ID G1NG52_MELGA Unreviewed; 810 AA.
AC G1NG52;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 94.
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:ENSMGAP00000012038.1};
OS Meleagris gallopavo (Wild turkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Meleagridinae; Meleagris.
OX NCBI_TaxID=9103 {ECO:0000313|Ensembl:ENSMGAP00000012038.1, ECO:0000313|Proteomes:UP000001645};
RN [1] {ECO:0000313|Ensembl:ENSMGAP00000012038.1, ECO:0000313|Proteomes:UP000001645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20838655; DOI=10.1371/journal.pbio.1000475;
RA Dalloul R.A., Long J.A., Zimin A.V., Aslam L., Beal K., Blomberg L.A.,
RA Bouffard P., Burt D.W., Crasta O., Crooijmans R.P., Cooper K.,
RA Coulombe R.A., De S., Delany M.E., Dodgson J.B., Dong J.J., Evans C.,
RA Frederickson K.M., Flicek P., Florea L., Folkerts O., Groenen M.A.,
RA Harkins T.T., Herrero J., Hoffmann S., Megens H.J., Jiang A., de Jong P.,
RA Kaiser P., Kim H., Kim K.W., Kim S., Langenberger D., Lee M.K., Lee T.,
RA Mane S., Marcais G., Marz M., McElroy A.P., Modise T., Nefedov M.,
RA Notredame C., Paton I.R., Payne W.S., Pertea G., Prickett D., Puiu D.,
RA Qioa D., Raineri E., Ruffier M., Salzberg S.L., Schatz M.C., Scheuring C.,
RA Schmidt C.J., Schroeder S., Searle S.M., Smith E.J., Smith J.,
RA Sonstegard T.S., Stadler P.F., Tafer H., Tu Z.J., Van Tassell C.P.,
RA Vilella A.J., Williams K.P., Yorke J.A., Zhang L., Zhang H.B., Zhang X.,
RA Zhang Y., Reed K.M.;
RT "Multi-platform next-generation sequencing of the domestic turkey
RT (Meleagris gallopavo): genome assembly and analysis.";
RL PLoS Biol. 8:E1000475-E1000475(2010).
RN [2] {ECO:0000313|Ensembl:ENSMGAP00000012038.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_003206523.1; XM_003206475.3.
DR AlphaFoldDB; G1NG52; -.
DR MEROPS; C02.004; -.
DR Ensembl; ENSMGAT00000012925.2; ENSMGAP00000012038.1; ENSMGAG00000011468.3.
DR GeneID; 100546035; -.
DR KEGG; mgp:100546035; -.
DR CTD; 825; -.
DR GeneTree; ENSGT00940000156092; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR OMA; RASCVAN; -.
DR OrthoDB; 142935at2759; -.
DR TreeFam; TF314748; -.
DR Proteomes; UP000001645; Chromosome 5.
DR Bgee; ENSMGAG00000011468; Expressed in breast and 7 other cell types or tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
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:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
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; PF00036; EF-hand_1; 1.
DR Pfam; PF13405; EF-hand_6; 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; 3.
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:UP000001645};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 68..410
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 681..707
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 711..746
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 776..810
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 584..638
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 351
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 810 AA; 93501 MW; 7988F8C4A153FCAD CRC64;
MPSAINPAVA QQTAAGSVSS TTSTTTEGTG GGTGGIYSAI ISRNQPIIKV KEKTYEELHK
KCLEKNILYE DPDFPPNETS LFYSQKVPIK FEWKRPREIC ENPRFIIGGA NRTDICQGEL
GDCWFLAAIA CLTLNKKLLC RVIPHDQSFI QNYAGIFHFQ FWRYGDWVDV IIDDCLPTYN
NQLVFTKSSQ RNEFWSALLE KAYAKLHGSY EALKGGNTTE AMEDFTGGVT EFYEIKDAPK
DIYKIMKHAI ARGSLMASSI DDNLGFSYGA APRSDIGEMI ARMVKNLENA QMTHPTVDHQ
GTDERPAWTI MPMQYETRMS CGLVKGHAYS VTAVEETTFK GEKIRLIRLR NPWGQVEWNG
PWSDKSEEWN FIKEEEKIRL QHKILEDGEF WISFEDFMRH 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 AGDDMEINAE
ELRNVLNNVV KKHKDLKTEG FELESCRSMI ALMDTDGSGK INFDEFRHLW DKIKSWQKIF
KHYDADHSGT INSYEMRNAV KDAGFRLNNQ LYDIITMRYA DKNMNIDFDS FICCFVRLDA
MFRAFHAFDK DGDGIIKLNV LEWLQLTMYA
//