OTU5A_DANRE
ID OTU5A_DANRE Reviewed; 560 AA.
AC Q08BW0; A9JTE0; B0UYD0; B0UYD1; Q8JFX0;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=OTU domain-containing protein 5-A;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme A;
DE Short=DUBA;
GN Name=otud5a; Synonyms=otud5;
GN ORFNames=si:dkey-83k24.3, si:rp71-30i22.1, zgc:154072;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tuebingen;
RX PubMed=23594743; DOI=10.1038/nature12111;
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., Threadgold G.,
RA Harden G., Ware D., Begum S., Mortimore B., Kerry G., Heath P.,
RA Phillimore B., Tracey A., Corby N., Dunn M., Johnson C., Wood J., Clark S.,
RA Pelan S., Griffiths G., Smith M., Glithero R., Howden P., Barker N.,
RA Lloyd C., Stevens C., Harley J., Holt K., Panagiotidis G., Lovell J.,
RA Beasley H., Henderson C., Gordon D., Auger K., Wright D., Collins J.,
RA Raisen C., Dyer L., Leung K., Robertson L., Ambridge K., Leongamornlert D.,
RA McGuire S., Gilderthorp R., Griffiths C., Manthravadi D., Nichol S.,
RA Barker G., Whitehead S., Kay M., Brown J., Murnane C., Gray E.,
RA Humphries M., Sycamore N., Barker D., Saunders D., Wallis J., Babbage A.,
RA Hammond S., Mashreghi-Mohammadi M., Barr L., Martin S., Wray P.,
RA Ellington A., Matthews N., Ellwood M., Woodmansey R., Clark G., Cooper J.,
RA Tromans A., Grafham D., Skuce C., Pandian R., Andrews R., Harrison E.,
RA Kimberley A., Garnett J., Fosker N., Hall R., Garner P., Kelly D., Bird C.,
RA Palmer S., Gehring I., Berger A., Dooley C.M., Ersan-Urun Z., Eser C.,
RA Geiger H., Geisler M., Karotki L., Kirn A., Konantz J., Konantz M.,
RA Oberlander M., Rudolph-Geiger S., Teucke M., Lanz C., Raddatz G.,
RA Osoegawa K., Zhu B., Rapp A., Widaa S., Langford C., Yang F.,
RA Schuster S.C., Carter N.P., Harrow J., Ning Z., Herrero J., Searle S.M.,
RA Enright A., Geisler R., Plasterk R.H., Lee C., Westerfield M.,
RA de Jong P.J., Zon L.I., Postlethwait J.H., Nusslein-Volhard C.,
RA Hubbard T.J., Roest Crollius H., 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=WIK; TISSUE=Embryo, and Ovary;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Deubiquitinating enzyme that may function as negative
CC regulator of the innate immune system. Has peptidase activity towards
CC 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. Can also cleave
CC 'Lys-11'-linked ubiquitin chains (in vitro) (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q08BW0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q08BW0-2; Sequence=VSP_034009;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI55305.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI55305.1; Type=Miscellaneous discrepancy; Note=BC155304 contains a 74bp deletion, resulting in a frameshift.; Evidence={ECO:0000305};
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 EMBL; AL590148; CAD43417.1; -; Genomic_DNA.
DR EMBL; CR450685; CAQ14391.1; -; Genomic_DNA.
DR EMBL; CR450685; CAQ14392.1; -; Genomic_DNA.
DR EMBL; BC124533; AAI24534.1; -; mRNA.
DR EMBL; BC155304; AAI55305.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001068578.1; NM_001075110.1. [Q08BW0-1]
DR AlphaFoldDB; Q08BW0; -.
DR SMR; Q08BW0; -.
DR STRING; 7955.ENSDARP00000114334; -.
DR MEROPS; C85.001; -.
DR PaxDb; Q08BW0; -.
DR Ensembl; ENSDART00000144986; ENSDARP00000114334; ENSDARG00000059006. [Q08BW0-1]
DR GeneID; 555459; -.
DR KEGG; dre:555459; -.
DR CTD; 555459; -.
DR ZFIN; ZDB-GENE-030616-61; otud5a.
DR eggNOG; KOG2605; Eukaryota.
DR GeneTree; ENSGT00940000158963; -.
DR InParanoid; Q08BW0; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; Q08BW0; -.
DR TreeFam; TF326812; -.
DR PRO; PR:Q08BW0; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 8.
DR Bgee; ENSDARG00000059006; Expressed in testis and 29 other tissues.
DR ExpressionAtlas; Q08BW0; baseline.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISS:UniProtKB.
DR GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR InterPro; IPR031084; OTU5.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR PANTHER; PTHR12419:SF4; PTHR12419:SF4; 1.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..560
FT /note="OTU domain-containing protein 5-A"
FT /id="PRO_0000278226"
FT DOMAIN 211..334
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..222
FT /note="Cys-loop"
FT /evidence="ECO:0000250"
FT REGION 271..281
FT /note="Variable-loop"
FT /evidence="ECO:0000250"
FT REGION 322..327
FT /note="His-loop"
FT /evidence="ECO:0000250"
FT REGION 411..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..36
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 219
FT /evidence="ECO:0000255"
FT ACT_SITE 222
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 327
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..236
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_034009"
SQ SEQUENCE 560 AA; 60038 MW; 425C1E21E8A5A5EA CRC64;
MTILPKKKPN SSVGVSDHPD DPDRRTGSDP HQHQHQHSHG VRPGARPRAS PPPWSYQAAP
PASREDRRTE SSSRPQQASP PPVGAGSSGG PGDATGMACV SGNRAELSGG VGCGGGMGGC
CSGPGLSKRR RQATCSGGVA GGGTGPGAAG GGGGGGGGGG VGGPSPEQEE GAGYNSEDEY
ENASRLQSED PATVEQQEHW FEKALQEKKG FVIKKMKEDG ACLFRAVADQ VYGDQDMHEV
VRKHCMDYLM KNADYFSNYV TEDFTTYINR KRKNNCHGNH IEMQAMAEMY NRPVEVYQSG
TEPINTFHGI HQNNDEPIRV SYHRNIHYNS VVNPNKATIG VGLGLPAFKP GFADQSLMKN
AIKTSEESWI EQQMLEDKKR ATDWEATNEA IEEQVARESY LQWLRDQEKQ ARQPRKASAT
CSSATAAASS GLEEWNARSP RQRSSAPSPE IPDPAHSDTA AKPPSPAGAL ALSKPPSPCA
PGPSNQACVG PDRPTSSSLV SLYPALGYRA IMQEMSPTAF GLTDWEDDEI LASVLAVSQQ
EYLDSMKKNA MHREPSPDSS
