ID H2NMN8_PONAB Unreviewed; 931 AA.
AC H2NMN8; A0A2J8RGU6;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 2.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=OTUD7A {ECO:0000313|Ensembl:ENSPPYP00000007132.2};
GN ORFNames=CR201_G0050974 {ECO:0000313|EMBL:PNJ07753.1};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601 {ECO:0000313|Ensembl:ENSPPYP00000007132.2, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000007132.2, ECO:0000313|Proteomes:UP000001595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Wilson R.K., Mardis E.;
RT "A 6x draft sequence assembly of the Pongo pygmaeus abelii genome.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PNJ07753.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ07753.1};
RA Pollen A., Hastie A., Hormozdiari F., Dougherty M., Liu R., Chaisson M.,
RA Hoppe E., Hill C., Pang A., Hillier L., Baker C., Armstrong J.,
RA Shendure J., Paten B., Wilson R., Chao H., Schneider V., Ventura M.,
RA Kronenberg Z., Murali S., Gordon D., Cantsilieris S., Munson K., Nelson B.,
RA Raja A., Underwood J., Diekhans M., Fiddes I., Haussler D., Eichler E.;
RT "High-resolution comparative analysis of great ape genomes.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSPPYP00000007132.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00000707};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the peptidase C64 family.
CC {ECO:0000256|ARBA:ARBA00005865}.
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DR EMBL; NDHI03003694; PNJ07753.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000007132; -.
DR Ensembl; ENSPPYT00000007428.2; ENSPPYP00000007132.2; ENSPPYG00000006293.2.
DR eggNOG; KOG4345; Eukaryota.
DR GeneTree; ENSGT00940000158999; -.
DR HOGENOM; CLU_013263_0_0_1; -.
DR OMA; RCAKQPE; -.
DR OrthoDB; 2909231at2759; -.
DR TreeFam; TF323312; -.
DR Proteomes; UP000001595; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd22773; OTU_OTUD7A; 1.
DR CDD; cd14347; UBA_Cezanne_like; 1.
DR Gene3D; 1.20.5.4770; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR002653; Znf_A20.
DR PANTHER; PTHR13367:SF9; OTU DOMAIN-CONTAINING PROTEIN 7A; 1.
DR PANTHER; PTHR13367; UBIQUITIN THIOESTERASE; 1.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF01754; zf-A20; 1.
DR SMART; SM00259; ZnF_A20; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50802; OTU; 1.
DR PROSITE; PS51036; ZF_A20; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00451}.
FT DOMAIN 199..374
FT /note="OTU"
FT /evidence="ECO:0000259|PROSITE:PS50802"
FT DOMAIN 889..924
FT /note="A20-type"
FT /evidence="ECO:0000259|PROSITE:PS51036"
FT REGION 75..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..613
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 555..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..594
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 931 AA; 100920 MW; 466A58C848E750ED CRC64;
MVSSVLPNPT SAECWAALLH DPMTLDMDAV LSDFVRSTGA EPGLARDLLE GKNWDLTAAL
SDYEQLRQVH TANLPHVFNE GRGPKQPERE PQPGHKVERP CLQRQDDIAQ EKRLSRGISH
ASSAIVSLAR SHVASECNNE QFPLEMPIYT FQLPDLSVYS EDFRSFIERD LIEQATMVAL
EQAGRLNWWS TVCTSCKRLL PLATTGDGNC LLHAASLGMW GFHDRDLVLR KALYTMMRTG
AEREALKRRW RWQQTQQNKE EEWEREWTEL LKLASSEPRT HFSKNGGTGG GVDNSEDPVY
ESLEEFHVFV LAHILRRPIV VVADTMLRDS GGEAFAPIPF GGIYLPLEVP PNRCHCSPLV
LAYDQAHFSA LVSMEQRDQQ REQAVIPLTD SEHKLLPLHF AVDPGKDWEW GKDDNDNARL
AHLILSLEAK LNLLHSYMNV TWIRIPSETR APLAQPESPT ASAGEDVQSL ADSLDSDRDS
VCSNSNSNNG KNGKDKEKEK QRKEKDKTRA DSVANKLGSF SKTLGIKLKK NMGGLGGLVH
GKMGRANSAN GKNGDSAERG KEKKAKSRKG SKEESGASAS TSPSEKTTPS PTDKAAGASP
AEKGGGPRGD AWKYSTDVKL SLNILRAAMQ GERKFIFAGL LLTSHRHQFH EEMIGYYLTS
AQERFSAEQE QRRRDAATAA AAAAAAAAAA AAASTAKRPP RRPETEGAPV PERASPGPPT
QLVLKLKERP SPGPAAGRAA RAAAGGTASP GGGARRGGAS GPVPGRSPPA PARQSVIHVQ
ASGARDEACA PAVGALRPCA TYPQQNRSLS SQSYSPARAA ALRTVNTVES LARAVPGALP
GSAGAAGAAE HKSQTYTNGF GAARDGLEFA DADAPTARSN GECGRGGPGP VQRRCQRENC
AFYGRAETEH YCSYCYREEL RRRREARGAR P
//