ID   OTU6A_MOUSE             Reviewed;         290 AA.
AC   Q6IE21; A2ADU1; A8E630;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=OTU domain-containing protein 6A;
DE            EC=3.4.19.12;
DE   AltName: Full=Hin-6 protease;
GN   Name=Otud6a; Synonyms=Hin6;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION.
RX   PubMed=15060002; DOI=10.1101/gr.1946304;
RA   Puente X.S., Lopez-Otin C.;
RT   "A genomic analysis of rat proteases and protease inhibitors.";
RL   Genome Res. 14:609-622(2004).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys-
CC       29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze
CC       'Lys-11'-linked ubiquitin chains (By similarity). {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;
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DR   EMBL; AL671299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC153817; AAI53818.1; -; mRNA.
DR   EMBL; BN000372; CAE51898.1; -; mRNA.
DR   CCDS; CCDS53146.1; -.
DR   RefSeq; NP_001156663.1; NM_001163191.1.
DR   AlphaFoldDB; Q6IE21; -.
DR   SMR; Q6IE21; -.
DR   STRING; 10090.ENSMUSP00000059861; -.
DR   MEROPS; C85.008; -.
DR   iPTMnet; Q6IE21; -.
DR   PhosphoSitePlus; Q6IE21; -.
DR   jPOST; Q6IE21; -.
DR   MaxQB; Q6IE21; -.
DR   PaxDb; 10090-ENSMUSP00000059861; -.
DR   ProteomicsDB; 294402; -.
DR   Antibodypedia; 43771; 129 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000060241.3; ENSMUSP00000059861.3; ENSMUSG00000051582.3.
DR   GeneID; 408193; -.
DR   KEGG; mmu:408193; -.
DR   UCSC; uc012hms.1; mouse.
DR   AGR; MGI:3644685; -.
DR   CTD; 139562; -.
DR   MGI; MGI:3644685; Otud6a.
DR   VEuPathDB; HostDB:ENSMUSG00000051582; -.
DR   eggNOG; KOG2606; Eukaryota.
DR   GeneTree; ENSGT00940000163556; -.
DR   HOGENOM; CLU_034963_0_0_1; -.
DR   InParanoid; Q6IE21; -.
DR   OMA; PADGHCM; -.
DR   OrthoDB; 242020at2759; -.
DR   PhylomeDB; Q6IE21; -.
DR   TreeFam; TF315010; -.
DR   BioGRID-ORCS; 408193; 2 hits in 75 CRISPR screens.
DR   PRO; PR:Q6IE21; -.
DR   Proteomes; UP000000589; Chromosome X.
DR   RNAct; Q6IE21; Protein.
DR   Bgee; ENSMUSG00000051582; Expressed in spermatid and 8 other cell types or tissues.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR   GO; GO:0035871; P:protein K11-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990167; P:protein K27-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0035523; P:protein K29-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:1990168; P:protein K33-linked deubiquitination; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd22761; OTU_OTUD6; 1.
DR   Gene3D; 3.90.70.80; -; 1.
DR   InterPro; IPR003323; OTU_dom.
DR   InterPro; IPR049772; OTU_OTUD6.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   PANTHER; PTHR12419; OTU DOMAIN CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR12419:SF13; OTU DOMAIN-CONTAINING PROTEIN 6A; 1.
DR   Pfam; PF02338; OTU; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS50802; OTU; 1.
PE   1: Evidence at protein level;
KW   Hydrolase; Protease; Reference proteome; Thiol protease;
KW   Ubl conjugation pathway.
FT   CHAIN           1..290
FT                   /note="OTU domain-containing protein 6A"
FT                   /id="PRO_0000076278"
FT   DOMAIN          142..276
FT                   /note="OTU"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT   REGION          27..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..153
FT                   /note="Cys-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          211..221
FT                   /note="Variable-loop"
FT                   /evidence="ECO:0000250"
FT   REGION          259..269
FT                   /note="His-loop"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        34..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        150
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        153
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        269
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   290 AA;  33738 MW;  DFCA5FACB71A6469 CRC64;
     MSDTEQELQR VIRRHYREKR ELQAHIQTLK ASVPKNDKGR RKQMLADISR LEAEMEQRHK
     QELEKFGENP DSSVDSVTAD LEKMNLENMP PRPPKAQKRR DRRAHQERRH QERMPAAQAE
     QLAANRREEE EKVAAILGAK NLEMKTIPAD GHCMYRAIQD QLVFSVTIES LRYRTAYYMR
     KHIDDFLPFF TEPEAGNFYT REDFLRYCDD IVHNASWGGQ LELRALSHVL QTPIEVVQAN
     SPTIVIGEEY TRKPVTLVYL HYACDFGEHY NSVKPIEVAG AFGGMAPRLF
//