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
//