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Database: UniProt
Entry: A0A2K5XCH2_MANLE
LinkDB: A0A2K5XCH2_MANLE
Original site: A0A2K5XCH2_MANLE 
ID   A0A2K5XCH2_MANLE        Unreviewed;      1048 AA.
AC   A0A2K5XCH2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=ubiquitinyl hydrolase 1 {ECO:0000256|ARBA:ARBA00012759};
DE            EC=3.4.19.12 {ECO:0000256|ARBA:ARBA00012759};
GN   Name=USP25 {ECO:0000313|Ensembl:ENSMLEP00000000980.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000000980.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000000980.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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};
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DR   AlphaFoldDB; A0A2K5XCH2; -.
DR   Ensembl; ENSMLET00000004188.1; ENSMLEP00000000980.1; ENSMLEG00000003404.1.
DR   GeneTree; ENSGT00940000157962; -.
DR   OMA; XKKFENT; -.
DR   Proteomes; UP000233140; Unplaced.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:InterPro.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR   CDD; cd02665; Peptidase_C19I; 1.
DR   CDD; cd14354; UBA_UBP25; 1.
DR   CDD; cd20486; USP25_C; 1.
DR   Gene3D; 6.10.250.1720; -; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR   Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR001394; Peptidase_C19_UCH.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR044635; UBP14-like.
DR   InterPro; IPR003903; UIM_dom.
DR   InterPro; IPR018200; USP_CS.
DR   InterPro; IPR028889; USP_dom.
DR   PANTHER; PTHR43982; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR43982:SF6; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 2-RELATED; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF02809; UIM; 2.
DR   SMART; SM00726; UIM; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF46934; UBA-like; 1.
DR   PROSITE; PS50330; UIM; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS00973; USP_2; 1.
DR   PROSITE; PS50235; USP_3; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000233140}.
FT   DOMAIN          162..650
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          457..503
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          720..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          679..706
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        465..503
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1048 AA;  121557 MW;  AD768AB4F1F52452 CRC64;
     LSIERNVWHQ QTFLNQLREI TGINDTQILQ QALKDSNGNL ELAVAFLTAK NAKTPQQEEA
     TYYQTALPGN DRYISVGSQA DTNVIDLTGD DKDDLQRAIA LSLAESNRAF RETGITDEEQ
     AISRVLEASI AENKACLKRT PTEVWRDSRN PYDRKRQDKA PVGLKNVGNT CWFSAVIQSL
     FNLLEFRRLV LNYKPPSNAQ DLPRNQKEHR NLPFMRELRY LFALLVGTKR KYVDPSRAVE
     ILKDAFKSND SQQQDVSEFT HKLLDWLEDA FQMKAEEETD EEKPKNPMVE LFYGRFLAVG
     VLEGKKFENT EMFGQYPLQV NGFKDLHECL EAAMIEGEIE SLHSENSGKS GQEHWFTELP
     PVLTFELSRF EFNQALGRPE KIHNKLEFPQ VLYLDRYMHR NREITRIKRE EIKRLKDYLT
     VLQQRLERYL SYGSGPKRFP LVDVLQYALE FASSKPVCTS PVDDIDASSP PSGSIPSQTL
     PSTTEQQGAP SSELPSTSPS SVAAVSSRSV IHKPFTQSRI PPDLPMHPAP RHITEEELSV
     LESCLHRWRT EIENDTRDLQ ESISRIHRTI ELMYSDKSMI QVPYRLHAVL VHEGQANAGH
     YWAYIFDHRE SRWMKYNDIA VTKSSWEELV RDSFGGYRNA SAYCLMYIND KAQFLIQEEF
     NKETGQPLVG IETLPPDLRD FVEEDNQRFE KELEEWDAQL AQKALQEKLL ASQKLRESET
     SVTTAQAAGD PEYLEQPSRS DFSKHLKEET IRIITKASHE HEDKSPETVL QSAIKLEYAR
     LVKLAQEDTP PETDYRLHHV VVYFIQNQTP KKIIEKTLLE QFGDRNLSFD ERCHNIMKVA
     QAKLEMIKPE EVNLEEYEEW HQDYRKFRET TMYLIIGLEN FQRESYIDSL LFLICAYQNN
     KELLSKGLYR GHDEELISHY RRECLLKLNE QAAELFESGE DREVNNGLII MNEFIVPFLP
     LLLVDEMEEK DILAVEDMRN RWCSYLGQEM EPHLQEKLTD FLPKLLDCSM EIKSFHEPPK
     LPSYSTHELC ERFARIMLSL SRTPADGR
//
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