ID   A0A3P9BMS5_9CICH        Unreviewed;       348 AA.
AC   A0A3P9BMS5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   03-MAY-2023, entry version 18.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
OS   Maylandia zebra (zebra mbuna).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Maylandia; Maylandia zebra complex.
OX   NCBI_TaxID=106582 {ECO:0000313|Ensembl:ENSMZEP00005011238.1, ECO:0000313|Proteomes:UP000265160};
RN   [1] {ECO:0000313|Ensembl:ENSMZEP00005011238.1, ECO:0000313|Proteomes:UP000265160}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=25186727; DOI=10.1038/nature13726;
RA   Brawand D., Wagner C.E., Li Y.I., Malinsky M., Keller I., Fan S.,
RA   Simakov O., Ng A.Y., Lim Z.W., Bezault E., Turner-Maier J., Johnson J.,
RA   Alcazar R., Noh H.J., Russell P., Aken B., Alfoldi J., Amemiya C.,
RA   Azzouzi N., Baroiller J.F., Barloy-Hubler F., Berlin A., Bloomquist R.,
RA   Carleton K.L., Conte M.A., D'Cotta H., Eshel O., Gaffney L., Galibert F.,
RA   Gante H.F., Gnerre S., Greuter L., Guyon R., Haddad N.S., Haerty W.,
RA   Harris R.M., Hofmann H.A., Hourlier T., Hulata G., Jaffe D.B., Lara M.,
RA   Lee A.P., MacCallum I., Mwaiko S., Nikaido M., Nishihara H.,
RA   Ozouf-Costaz C., Penman D.J., Przybylski D., Rakotomanga M., Renn S.C.P.,
RA   Ribeiro F.J., Ron M., Salzburger W., Sanchez-Pulido L., Santos M.E.,
RA   Searle S., Sharpe T., Swofford R., Tan F.J., Williams L., Young S., Yin S.,
RA   Okada N., Kocher T.D., Miska E.A., Lander E.S., Venkatesh B., Fernald R.D.,
RA   Meyer A., Ponting C.P., Streelman J.T., Lindblad-Toh K., Seehausen O.,
RA   Di Palma F.;
RT   "The genomic substrate for adaptive radiation in African cichlid fish.";
RL   Nature 513:375-381(2014).
RN   [2] {ECO:0000313|Ensembl:ENSMZEP00005011238.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JAN-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   RefSeq; XP_014265719.1; XM_014410233.1.
DR   AlphaFoldDB; A0A3P9BMS5; -.
DR   STRING; 106582.XP_004540663.1; -.
DR   Ensembl; ENSMZET00005011627.1; ENSMZEP00005011238.1; ENSMZEG00005008446.1.
DR   GeneID; 101472976; -.
DR   KEGG; mze:101472976; -.
DR   CTD; 4287; -.
DR   GeneTree; ENSGT00390000001830; -.
DR   OrthoDB; 337428at2759; -.
DR   Proteomes; UP000265160; LG19.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR   Gene3D; 3.90.70.40; -; 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; 2.
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:UP000265160};
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          261..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        291..308
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        309..348
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   348 AA;  39058 MW;  5A4967B893282F47 CRC64;
     MDSIFHEKQE GSLCAQHCLN NLLQGEYFTP VDLSSIAHQL DEEERMRMAE GGMASEEYRT
     FLQQPSGNMD DSGFFSIQVI SNALRVWGLE LILFNSREYQ SLMINPINEK AFICNYKEHW
     FTIRKLGQQW FNLNSLLTGP ELISDTYLAL FLAQLQQEGY SIFVIRGNLP ECEAEQILGI
     MRVQQQQRPR LIGEEEAQTS SGSRSVALGQ SEMAFGVEDE VVDEDEELKR ALALSRQDID
     VEDEEADLRR AIQLSMQGAV MSNKSSECGV GNVKSGSQAA GSAAREQREG QNETLTAEEL
     RKRRQAYFDR QQQQTQTNIP QPKDTQPTGS SGSVNAGSEG DQQPKPSQ
//