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; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50203; CALPAIN_CAT; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 2.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU367132};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367132}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000000715};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 74..417
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 722..757
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 787..821
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 611..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..634
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..650
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 129
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 334
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 358
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 821 AA; 94328 MW; BF3FAEAABFAA1A54 CRC64;
MPTVISPSVA PRTGAEPRSP GPIPPPGEGK TTEAGGTNPS GIYSAIISRN FPIIGVKEKT
FEQLHKKCLE KKVLYLDPEF PPDETSLFYS QKFPIQFIWK RPPEICENPR FIIGGANRTD
ICQGDLGDCW FLAAIACLTL NERLLFRVIP HDQSFTENYA GIFHFQFWRY GDWVDVVIDD
CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVTEFFE
IKDAPRDMYK IMKKAIERGS LMGCSIDDGT NMTYGTSPSG LKMGDLIARM VRNMDNSQLR
DSDLLPRGSE DRPTRTIVPV QYETRMACGL VKGHAYSVTG LEEALFKGEK VKLVRLRNPW
GQVEWNGSWS DGWKDWSFVD KDEKARLQHQ VTEDGEFWMS YDDFIYHFTK LEICNLTADA
LESDKLQTWT VSVNEGRWVR GCSAGGCRNF PDTFWTNPQY RLKLLEEDDD PDDSEVICSF
LVALMQKNRR KDRKLGANLF TIGFAIYEVP KEMHGNKQHL QKDFFLYNAS KARSKTYINM
REVSERFRLP PSEYVIVPST YEPHQEGEFI LRVFSEKRNL SEEVENTISV DRPVKKKKTK
PIIFVSDRAN SNKELGVDQE SEEGKDKTSP DKQEKSPQPR PGNTDQESEE QLQFRNIFRQ
IAGDDMEVCA DELKNILNTV VNKHKDLKTQ GFTLESCRSM IALMDTDGSG RLNLQEFHHL
WKKIKAWQKI FKHYDTDHSG TINSYEMRNA VNDAGFHLNS QLYDIITMRY ADKHMNIDFD
SFICCFVRLE GMFRAFNAFD KDGDGIIKLN VLEWLQLTMY A
//
