ID G1P857_MYOLU Unreviewed; 914 AA.
AC G1P857;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=USP20 {ECO:0000313|Ensembl:ENSMLUP00000006338.2};
OS Myotis lucifugus (Little brown bat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Microchiroptera; Vespertilionidae;
OC Myotis.
OX NCBI_TaxID=59463 {ECO:0000313|Ensembl:ENSMLUP00000006338.2, ECO:0000313|Proteomes:UP000001074};
RN [1] {ECO:0000313|Ensembl:ENSMLUP00000006338.2, ECO:0000313|Proteomes:UP000001074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSMLUP00000006338.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Deubiquitinating enzyme that removes conjugated ubiquitin
CC from specific proteins to regulate different cellular processes.
CC {ECO:0000256|RuleBase:RU366025}.
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 ECO:0000256|RuleBase:RU366025};
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. USP20/USP33 subfamily.
CC {ECO:0000256|ARBA:ARBA00008269}.
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 EMBL; AAPE02050576; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPE02050577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_006104835.1; XM_006104773.2.
DR RefSeq; XP_014302523.1; XM_014447037.1.
DR AlphaFoldDB; G1P857; -.
DR STRING; 59463.ENSMLUP00000006338; -.
DR MEROPS; C19.025; -.
DR Ensembl; ENSMLUT00000006934.2; ENSMLUP00000006338.2; ENSMLUG00000006914.2.
DR GeneID; 102433737; -.
DR KEGG; mlf:102433737; -.
DR CTD; 10868; -.
DR eggNOG; KOG1870; Eukaryota.
DR GeneTree; ENSGT00940000158829; -.
DR HOGENOM; CLU_004896_0_0_1; -.
DR InParanoid; G1P857; -.
DR OMA; IDQDDEC; -.
DR OrthoDB; 227085at2759; -.
DR TreeFam; TF352179; -.
DR Proteomes; UP000001074; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IEA:Ensembl.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0043124; P:negative regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR GO; GO:0010508; P:positive regulation of autophagy; IEA:Ensembl.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF13; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 20; 1.
DR Pfam; PF06337; DUSP; 2.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00695; DUSP; 2.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51283; DUSP; 2.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Endocytosis {ECO:0000256|ARBA:ARBA00022583};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366025};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366025};
KW Reference proteome {ECO:0000313|Proteomes:UP000001074};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Thiol protease {ECO:0000256|ARBA:ARBA00022807,
KW ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00502}.
FT DOMAIN 6..112
FT /note="UBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50271"
FT DOMAIN 145..685
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT DOMAIN 687..780
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 789..892
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT REGION 262..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 914 AA; 101744 MW; 380FE71E65F9CDF4 CRC64;
MGDSRDLCPH LDSIGEVTKD DLLLKSKGAC QSCGVSGPNL WACLQVACPY VGCGESFADH
STLHAQAQKH NLTVNLTTFR VWCYACEKEV FPEQRLAAPL PAASPRLFEQ DSPLPSHPLK
AVPIAVADEG ESESEDDDLK PRGLTGMKNL GNSCYMNAAL QALSNCPPLT QFFLECGGLV
RTDKKPALCK SYQKLVSEVW HRKRPSYVVP TSLSHGIKLV NPMFRGYAQQ DTQEFLRCLM
DQLHEELKEP VVAVAAALTE ARDSDLSDSD EKREGDRSPS EDEFLSCDSS SDRGEGGGQG
RGEGGSAEAE LLIGDEAGRA ISEKERMKDR KFSWGQQRTS SEQVDEDADV DTALAALDPR
PPEAQPPSPR SASPCRTPEP DNEAHMRSAS RPCSPVHHHE GHTKLASSPP RASPVRMGPA
YVLKKAQGPS TGSRRRKEQR YRSVISDIFD GSILSLVQCL TCDRVSTTVE TFQDLSLPIP
GKEDLAKLHS AIYQNAPAKP GSCGDSYAAQ GWLAFIMEYI RRFVVSCTPS WFWGPVITLE
DCLAAFFAAD ELKGDNMYSC ERCKKLRNGV KYCKVLRLPE ILCIHLKRFR HEVMYSFKIS
SHVSFPLEGL DLRPFLAKEC TSQITTYDLL SVICHHGTAG SGHYIAYCQN VINGQWYEFD
DQYVTEVHET VVQSSEAYVL FYRKSSEEAV RERQQVVSLA AMREPSLLRF YVSREWLNKF
NTFAEPGPIT NHTFLCSHGG IPPNKYHYID DLVVILPQNV WEHLYSRFGG GPAVNHLYVC
SICQVEIEAL AKRRRIEIDT FIKLNKAFQA EESPGVIYCI SMHWFREWEA FVKGKDNEPP
GPIDNSRIAQ VKGSGHIQLK PGADYGQISE ETWAYLHSLY GGGPEIAIRQ SVAQLPDPDS
LHGEQKIEAE TRAL
//
