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Database: UniProt
Entry: Q29R92_DANRE
LinkDB: Q29R92_DANRE
Original site: Q29R92_DANRE 
ID   Q29R92_DANRE            Unreviewed;       245 AA.
AC   Q29R92; A0A8M1N8D8;
DT   04-APR-2006, integrated into UniProtKB/TrEMBL.
DT   04-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Caspase-6 {ECO:0000256|ARBA:ARBA00029534};
DE            EC=3.4.22.59 {ECO:0000256|ARBA:ARBA00029486};
GN   Name=casp6b.2 {ECO:0000313|Ensembl:ENSDARP00000093958,
GN   ECO:0000313|RefSeq:NP_001035069.1,
GN   ECO:0000313|ZFIN:ZDB-GENE-060312-12};
GN   Synonyms=casp6c {ECO:0000313|RefSeq:NP_001035069.1}, casp6l2
GN   {ECO:0000313|RefSeq:NP_001035069.1}, zgc:136946
GN   {ECO:0000313|RefSeq:NP_001035069.1};
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955 {ECO:0000313|EMBL:AAI14319.1};
RN   [1] {ECO:0000313|RefSeq:NP_001035069.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=16888647; DOI=10.1038/sj.cdd.4402015;
RA   Eimon P.M., Kratz E., Varfolomeev E., Hymowitz S.G., Stern H., Zha J.,
RA   Ashkenazi A.;
RT   "Delineation of the cell-extrinsic apoptosis pathway in the zebrafish.";
RL   Cell Death Differ. 13:1619-1630(2006).
RN   [2] {ECO:0000313|EMBL:AAI14319.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Whole {ECO:0000313|EMBL:AAI14319.1};
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|Ensembl:ENSDARP00000093958}
RP   IDENTIFICATION.
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000093958};
RG   Ensembl;
RL   Submitted (FEB-2012) to UniProtKB.
RN   [4] {ECO:0000313|Ensembl:ENSDARP00000093958, ECO:0000313|Proteomes:UP000000437}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tuebingen {ECO:0000313|Ensembl:ENSDARP00000093958};
RX   PubMed=23594743; DOI=10.1038/nature12111;
RG   Genome Reference Consortium Zebrafish;
RA   Howe K., Clark M.D., Torroja C.F., Torrance J., Berthelot C., Muffato M.,
RA   Collins J.E., Humphray S., McLaren K., Matthews L., McLaren S., Sealy I.,
RA   Caccamo M., Churcher C., Scott C., Barrett J.C., Koch R., Rauch G.J.,
RA   White S., Chow W., Kilian B., Quintais L.T., Guerra-Assuncao J.A., Zhou Y.,
RA   Gu Y., Yen J., Vogel J.H., Eyre T., Redmond S., Banerjee R., Chi J., Fu B.,
RA   Langley E., Maguire S.F., Laird G.K., Lloyd D., Kenyon E., Donaldson S.,
RA   Sehra H., Almeida-King J., Loveland J., Trevanion S., Jones M., Quail M.,
RA   Willey D., Hunt A., Burton J., Sims S., McLay K., Plumb B., Davis J.,
RA   Clee C., Oliver K., Clark R., Riddle C., Elliot D., Eliott D.,
RA   Threadgold G., Harden G., Ware D., Begum S., Mortimore B., Mortimer B.,
RA   Kerry G., Heath P., Phillimore B., Tracey A., Corby N., Dunn M.,
RA   Johnson C., Wood J., Clark S., Pelan S., Griffiths G., Smith M.,
RA   Glithero R., Howden P., Barker N., Lloyd C., Stevens C., Harley J.,
RA   Holt K., Panagiotidis G., Lovell J., Beasley H., Henderson C., Gordon D.,
RA   Auger K., Wright D., Collins J., Raisen C., Dyer L., Leung K.,
RA   Robertson L., Ambridge K., Leongamornlert D., McGuire S., Gilderthorp R.,
RA   Griffiths C., Manthravadi D., Nichol S., Barker G., Whitehead S., Kay M.,
RA   Brown J., Murnane C., Gray E., Humphries M., Sycamore N., Barker D.,
RA   Saunders D., Wallis J., Babbage A., Hammond S., Mashreghi-Mohammadi M.,
RA   Barr L., Martin S., Wray P., Ellington A., Matthews N., Ellwood M.,
RA   Woodmansey R., Clark G., Cooper J., Cooper J., Tromans A., Grafham D.,
RA   Skuce C., Pandian R., Andrews R., Harrison E., Kimberley A., Garnett J.,
RA   Fosker N., Hall R., Garner P., Kelly D., Bird C., Palmer S., Gehring I.,
RA   Berger A., Dooley C.M., Ersan-Urun Z., Eser C., Geiger H., Geisler M.,
RA   Karotki L., Kirn A., Konantz J., Konantz M., Oberlander M.,
RA   Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G., Osoegawa K., Zhu B.,
RA   Rapp A., Widaa S., Langford C., Yang F., Schuster S.C., Carter N.P.,
RA   Harrow J., Ning Z., Herrero J., Searle S.M., Enright A., Geisler R.,
RA   Plasterk R.H., Lee C., Westerfield M., de Jong P.J., Zon L.I.,
RA   Postlethwait J.H., Nusslein-Volhard C., Hubbard T.J., Roest Crollius H.,
RA   Rogers J., Stemple D.L.;
RT   "The zebrafish reference genome sequence and its relationship to the human
RT   genome.";
RL   Nature 496:498-503(2013).
RN   [5] {ECO:0000313|RefSeq:NP_001035069.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24613356;
RA   Zhang P., Yao Q., Lu L., Li Y., Chen P.J., Duan C.;
RT   "Hypoxia-inducible factor 3 is an oxygen-dependent transcription activator
RT   and regulates a distinct transcriptional response to hypoxia.";
RL   Cell Rep. 6:1110-1121(2014).
RN   [6] {ECO:0000313|RefSeq:NP_001035069.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=28402832; DOI=10.1016/j.chemosphere.2017.03.100;
RA   Zhao J., Huang G., Xu T., Yin D., Bai J., Gu W.;
RT   "Early developmental exposure to pentachlorophenol causes alterations on
RT   mRNA expressions of caspase protease family in zebrafish embryos.";
RL   Chemosphere 180:141-148(2017).
RN   [7] {ECO:0000313|RefSeq:NP_001035069.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=29791492; DOI=10.1371/journal.pone.0197966;
RA   Spead O., Verreet T., Donelson C.J., Poulain F.E.;
RT   "Characterization of the caspase family in zebrafish.";
RL   PLoS ONE 13:E0197966-E0197966(2018).
RN   [8] {ECO:0000313|RefSeq:NP_001035069.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Strict requirement for Asp at position P1 and has a preferred
CC         cleavage sequence of Val-Glu-His-Asp-|-.; EC=3.4.22.59;
CC         Evidence={ECO:0000256|ARBA:ARBA00029356};
CC   -!- SUBUNIT: Heterotetramer that consists of two anti-parallel arranged
CC       heterodimers, each one formed by a 18 kDa (Caspase-6 subunit p18) and a
CC       11 kDa (Caspase-6 subunit p11) subunit.
CC       {ECO:0000256|ARBA:ARBA00029473}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the peptidase C14A family.
CC       {ECO:0000256|ARBA:ARBA00010134, ECO:0000256|RuleBase:RU003971}.
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DR   EMBL; CT583642; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC114318; AAI14319.1; -; mRNA.
DR   RefSeq; NP_001035069.1; NM_001039980.1.
DR   STRING; 7955.ENSDARP00000093958; -.
DR   MEROPS; C14.005; -.
DR   Ensembl; ENSDART00000103182.5; ENSDARP00000093958.3; ENSDARG00000070368.5.
DR   GeneID; 664751; -.
DR   KEGG; dre:664751; -.
DR   AGR; ZFIN:ZDB-GENE-060312-12; -.
DR   CTD; 664751; -.
DR   ZFIN; ZDB-GENE-060312-12; casp6b.2.
DR   HOGENOM; CLU_036904_2_0_1; -.
DR   OMA; MCENSIR; -.
DR   OrthoDB; 2873736at2759; -.
DR   TreeFam; TF102023; -.
DR   Proteomes; UP000000437; Alternate scaffold 3.
DR   Proteomes; UP000000437; Chromosome 3.
DR   Bgee; ENSDARG00000070368; Expressed in intestine and 7 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0097200; F:cysteine-type endopeptidase activity involved in execution phase of apoptosis; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00032; CASc; 1.
DR   Gene3D; 3.40.50.1460; -; 1.
DR   InterPro; IPR029030; Caspase-like_dom_sf.
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:SF206; CASPASE-6; 1.
DR   Pfam; PF00656; Peptidase_C14; 1.
DR   PRINTS; PR00376; IL1BCENZYME.
DR   SMART; SM00115; CASc; 1.
DR   SUPFAM; SSF52129; Caspase-like; 1.
DR   PROSITE; PS01121; CASPASE_HIS; 1.
DR   PROSITE; PS50207; CASPASE_P10; 1.
DR   PROSITE; PS50208; CASPASE_P20; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Autocatalytic cleavage {ECO:0000256|ARBA:ARBA00022813};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000437}.
FT   DOMAIN          5..128
FT                   /note="Caspase family p20"
FT                   /evidence="ECO:0000259|PROSITE:PS50208"
FT   DOMAIN          151..243
FT                   /note="Caspase family p10"
FT                   /evidence="ECO:0000259|PROSITE:PS50207"
SQ   SEQUENCE   245 AA;  27714 MW;  4CCB3488F8E69644 CRC64;
     MKHAKRGLAL IFNQKDFSLL GLKTRKGTDK DRDSLVSRFE ELDFEVKAYN DYSRDKVLKE
     IKEVAAADHV DADCFVCIFL SHGEDGHVYA NDEKIKIPEI TDLFKGDKCR GLVGKPKIFI
     WQACRGDKKD DPVAPMSAED SDDEMAVDAG VSNTLPAGAD FIMCYSTTEG FCSFRDPLNG
     TWYIQDLCEI MGRYRSQLEF TNILTLVNRK VSLRSICDDL SATGTKQMPC FASMLTKRLF
     FRPKK
//
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