ID H2PUX6_PONAB Unreviewed; 355 AA.
AC H2PUX6; A0A2J8W4K2; A0A6D2W8G3;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=ATXN3L {ECO:0000313|Ensembl:ENSPPYP00000022516.1};
GN ORFNames=CR201_G0013357 {ECO:0000313|EMBL:PNJ64699.1};
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:ENSPPYP00000022516.1, ECO:0000313|Proteomes:UP000001595};
RN [1] {ECO:0000313|Ensembl:ENSPPYP00000022516.1, 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:PNJ64699.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Susie {ECO:0000313|EMBL:PNJ64699.1};
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:ENSPPYP00000022516.1}
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: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; NDHI03003400; PNJ64699.1; -; Genomic_DNA.
DR STRING; 9601.ENSPPYP00000022516; -.
DR Ensembl; ENSPPYT00000023474.2; ENSPPYP00000022516.1; ENSPPYG00000020129.2.
DR eggNOG; KOG2935; Eukaryota.
DR GeneTree; ENSGT00390000001830; -.
DR HOGENOM; CLU_031228_1_0_1; -.
DR OMA; WGLEIIH; -.
DR TreeFam; TF314228; -.
DR Proteomes; UP000001595; Chromosome X.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.40; -; 1.
DR Gene3D; 6.10.140.100; -; 1.
DR Gene3D; 1.10.287.10; S15/NS1, RNA-binding; 1.
DR InterPro; IPR033865; Ataxin-3.
DR InterPro; IPR006155; Josephin.
DR InterPro; IPR003903; UIM_dom.
DR PANTHER; PTHR14159; ATAXIN-3-RELATED; 1.
DR PANTHER; PTHR14159:SF0; ATAXIN-3-RELATED; 1.
DR Pfam; PF02099; Josephin; 1.
DR Pfam; PF16619; SUIM_assoc; 1.
DR Pfam; PF02809; UIM; 2.
DR PRINTS; PR01233; JOSEPHIN.
DR SMART; SM01246; Josephin; 1.
DR SMART; SM00726; UIM; 2.
DR PROSITE; PS50957; JOSEPHIN; 1.
DR PROSITE; PS50330; UIM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU00331}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001595};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 1..180
FT /note="Josephin"
FT /evidence="ECO:0000259|PROSITE:PS50957"
FT REGION 209..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..276
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 14
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 14
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 119
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00331"
FT ACT_SITE 119
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR633865-1,
FT ECO:0000256|PROSITE-ProRule:PRU00331"
SQ SEQUENCE 355 AA; 40796 MW; 956F055855C66F6B CRC64;
MDFIFHEKQE GFLCAQHCLN NLLQGEYFSP VELASIAHQL DEEERMRMAE GGVTSEEYLA
FLQQPSENMD DTGFFSIQVI SNALKFWGLE IIHFNNPEYQ KLGIDPINER SFICNYKQHW
FTIRKFGKHW FNLNSLLAGP ELVSDTCLAN FLARLQQQAY SVFVVKGDLP DCEADQLLQI
ISVEEMDTPK LNGKKSVKEK EHRVYKTVLE KVSEESDESG TSDQDDEDFQ RTLELSRQET
NREDEDLRRA IELSMQGSSG NTSQDLPKTS CVTPASEQPK KIKEDYFEQH QQEQKLQQQQ
SDLPGYSSYI HERPTTSSRA IESDLSDDIS EDTVQAAVDT VLEIMRKNLK IKGEK
//
