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Database: UniProt
Entry: H2LTP7_ORYLA
LinkDB: H2LTP7_ORYLA
Original site: H2LTP7_ORYLA 
ID   H2LTP7_ORYLA            Unreviewed;       952 AA.
AC   H2LTP7;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 2.
DT   27-MAR-2024, entry version 66.
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:ENSORLP00000009467.2};
OS   Oryzias latipes (Japanese rice fish) (Japanese killifish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=8090 {ECO:0000313|Ensembl:ENSORLP00000009467.2, ECO:0000313|Proteomes:UP000001038};
RN   [1] {ECO:0000313|Ensembl:ENSORLP00000009467.2, ECO:0000313|Proteomes:UP000001038}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009467.2,
RC   ECO:0000313|Proteomes:UP000001038};
RX   PubMed=17554307; DOI=10.1038/nature05846;
RA   Kasahara M., Naruse K., Sasaki S., Nakatani Y., Qu W., Ahsan B., Yamada T.,
RA   Nagayasu Y., Doi K., Kasai Y., Jindo T., Kobayashi D., Shimada A.,
RA   Toyoda A., Kuroki Y., Fujiyama A., Sasaki T., Shimizu A., Asakawa S.,
RA   Shimizu N., Hashimoto S., Yang J., Lee Y., Matsushima K., Sugano S.,
RA   Sakaizumi M., Narita T., Ohishi K., Haga S., Ohta F., Nomoto H., Nogata K.,
RA   Morishita T., Endo T., Shin-I T., Takeda H., Morishita S., Kohara Y.;
RT   "The medaka draft genome and insights into vertebrate genome evolution.";
RL   Nature 447:714-719(2007).
RN   [2] {ECO:0000313|Ensembl:ENSORLP00000009467.2}
RP   IDENTIFICATION.
RC   STRAIN=Hd-rR {ECO:0000313|Ensembl:ENSORLP00000009467.2};
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   RefSeq; XP_004070051.1; XM_004070003.2.
DR   RefSeq; XP_011474412.1; XM_011476110.1.
DR   AlphaFoldDB; H2LTP7; -.
DR   STRING; 8090.ENSORLP00000009467; -.
DR   Ensembl; ENSORLT00000009468.2; ENSORLP00000009467.2; ENSORLG00000007552.2.
DR   eggNOG; KOG4345; Eukaryota.
DR   GeneTree; ENSGT00940000158999; -.
DR   HOGENOM; CLU_013263_0_0_1; -.
DR   InParanoid; H2LTP7; -.
DR   OrthoDB; 2909231at2759; -.
DR   TreeFam; TF323312; -.
DR   Proteomes; UP000001038; Chromosome 6.
DR   Bgee; ENSORLG00000007552; Expressed in brain and 8 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0070530; F:K63-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0043170; P:macromolecule metabolic process; IEA:UniProt.
DR   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR   GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
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; PF14555; UBA_4; 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:UP000001038};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT   DOMAIN          179..361
FT                   /note="OTU"
FT                   /evidence="ECO:0000259|PROSITE:PS50802"
FT   DOMAIN          908..943
FT                   /note="A20-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51036"
FT   REGION          438..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          518..605
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          665..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        440..476
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..499
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..559
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        560..605
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        665..682
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        697..728
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   952 AA;  106586 MW;  CCFDFF44FC55C308 CRC64;
     MTLDMDAVLS DFVRSTGAEP GLARDLLEGK NWDLSAALND YEELRQVHTA NLPQVFNEGR
     YYKQPEARDT PTHVSKIDRL CAQKQEDSTQ EKRLSRGISH ASSAIVSLAR LQVASECTSE
     QFPIEMPIYT FQLPDLSVYS EDFRSFIERD LIEQSTMMAL EQAGRLNWWS TMCTSCKKLL
     PLATTGDGNC LLHAASLGMW GFHDRDLMLR KSLYTMMKSG TERDALKRRW RWQQTQQNKE
     SGLVYTEEEW EREWNELLKL ASSEPRSHLS KNGNTSGGVD NSEDPVYESL EEFHVFVLAH
     VLRRPIVVVA DTMLRDSGGE AFAPIPFGGL YLPLEVPPTR CHCSPLVLAY DQAHFSALVS
     MEQRDQQREQ AVIPLTDSEH KLLALHFAVD PGRDWEWGRD DNDNAKLANL ILSLEAKLNL
     LHSYMNVTWI RIPSETRAPL AQPESPTASA GEDVQSLAES MDSDRESVGS NSHVNTGKSS
     KDKDKDKQRK DKDKGRTDSV ANRLGSFSKT LGIKLKKNMG GLGGLVHGKI NKSNSSSGRH
     TENGSEKAKK KESKATRGNK EESGQSTSST SSEKATSPSP TDGDRPSSSS PTERQDSSGR
     SSADKTLENW KYSTDVKLSL NILRAAMQGE RKFIFAALLL TSHRHQFHEE MISYYLTNAQ
     ERFSQEQEQK RKEAEKKPPA SSEVVLKNES VFQRERSDSS PPESCSPVLP HHTYNNPQPL
     SGLKTQGRNS PIPVAPPVSV PPLTPPTISH HVPHPAPSPA PYCSPIIGAK RPGPVPVSAH
     YSHTPPIQRH SVIHLQDVNM QSSIFQDEPY NKPVVGTLKT CATYPQQNRT LSSQSYSPAR
     LSGVRTVHTT GTLSYNMPAE NKSHTYTNGF NAGDIQDCLE FADEDNSSHT WLNQDKTKGR
     SSGTPLYCFQ QRRCKRENCS FYGRPETDNY CSYCYREELK RREKDGKVQR PA
//
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