OTU6A_MOUSE
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 03-AUG-2022, entry version 102.
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; Q6IE21; -.
DR PRIDE; Q6IE21; -.
DR ProteomicsDB; 294402; -.
DR Antibodypedia; 43771; 118 antibodies from 24 providers.
DR Ensembl; ENSMUST00000060241; ENSMUSP00000059861; ENSMUSG00000051582.
DR GeneID; 408193; -.
DR KEGG; mmu:408193; -.
DR UCSC; uc012hms.1; mouse.
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; QDQLVFS; -.
DR OrthoDB; 1541668at2759; -.
DR PhylomeDB; Q6IE21; -.
DR TreeFam; TF315010; -.
DR BioGRID-ORCS; 408193; 2 hits in 70 CRISPR screens.
DR PRO; PR:Q6IE21; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q6IE21; protein.
DR Bgee; ENSMUSG00000051582; Expressed in spermatid and 6 other tissues.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; ISS:UniProtKB.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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 InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR Pfam; PF02338; OTU; 1.
DR SUPFAM; SSF54001; SSF54001; 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
