ID K7FYC7_PELSI Unreviewed; 705 AA.
AC K7FYC7;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Calpain-3 {ECO:0000256|RuleBase:RU367132};
DE EC=3.4.22.54 {ECO:0000256|RuleBase:RU367132};
GN Name=CAPN3 {ECO:0000313|Ensembl:ENSPSIP00000013037.1};
OS Pelodiscus sinensis (Chinese softshell turtle) (Trionyx sinensis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Trionychia;
OC Trionychidae; Pelodiscus.
OX NCBI_TaxID=13735 {ECO:0000313|Ensembl:ENSPSIP00000013037.1, ECO:0000313|Proteomes:UP000007267};
RN [1] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
RG Soft-shell Turtle Genome Consortium;
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000007267}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Daiwa-1 {ECO:0000313|Proteomes:UP000007267};
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).
RN [3] {ECO:0000313|Ensembl:ENSPSIP00000013037.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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|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}.
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DR EMBL; AGCU01135040; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01135041; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01135042; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; K7FYC7; -.
DR Ensembl; ENSPSIT00000013100.1; ENSPSIP00000013037.1; ENSPSIG00000011344.1.
DR GeneTree; ENSGT00940000156092; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR Proteomes; UP000007267; 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; 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; 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; 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; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU367132};
KW Cytoplasm {ECO:0000256|RuleBase:RU367132};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Metal-binding {ECO:0000256|RuleBase:RU367132};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 68..410
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT REGION 608..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 123
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 327
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 351
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 705 AA; 80990 MW; C35F271E28342386 CRC64;
MPSAINAVVA QQTEAGSVPS TNISTTAETG GGPGGIYSAI ISRNQPIIRV KEKTFEELHK
KCLEKKILYE DPDFPPNESS LFYNQKLPVK FEWKRPPEIC ENPRFIIGGA NRTDICQGEL
GDCWFLAAIA CLTLNEKLLC RVIPHDQTFI KNYAGIFHFQ FWRYGDWVDV VVDDFLPTYN
NQLVFTKSSQ RNEFWSALLE KAYAKLHGSY EALKGGNTTE AMEDFTGGVT EFYEIKDAPK
DIYKIMKHAS DRGSLMACSI DDNMGFSYGS APQSDLGELI ARMVKNVNSM PQIDPALEFQ
SVDERPAWTI VPMQFETRMT CGLVKGHAYS VTAVEETSFK AGKIKLVRLR NPWGQVEWKG
AWSDRSDEWT LIDKAEKIRL QHNIEEDGEF WMSFEDFMRY FTKLEICNIT PDTLEADKLH
TWTVSVNEGR WVRGCSGGGC RNYPDTFWTN PQYRLKLLEE DDDPEDNEVV CSFLVALMQK
NRRKERKLGA NLLTIGFAIY EVPKEMHGNK QHLQKDFFLY NASKARSKSY INIREVSERF
RLPPSEYVII PSTYEPHQEG EFILRVFSEK RNLSEEVENK IEVERPSKKK KDKPIIFVSD
RANSNKELKV DDISDKEKKK TSRDEKKKSN EPTPTKSDKD SEEEEQFRNI FQQIAGDDME
ISADELRSVL NNVLKKHKDL KTEGFALESC RSMIALMDVS FSNHR
//
