ID K7FM40_PELSI Unreviewed; 716 AA.
AC K7FM40;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Calpain-1 catalytic subunit {ECO:0000256|ARBA:ARBA00020246};
DE EC=3.4.22.52 {ECO:0000256|ARBA:ARBA00012482};
DE AltName: Full=Calcium-activated neutral proteinase 1 {ECO:0000256|ARBA:ARBA00031279};
DE AltName: Full=Calpain mu-type {ECO:0000256|ARBA:ARBA00031878};
DE AltName: Full=Calpain-1 large subunit {ECO:0000256|ARBA:ARBA00032619};
DE AltName: Full=Micromolar-calpain {ECO:0000256|ARBA:ARBA00032278};
GN Name=CAPN1 {ECO:0000313|Ensembl:ENSPSIP00000009100.1};
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:ENSPSIP00000009100.1, 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:ENSPSIP00000009100.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Broad endopeptidase specificity.; EC=3.4.22.52;
CC Evidence={ECO:0000256|ARBA:ARBA00001208};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
CC Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC {ECO:0000256|ARBA:ARBA00004370}.
CC -!- SIMILARITY: Belongs to the peptidase C2 family.
CC {ECO:0000256|ARBA:ARBA00007623}.
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DR EMBL; AGCU01174383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174386; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGCU01174389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006136645.1; XM_006136583.2.
DR RefSeq; XP_006136646.1; XM_006136584.2.
DR AlphaFoldDB; K7FM40; -.
DR STRING; 13735.ENSPSIP00000009100; -.
DR MEROPS; C02.001; -.
DR Ensembl; ENSPSIT00000009146.1; ENSPSIP00000009100.1; ENSPSIG00000008053.1.
DR GeneID; 102458417; -.
DR KEGG; pss:102458417; -.
DR CTD; 823; -.
DR eggNOG; KOG0045; Eukaryota.
DR GeneTree; ENSGT00940000159147; -.
DR HOGENOM; CLU_010982_0_1_1; -.
DR OMA; WNRIKNY; -.
DR OrthoDB; 142935at2759; -.
DR TreeFam; TF314748; -.
DR Proteomes; UP000007267; Unassembled WGS sequence.
DR GO; GO:0001533; C:cornified envelope; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005764; C:lysosome; IEA:Ensembl.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0004198; F:calcium-dependent cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0032801; P:receptor catabolic process; IEA:Ensembl.
DR GO; GO:0097264; P:self proteolysis; IEA:Ensembl.
DR CDD; cd00214; Calpain_III; 1.
DR CDD; cd00044; CysPc; 1.
DR CDD; cd16198; EFh_PEF_CAPN1; 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:SF284; CALPAIN-1 CATALYTIC SUBUNIT; 1.
DR Pfam; PF01067; Calpain_III; 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; 1.
DR PROSITE; PS00139; THIOL_PROTEASE_CYS; 1.
PE 3: Inferred from homology;
KW Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU00239}; Reference proteome {ECO:0000313|Proteomes:UP000007267};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807, ECO:0000256|PROSITE-
KW ProRule:PRU00239}.
FT DOMAIN 55..354
FT /note="Calpain catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50203"
FT DOMAIN 617..652
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT ACT_SITE 115
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 272
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
FT ACT_SITE 296
FT /evidence="ECO:0000256|PIRSR:PIRSR622684-1,
FT ECO:0000256|PROSITE-ProRule:PRU00239"
SQ SEQUENCE 716 AA; 81751 MW; 6A3A8E94ECC6FFE6 CRC64;
MAEEIITPVY CTGVSAQVQK QRAKDLGLGK HENAVKYLGQ DFETLRNACL QRGSLFQDDT
FPPTASSLGF KELGPNSSKT YGIKWKRPTE MCSNPQFIVD GATRTDICQG ALGDCWLLAA
IASLTLNDTI LHRVVPHGQS FQSGYAGIFH FQIWQFGEWV DVVVDDLLPT KDGKLTFVHS
AEGNEFWSAL LEKAYAKVNG CYEALSGGST SEGFEDFTGG VTEWYELRKP PNDLYQIILK
ALERGSLLGC SIDITSAFDM EAVTFKKLVK GHAYSVTGAK QINFRGQSVN LIRMRNPWGE
VEWTGSWSDN SSEWNVVDPS VGQQLRIKME DGEFWMSFQD FLREFSRLEI CNLTPDTLKS
RKLRKWNTTL YDGTWRRGST AGGCRNYPAT FWINPQFKIR LEEVDDDDED DSYSRESGCS
FVMALMQKHR RRERRFGKDM ETIGFAVYEV PREFVGQSAV HLKRDFFLAN SSRARSEQFI
NLREVSTRFK LPPGEYIVVP STFEPNKEGD FVLRVFSEKK AGTEEMDDQI QANLPDEKVL
SESEIDESFK QMFKQLAGAD MEISVSELQT ILNKIISKHK DLRTKGFSTE SCRSMVNLMD
RDGNGKLGLV EFNILWNKIR NYLAVFRKFD LDKSGCMSAY EMRMALESAG FKLNKKLYEL
IITRYSEPDL AVDFDNFVCC LVRLETMFRF FQAMDTDKDG IITFDLFKWL QLTMFA
//
