ID I3IUT6_ORENI Unreviewed; 914 AA.
AC I3IUT6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN Name=LOC100693654 {ECO:0000313|Ensembl:ENSONIP00000000376.2};
OS Oreochromis niloticus (Nile tilapia) (Tilapia nilotica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Oreochromini; Oreochromis.
OX NCBI_TaxID=8128 {ECO:0000313|Ensembl:ENSONIP00000000376.2, ECO:0000313|Proteomes:UP000005207};
RN [1] {ECO:0000313|Proteomes:UP000005207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Broad Institute Genome Assembly Team;
RG Broad Institute Sequencing Platform;
RA Di Palma F., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Oreochromis niloticus (Nile Tilapia).";
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSONIP00000000376.2}
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, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm,
CC perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085}.
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DR AlphaFoldDB; I3IUT6; -.
DR STRING; 8128.ENSONIP00000042092; -.
DR Ensembl; ENSONIT00000000375.2; ENSONIP00000000376.2; ENSONIG00000000300.2.
DR eggNOG; KOG3556; Eukaryota.
DR GeneTree; ENSGT00390000018123; -.
DR HOGENOM; CLU_003910_0_0_1; -.
DR TreeFam; TF318734; -.
DR Proteomes; UP000005207; Linkage group LG3.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 3.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11830; 40S RIBOSOMAL PROTEIN S3A; 1.
DR PANTHER; PTHR11830:SF45; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE CYLD-LIKE; 1.
DR Pfam; PF01302; CAP_GLY; 2.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM01052; CAP_GLY; 3.
DR SUPFAM; SSF74924; Cap-Gly domain; 3.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000005207};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 432..475
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 532..876
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 187..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 100565 MW; 653C83824CBC0AD2 CRC64;
MSGAHEEIRK RRPPKTFLIS TDIKVRDQLE GTIALQRGFI CQEQDLGRKG DSPWVKVLDN
DFMGKIDRRF LIDVPADLTG LLEAVKDPEA RLKLLSQPGK LQQLASLPSD SPLWVQIGQQ
DELAEAELKY IGPLTRGSSA VYFGVQLKGS AVGRGLGNGT YKGQRLFTCP EACALFVPAS
LIMPRQWSSS SEGQQRPRDF RQHPPNSSSQ VSPFSILPRT AESAPVTTQN HVRGPRVCFP
LDDKVCAGEV VFCGPLPGRA SSGMYVGAIL DTPDGNWDGT YKGEKLCHIP SILYGSHRTN
PTHKSSRTVL KVALPPVTKS VPISPPASAP KIALMPPIKP ALKSPPLPPP KPAQKPGLPA
PPPLPPPKPQ GLTAGQQQHT NGTHGPASPL RAPGNGDDAA ENGEAGSGSN LEVGSMVEVN
DPPLFGVIRW IGWINGISEP VAGIELEQEL SAGTDGSYLG ERHFRCPANK GLFVKLRNCR
RDSRFPAPEM PVNQVERCNS IAFAEWGSER VEEHTPPVEG DEARELYQGW KKGIQGHLNS
CYLDATLFSL FSCCSSADCV LFWPTDPEID QSSSQAQDLL RCDIVNPLRR YGYVCASKTM
ALRRLLEAAN SDMGFTNQEK DPEEFLNKLF QLLRVEPLLK IRSMSQQPQE CHLYQLFPPA
LPPSPSSPES LSPVDSPIPL SSAPSMRVAS VQTLLESSFL HSGLKFVEAP SCLLLLMPRF
GKDFKMFDAI LPTLSLDITD LLDDTLRQCT ICQAVAEWEC LQCYDDIDIT PGHLKQYCKT
CNVQVHSHRK RASHNPVKIG VPGEQWTGPL HCTRQRMSLF AVTCIETSHY VSFVKNGPLD
TDWLFFDSMA DREGGENGFN IPQVKACPEV GRYLSLSEEE LSRVDPSSLR EAARRLLCDS
YMCLYHSPEL SLYK
//
