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-AUG-2022, entry version 15. 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, ECO:0000313|Proteomes:UP000265160}; RN [1] {ECO:0000313|Ensembl:ENSMZEP00005011238, 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} RP IDENTIFICATION. RG Ensembl; RL Submitted (DEC-2018) 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR RefSeq; XP_014265719.1; XM_014410233.1. 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 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 InterPro; IPR033865; Ataxin-3. DR InterPro; IPR006155; Josephin. DR InterPro; IPR003903; UIM_dom. DR PANTHER; PTHR14159; PTHR14159; 1. DR Pfam; PF02099; Josephin; 1. DR Pfam; PF02809; UIM; 2. 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 //