GenomeNet

Database: UniProt
Entry: G3W5D0_SARHA
LinkDB: G3W5D0_SARHA
Original site: G3W5D0_SARHA 
ID   G3W5D0_SARHA            Unreviewed;       281 AA.
AC   G3W5D0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   07-APR-2021, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=Caspase-3 {ECO:0000256|ARBA:ARBA00039708};
DE            EC=3.4.22.56 {ECO:0000256|ARBA:ARBA00038900};
GN   Name=LOC100922757 {ECO:0000313|Ensembl:ENSSHAP00000010635.2};
OS   Sarcophilus harrisii (Tasmanian devil) (Sarcophilus laniarius).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Metatheria; Dasyuromorphia; Dasyuridae; Sarcophilus.
OX   NCBI_TaxID=9305 {ECO:0000313|Ensembl:ENSSHAP00000010635.2, ECO:0000313|Proteomes:UP000007648};
RN   [1] {ECO:0000313|Ensembl:ENSSHAP00000010635.2, ECO:0000313|Proteomes:UP000007648}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21709235; DOI=10.1073/pnas.1102838108;
RA   Miller W., Hayes V.M., Ratan A., Petersen D.C., Wittekindt N.E., Miller J.,
RA   Walenz B., Knight J., Qi J., Zhao F., Wang Q., Bedoya-Reina O.C.,
RA   Katiyar N., Tomsho L.P., Kasson L.M., Hardie R.A., Woodbridge P.,
RA   Tindall E.A., Bertelsen M.F., Dixon D., Pyecroft S., Helgen K.M.,
RA   Lesk A.M., Pringle T.H., Patterson N., Zhang Y., Kreiss A., Woods G.M.,
RA   Jones M.E., Schuster S.C.;
RT   "Genetic diversity and population structure of the endangered marsupial
RT   Sarcophilus harrisii (Tasmanian devil).";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:12348-12353(2011).
RN   [2] {ECO:0000313|Ensembl:ENSSHAP00000010635.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Strict requirement for an Asp residue at positions P1 and P4.
CC         It has a preferred cleavage sequence of Asp-Xaa-Xaa-Asp-|- with a
CC         hydrophobic amino-acid residue at P2 and a hydrophilic amino-acid
CC         residue at P3, although Val or Ala are also accepted at this
CC         position.; EC=3.4.22.56; Evidence={ECO:0000256|ARBA:ARBA00036189};
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC       heterodimers, each one formed by a 17 kDa (p17) and a 12 kDa (p12)
CC       subunit. Interacts with BIRC6/bruce. {ECO:0000256|ARBA:ARBA00038525}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; G3W5D0; -.
DR   STRING; 9305.ENSSHAP00000010635; -.
DR   MEROPS; C14.003; -.
DR   Ensembl; ENSSHAT00000010729.2; ENSSHAP00000010635.2; ENSSHAG00000027604.1.
DR   eggNOG; KOG3573; Eukaryota.
DR   GeneTree; ENSGT00940000153232; -.
DR   HOGENOM; CLU_036904_2_0_1; -.
DR   OrthoDB; 2873736at2759; -.
DR   TreeFam; TF102023; -.
DR   Proteomes; UP000007648; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00032; CASc; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
DR   InterPro; IPR033139; Caspase_cys_AS.
DR   InterPro; IPR016129; Caspase_his_AS.
DR   InterPro; IPR011600; Pept_C14_caspase.
DR   InterPro; IPR002138; Pept_C14_p10.
DR   InterPro; IPR001309; Pept_C14_p20.
DR   InterPro; IPR015917; Pept_C14A.
DR   PANTHER; PTHR10454; CASPASE; 1.
DR   PANTHER; PTHR10454:SF198; CASPASE-3; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; Caspase-like; 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   3: Inferred from homology;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007648};
KW   S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW   Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   DOMAIN          42..166
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          187..281
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
SQ   SEQUENCE   281 AA;  31809 MW;  0FEBC579D58B8751 CRC64;
     MENTEITIDS KSSKSSGLKI FHGSKSVESG LSSDSYKMDY PEMGLCVIIN NKNFHPNTGM
     SFRSGTDVDA AHLRDTFKSL KYEVRNKNDL TCKEIIELLY NVSKEDHSQR SSFVCVILSH
     GEEGIIFGTD GSVELKRLTY FFKGDKCKSL TGKPKLFIIQ ACRGTELDCG VEVDSGPDDN
     DTDEDITCQK IPVEADFLYA YSTAPGYFSW RNEKDGSWFI QSLCAVLKQY AHKLEIMQIL
     TRVNWKVATE FESYSLDATF HAKKQVPCIM SMLTKELYFF P
//
DBGET integrated database retrieval system