ID A0A2K5X566_MACFA Unreviewed; 1113 AA.
AC A0A2K5X566;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 25.
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:ENSMFAP00000044558.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000044558.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000044558.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000044558.2}
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; A0A2K5X566; -.
DR Ensembl; ENSMFAT00000018853.2; ENSMFAP00000044558.2; ENSMFAG00000039436.2.
DR VEuPathDB; HostDB:ENSMFAG00000039436; -.
DR GeneTree; ENSGT00940000157962; -.
DR Proteomes; UP000233100; Chromosome 3.
DR Bgee; ENSMFAG00000039436; Expressed in skeletal muscle tissue and 13 other cell types or tissues.
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:UP000233100}.
FT DOMAIN 157..645
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 452..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..737
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..779
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 674..701
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 460..498
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1113 AA; 128649 MW; 54A249852681BA60 CRC64;
MTLHQQTFLN QLREITGIND TQILQQALKD SNGNLELAVA FLTAKNAKTP QQEEATYYQT
ALPGNDRYIS VGSQADTNVI DLTGDDKDDL QRAIALSLAE SNRAFRETGI TDEEQAISRV
LEASIAENKA CLKRTPTEVW RDSRNPYDRK RQDKAPVGLK NVGNTCWFSA VIQSLFNLLE
FRRLVLNYKP PSNAQDLPRN QKEHRNLPFM RELRYLFALL VGTKRKYVDP SRAVEILKDA
FKSNDSQQQD VSEFTHKLLD WLEDAFQMKA EEETDEEKPK NPMVELFYGR FLAVGVLEGK
KFENTEMFGQ YPLQVNGFKD LHECLEAAMI EGEIESLHSE NSGKSGQEHW FTELPPVLTF
ELSRFEFNQA LGRPEKIHNK LEFPQVLYLD RYMHRNREIT RIKREEIKRL KDYLTVLQQR
LERYLSYGSG PKRFPLVDVL QYALEFASSK PVCTSPVDDI DASSPPSGSI PSQTLPSTTE
QQGAPSSELP STSPSSVAAV SSRSVIHKPF TQSRIPPDLP MHPAPRHITE EELSVLESCL
HRWRTEIEND TRDLQESISR IHRTIELMYS DKSMIQVPYR LHAVLVHEGQ ANAGHYWAYI
FDHRESRWMK YNDIAVTKSS WEELVRDSFG GYRNASAYCL MYINDKAQFL IQEEFNKETG
QPLVGIETLP PDLRDFVEED NQRFEKELEE WDAQLAQKAL QEKLLASQKL RESETSVTTA
QAAGDPEYLE QPSRSDFSKH LKEETIRIIT KASHEHEDKS PETVLQSKPE NTTSQPLSNQ
RVVEVAIPHV GKFMIESKEG GYDDEIMMTP NMQGIIMAIG KSRSVYDRCG PEAGFFKAIK
LEYARLVKLA QEDTPPETDY RLHHVVVYFI QNQTPKKIIE KTLLEQFGDR NLSFDERCHN
IMKVAQAKLE MIKPEEVNLE EYEEWHQDYR KFRETTMYLI IGLENFQRES YIDSLLFLIC
AYQNNKELLS KGLYRGHDEE LISHYRRECL LKLNEQAAEL FESGEDREVN NGLIIMNEFI
VPFLPLLLVD EMEEKDILAV EDMRNRWCSY LGQEMEPHLQ EKLTDFLPKL LDCSMEIKSF
HEPPKLPSYS THELCERFAR IMLSLSRTPA DGR
//
