ID M7C532_CHEMY Unreviewed; 688 AA.
AC M7C532;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Calpain-3 {ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|RuleBase:RU367132};
GN ORFNames=UY3_03184 {ECO:0000313|EMBL:EMP39588.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP39588.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
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|RuleBase:RU367132};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU367132}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367132}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623, ECO:0000256|RuleBase:RU367132}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00239}.
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DR EMBL; KB516251; EMP39588.1; -; Genomic_DNA.
DR AlphaFoldDB; M7C532; -.
DR STRING; 8469.M7C532; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; 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; cd00044; CysPc; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; 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; PF00648; Peptidase_C2; 2.
DR PRINTS; PR00704; CALPAIN.
DR SMART; SM00720; calpain_III; 1.
DR SMART; SM00230; CysPc; 1.
DR SMART; SM00054; EFh; 1.
DR SUPFAM; SSF49758; Calpain large subunit, middle domain (domain III); 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 2.
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|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367132};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367132};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU367132};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU367132}.
FT DOMAIN 68..406
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 596..631
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 661..688
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 512..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1"
SQ SEQUENCE 688 AA; 78658 MW; FCBFC7342FC998DF CRC64;
MPSAINAVLA QQTEAGSVPS TSISTTAETG GGSGGIYSAI ISRNQPIIGV REKTFEELHK
KCLEKKILYV DPDFPPNESS LFYSQKLPIT FEWKRPTEIC ENPRFIIDGA NRTDICQGEL
GDCWFLAAIA CLTLNEKLLC RVIPHDQTFI KNYAGIFHFQ FWRYGNWVDV VIDDCLPTYN
NQLVFTKSSQ RNEFWSALLE KAYAKLHGSY EALKGGNTTE AMEDFTGGVT EFYEIKDAPK
DIYKIMKHAK DRGSLMACSI DDNMGFSYRT APQSDLGELI ARMVKNVNSM LRTDSTLTFQ
GTDERPAWVY SKQTIPLGKT LSYKKTQKQE YTFPPAQRIS HPSACPASRS PHWPGTANCG
HSDEWNLIDK AEKIRLQYRI AEDGEFWMSF DDFMRYFTKL EMCNLTPDTL EADKLQTWTV
SVNEGRWVRG CSAGGCRNYP DTFWTNPQYR LELLEEDDDP EDNEVVCSFL VALMQKNRRK
ERKLGANLLT IGFAIYEPII FVSDRANSNK ELRVDEASDK EKKKTSRDEK KKSDEPTPTN
ADKDSEEEKQ FRNIFQQIAG DDMEISADEL RSVLNNVLKK HKDLKTKGFA LESCRSMIAL
MDKIFKHYDT DHSGTINSYE MRNAVKDAGF CLNKQLYDII TMRYADRNMN IDFDSFICCF
VRLEGMFRAF HAFDKDGDGI IKLNVLEE
//
