ID   OTU5A_XENLA             Reviewed;         513 AA.
AC   Q7ZX21;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=OTU domain-containing protein 5-A;
DE            EC=3.4.19.12 {ECO:0000250|UniProtKB:Q96G74};
DE   AltName: Full=Deubiquitinating enzyme A;
DE            Short=DUBA;
GN   Name=otud5-a;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JAN-2003) 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|UniProtKB:Q96G74}.
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   -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
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DR   EMBL; BC046254; AAH46254.1; -; mRNA.
DR   RefSeq; NP_001080318.1; NM_001086849.1.
DR   AlphaFoldDB; Q7ZX21; -.
DR   SMR; Q7ZX21; -.
DR   MEROPS; C85.001; -.
DR   DNASU; 380010; -.
DR   GeneID; 380010; -.
DR   KEGG; xla:380010; -.
DR   AGR; Xenbase:XB-GENE-6254232; -.
DR   CTD; 380010; -.
DR   Xenbase; XB-GENE-6254232; otud5.S.
DR   OrthoDB; 691582at2759; -.
DR   Proteomes; UP000186698; Chromosome 8S.
DR   Bgee; 380010; Expressed in internal ear and 19 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0032496; P:response to lipopolysaccharide; ISS:UniProtKB.
DR   CDD; cd22752; OTU_OTUD5-like; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF4; OTU DOMAIN-CONTAINING PROTEIN 5; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..513
FT                   /note="OTU domain-containing protein 5-A"
FT                   /id="PRO_0000278227"
FT   DOMAIN          166..289
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          99..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          171..177
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          226..236
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          277..282
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          387..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        422..436
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        174
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        177
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:Q96G74"
FT   ACT_SITE        282
FT                   /evidence="ECO:0000250|UniProtKB:Q96G74"
SQ   SEQUENCE   513 AA;  55868 MW;  A8734AD6E686FEDA CRC64;
     MTILPKKKPP PPPDPEANGE RSGSGAPDSH SRSGARPRSS PPPRWAYPGN PSSAAERHTQ
     QVSPPPGSAT SGGAGPLGDG ALGSCCCCNG AGAGGCCSGP GHSKRRRQVL SAGPGATGNC
     PDTDDGAGNN SEDEYETAAQ TQHLDPDTAE QQELCFEKTL SDKKGFIIKQ MKEDGACLFR
     AVADQVYGDQ DMHEVVRKHC MDYLMKNADY FSNYVTEDFT TYINRKRKNN CHGNHIEMQA
     MAEMYNRPVE VYQYGTEPIN TFHGIQKNED EPIRVSYHRN IHYNSVVNPN KATIGVGLGL
     PSFKPGYAEQ SLMKSAIRTS EESWIEQQML EDKKRATDWE ATNEAIEEQV ARESYLQWLR
     DQEKQARQPR KASATCSSAT AAACSGLEEW SGRSPRQRST AGSPEHPDLH AELCMKPPSP
     GAPLILGKPP SPCAPGPSNQ MSTGADRATS PLVSLYPALE CRAIMQHMSP TAFGLKDWDN
     DEILASVLAA SQQEYLDTMK KSTLRRESSP DHS
//