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Database: UniProt
Entry: A0A087QYR8_APTFO
LinkDB: A0A087QYR8_APTFO
Original site: A0A087QYR8_APTFO 
ID   A0A087QYR8_APTFO        Unreviewed;       794 AA.
AC   A0A087QYR8;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 45.
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};
DE   Flags: Fragment;
GN   ORFNames=AS27_02339 {ECO:0000313|EMBL:KFM06372.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM06372.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM06372.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM06372.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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; KL226001; KFM06372.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087QYR8; -.
DR   STRING; 9233.A0A087QYR8; -.
DR   MEROPS; C02.004; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
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; 2.
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:UP000053286};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}.
FT   DOMAIN          69..411
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   DOMAIN          673..699
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          703..738
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          768..794
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   ACT_SITE        124
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        328
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        352
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   NON_TER         794
FT                   /evidence="ECO:0000313|EMBL:KFM06372.1"
SQ   SEQUENCE   794 AA;  91212 MW;  E5922DBAB0C302B4 CRC64;
     MPSAINAAVA QQTAAGSVPS ATISTTTEGA GGGTGGIYSA IISRNQPIIG VKEKTYEELH
     KKCLEKNILY EDPDFPPNES SLFYSQKIPI KFEWKRPREI CENPRFIIGG ANRTDICQGE
     LGDCWFLAAI ACLTLNKKLL CRVIPHDQSF IQNYAGIFHF QFWRYGDWVD VVIDDCLPTY
     NNQLVFTKSS QRNEFWSALL EKAYAKLHGS YEALKGGNTT EAMEDFTGGV TEFYEIKDAP
     KDTYKIMKHA IDRGSLMASS IDDNLGFSYG SAPRSDIGEL IARMVKNLEN AQMTHSTVDY
     QGTDERPAWT IVPMQYETRM SCGLVKGHAY SVTAVEETTF KGEKIRLVRL RNPWGQVEWN
     GPWSDKSEEW NFINEAEKIR LQHKIMEDGE FWISFEDFMR HFTKLEICNL TPDTLEADKL
     QTWTVSVSEG RWVRGCSAGG CRNYPDTFWT NPQYRLKLLE EDDDPEDEEV VCSFLVALMQ
     KNRRKERKLG ANLYTIGFAI YEIHGTKHHL QKDFFLYNAS KARSKTYINM REISERFRLP
     PSEYVIIPST YEPHQEGEFI LRVFSEKRSL SEEVENTIEA ERPSPIIFVS DRANSNKELT
     ADEDTGEDGE KTHVDEKKVS AATKAREGNE EEKQFRNIFR QIAGDDMEIN AEELRNVLNN
     VVKKHKDLKT EGFELESCRS MIALMDTDGS GKINFDEFRH LWDKIKSWQK IFKRYDTDHS
     GTINSYEMRN AVNDAGFRLN NQLYDIITMR YADKNMNIDF DSFICCFVRL DAMFRAFHAF
     DKDGDGIIKL NVLE
//
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