CASP7_MESAU
ID CASP7_MESAU Reviewed; 303 AA.
AC P55214;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Caspase-7;
DE Short=CASP-7;
DE EC=3.4.22.60;
DE AltName: Full=Apoptotic protease Mch-3;
DE AltName: Full=ICE-like apoptotic protease 3;
DE Short=ICE-LAP3;
DE AltName: Full=SREBP cleavage activity 2;
DE Short=SCA-2;
DE Contains:
DE RecName: Full=Caspase-7 subunit p20;
DE Contains:
DE RecName: Full=Caspase-7 subunit p11;
DE Flags: Precursor;
GN Name=CASP7; Synonyms=MCH3;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Syrian; TISSUE=Liver;
RX PubMed=8643593; DOI=10.1073/pnas.93.11.5437;
RA Pai J.-T., Brown M.S., Goldstein J.L.;
RT "Purification and cDNA cloning of a second apoptosis-related cysteine
RT protease that cleaves and activates sterol regulatory element binding
RT proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:5437-5442(1996).
CC -!- FUNCTION: Involved in the activation cascade of caspases responsible
CC for apoptosis execution. Cleaves and activates sterol regulatory
CC element binding proteins (SREBPs). Overexpression promotes programmed
CC cell death (By similarity). Cleaves phospholipid scramblase proteins
CC XKR4, XKR8 and XKR9 (By similarity). {ECO:0000250|UniProtKB:P55210,
CC ECO:0000250|UniProtKB:P97864}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Strict requirement for an Asp residue at position P1 and has a
CC preferred cleavage sequence of Asp-Glu-Val-Asp-|-.; EC=3.4.22.60;
CC Evidence={ECO:0000250|UniProtKB:P55210};
CC -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11)
CC subunit. Interacts with BIRC6/bruce. Interacts with HSPA5 (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P55210}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- PTM: Cleavages by granzyme B or caspase-10 generate the two active
CC subunits. Propeptide domains can also be cleaved efficiently by
CC caspase-3. Active heterodimers between the small subunit of caspase-7
CC and the large subunit of caspase-3, and vice versa, also occur (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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DR EMBL; U47332; AAC52595.1; -; mRNA.
DR RefSeq; NP_001268771.1; NM_001281842.1.
DR AlphaFoldDB; P55214; -.
DR SMR; P55214; -.
DR STRING; 10036.XP_005063197.1; -.
DR MEROPS; C14.004; -.
DR GeneID; 101825089; -.
DR CTD; 840; -.
DR eggNOG; KOG3573; Eukaryota.
DR OrthoDB; 984395at2759; -.
DR BRENDA; 3.4.22.60; 3239.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00032; CASc; 1.
DR InterPro; IPR015471; Casp3/7.
DR InterPro; IPR029030; Caspase-like_dom_sf.
DR InterPro; IPR033139; Caspase_cys_AS.
DR InterPro; IPR016129; Caspase_his_AS.
DR InterPro; IPR002398; Pept_C14.
DR InterPro; IPR002138; Pept_C14_p10.
DR InterPro; IPR001309; Pept_C14_p20.
DR InterPro; IPR015917; Pept_C14A.
DR PANTHER; PTHR10454; PTHR10454; 1.
DR PANTHER; PTHR10454:SF31; PTHR10454:SF31; 1.
DR PRINTS; PR00376; IL1BCENZYME.
DR SMART; SM00115; CASc; 1.
DR SUPFAM; SSF52129; SSF52129; 1.
DR PROSITE; PS01122; CASPASE_CYS; 1.
DR PROSITE; PS01121; CASPASE_HIS; 1.
DR PROSITE; PS50207; CASPASE_P10; 1.
DR PROSITE; PS50208; CASPASE_P20; 1.
PE 1: Evidence at protein level;
KW Acetylation; Apoptosis; Cytoplasm; Direct protein sequencing; Hydrolase;
KW Protease; Reference proteome; Thiol protease; Zymogen.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P55210"
FT PROPEP 2..23
FT /note="N-terminally processed"
FT /evidence="ECO:0000269|PubMed:8643593"
FT /id="PRO_0000004620"
FT CHAIN 24..198
FT /note="Caspase-7 subunit p20"
FT /id="PRO_0000004621"
FT PROPEP 199..206
FT /evidence="ECO:0000250"
FT /id="PRO_0000004622"
FT CHAIN 207..303
FT /note="Caspase-7 subunit p11"
FT /id="PRO_0000004623"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 144
FT /evidence="ECO:0000250"
FT ACT_SITE 186
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P55210"
SQ SEQUENCE 303 AA; 34038 MW; EA29356D90984648 CRC64;
MADDQNCAPE LEKADPSGED GVDAKPDRSS IISSILGKKK KNASACPVKT ARDRVPTYLY
RMDFEKMGKC IIINNKNFDK VTGMDVRNGT DKDAEALFKC FRSLGFDVVV YNDCSCAKMQ
DLLRKASEED HSNSACFACV LLSHGEENLI YGKDGVTPIK DLTAHFRGDR CKTLLEKPKL
FFIQACRGTE LDDGVQADSG PINETDANPR YKIPVEADFL FAYSTVPGYY SWRNPGKGSW
FVQALCSILD EHGKDLEIMQ ILTRVNDRVA RHFESQCDDP CFNEKKQIPC MVSMLTKELY
FGR
