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Database: UniProt
Entry: A0A2I2UST5_FELCA
LinkDB: A0A2I2UST5_FELCA
Original site: A0A2I2UST5_FELCA 
ID   A0A2I2UST5_FELCA        Unreviewed;       729 AA.
AC   A0A2I2UST5;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 2.
DT   24-JAN-2024, entry version 33.
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:ENSFCAP00000035602.2,
GN   ECO:0000313|VGNC:VGNC:81025};
OS   Felis catus (Cat) (Felis silvestris catus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX   NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000035602.2, ECO:0000313|Proteomes:UP000011712};
RN   [1] {ECO:0000313|Ensembl:ENSFCAP00000035602.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000035602.2,
RC   ECO:0000313|Proteomes:UP000011712};
RX   PubMed=17975172; DOI=10.1101/gr.6380007;
RA   Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA   Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA   Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA   Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA   Tesler G., O'Brien S.J.;
RT   "Initial sequence and comparative analysis of the cat genome.";
RL   Genome Res. 17:1675-1689(2007).
RN   [2] {ECO:0000313|Ensembl:ENSFCAP00000035602.2, ECO:0000313|Proteomes:UP000011712}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000035602.2,
RC   ECO:0000313|Proteomes:UP000011712};
RA   Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT   "Sequence assembly of the Felis catus genome version 6.2.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSFCAP00000035602.2}
RP   IDENTIFICATION.
RC   STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000035602.2};
RG   Ensembl;
RL   Submitted (SEP-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}.
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DR   EMBL; AANG04001761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; A0A2I2UST5; -.
DR   Ensembl; ENSFCAT00000038550.2; ENSFCAP00000035602.2; ENSFCAG00000018326.4.
DR   VGNC; VGNC:81025; CAPN3.
DR   GeneTree; ENSGT00940000156092; -.
DR   Proteomes; UP000011712; Chromosome B3.
DR   Bgee; ENSFCAG00000018326; Expressed in eyeball of camera-type eye and 1 other cell type or tissue.
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; PF13405; EF-hand_6; 1.
DR   Pfam; PF13833; EF-hand_8; 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; 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|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:UP000011712};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW   ProRule:PRU00239}.
FT   DOMAIN          74..369
FT                   /note="Calpain catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50203"
FT   DOMAIN          630..665
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          695..729
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        129
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        286
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
FT   ACT_SITE        310
FT                   /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU00239"
SQ   SEQUENCE   729 AA;  84078 MW;  B3279B0D592D1C18 CRC64;
     MPTVISASVA PRTGAEPRSP GPIPQQGQGK TTEAGGGNPS GIYSAIISRN FPIIGVKEKT
     FEQLHKKCLE KKVLYLDPEF PPDETSLFYS QKFPIQFIWK RPPEICENPR FIIGGANRTD
     ICQGDLGDCW FLAAIACLTL NERLLFRVIP HDQSFTENYA GIFHFQFWRY GDWVDVVIDD
     CLPTYNNQLV FTKSNHRNEF WSALLEKAYA KLHGSYEALK GGNTTEAMED FTGGVTEFFE
     IKDAPRDMYK IMKKAIERGS LMGCSIDTIV PVQYETRMAC GLVKGHAYSV TGLEETLFKG
     EKVKLVRLRN PWGQVEWNGS WSDSWKDWSF VDKAEKARLQ HQVTEDGEFW MSYDDFIYHF
     TKLEICNLTA DALESDKMQT WTVSVNEGRW VRGCSAGGCR NFPDTFWTNP QYRLKLLEED
     DDPEDSEVIC SFLVALMQKN RRKDRKLGAN LFTIGFAIYE VPKEMHGNKQ HLQKDFFLYN
     ASKARSKTYI NMREVSERFR LPPSEYVIVP STYEPHQEGE FILRVFSEKR NLSEEVENTI
     SVDRPVPRPG NTGQETEEQQ QFRNIFRQIA GEDMEVCADE LKNILNTVVN KHKDLKTQGF
     TLESCRSMIA LMDTDGSGRL NLQEFHHLWK KIKAWQKIFK HYDTDQSGTI NSYEMRNAVN
     DAGFHLNSQL YDIITMRYAD KHMNIDFDSF ICCFVRLEGM FRAFNAFDKD GDGIIKLNVL
     EWLQLTMYA
//
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