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Database: UniProt
Entry: M7AZA5_CHEMY
LinkDB: M7AZA5_CHEMY
Original site: M7AZA5_CHEMY 
ID   M7AZA5_CHEMY            Unreviewed;       686 AA.
AC   M7AZA5;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Calpain-9 {ECO:0000313|EMBL:EMP25138.1};
GN   ORFNames=UY3_17819 {ECO:0000313|EMBL:EMP25138.1};
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:EMP25138.1, 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   -!- SIMILARITY: Belongs to the peptidase C2 family.
CC       {ECO:0000256|ARBA:ARBA00007623}.
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DR   EMBL; KB594214; EMP25138.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7AZA5; -.
DR   STRING; 8469.M7AZA5; -.
DR   Proteomes; UP000031443; Unassembled WGS sequence.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00214; Calpain_III; 1.
DR   CDD; cd00044; CysPc; 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; 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:SF385; CALPAIN-9; 1.
DR   Pfam; PF01067; Calpain_III; 1.
DR   Pfam; PF00648; Peptidase_C2; 1.
DR   PRINTS; PR00704; CALPAIN.
DR   SMART; SM00720; calpain_III; 1.
DR   SMART; SM00230; CysPc; 1.
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; 1.
DR   PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}.
FT   DOMAIN          15..282
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   DOMAIN          510..545
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          454..474
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        60
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        217
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        241
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   686 AA;  77642 MW;  9BAB9A86225D2221 CRC64;
     MTLIRERFAA ACDPFSELDP SEKPPIPFVW KRPGEIVKNP QFITGGATRT DICQGDLGDC
     WLLAAIASLT LKEKTLARVV PQDQNFGPGY AGIFHFQFWQ HNEWLDIVID DRLPTFKDRL
     VFLHSSEHNE FWSALLEKAY AKLNGSYEAL KGGSTLEAME DFTGGVGEMY EVKKAPENFY
     EILGKALERG SLVGCSIDTS SAAESEARTP FGLIKGHAYS VTGIDEVSYR GRKVQLVRPR
     NPWGQVEWNG RWSDNSPEWQ SVSPSEQKRL CQTVLDDGEF WYGTPLKNKY ADENQYSLKA
     DPFTASDVPV DPSYVLLHIG LSVRFLVYTF WTNPQIRLHL TEKDDGNDEC TFIAALMQKN
     RRKLRKLGAE MLTIGYAIYE SPSKDGHLNK DFFRYHPSKA RSKTYINLRE VSDRVKLPPG
     DYVIVPSTFE PHQEADFCLR IFSEKKAITE NVDGNIDINL PEPPKPTTPQ QETEEEKQFR
     ALFEQVAGED MEITAEELEY VLNAVLKKTN TIAFEKGVYL KFDSDKSGTM SSYELRSALT
     AAGFQLNNYL LQLIVLRYSD DQFRIDFDDF LNCLIRLENA NRASLPSLSE SMDPALLFCY
     EHKAIRSRGG STNFAAPKQS PLNCRRAQKS SRAAAQKPPW RQERWSCRRI AAAGHGLPPH
     SECRPKHLLG KLVPGAGPDK KNSMWG
//
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