ID A0A2H5MZW5_CITUN Unreviewed; 959 AA.
AC A0A2H5MZW5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN ORFNames=CUMW_004570 {ECO:0000313|EMBL:GAY32885.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY32885.1};
RN [1] {ECO:0000313|EMBL:GAY32885.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
CC -!- FUNCTION: Recognizes and hydrolyzes the peptide bond at the C-terminal
CC Gly of ubiquitin. Involved in the processing of poly-ubiquitin
CC precursors as well as that of ubiquitinated proteins.
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|RuleBase:RU366025};
CC -!- SIMILARITY: Belongs to the peptidase C19 family.
CC {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY32885.1}.
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DR EMBL; BDQV01000001; GAY32885.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5MZW5; -.
DR STRING; 55188.A0A2H5MZW5; -.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF75; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU366025};
KW Protease {ECO:0000256|RuleBase:RU366025};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 340..955
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 692..716
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..706
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 959 AA; 109060 MW; 927E4024DDC1DACE CRC64;
MTRLAEKLQL SLLLTRNTTR FLSRVSLSTL RLCKSLLSKT LAGLFSAMDN DYPFSSEGDD
HLFEFDYSNS SRQNNYFSQP TATNSRGLFD DDDRQKVYLV PYRWWKESQI LLAEKVGGVL
YEVSSNDDNT DLEILLHLKK KEGSVDSDCG EGGVSVREYA LVPEGMWLRA LKWHNDSKAA
VKDFGSSFAA DEQDVFPLQI RLSVSQETNS LLVKISLEDN KVDLYKRACN LFISVSEMLY
IWDFSGQTTQ FLMNDRVTMS DDFSAKPGEE VFLQLQVHGF SDSVGETNDE MAEHYKIIDS
ICNGSVKKNG SNDNLNSYIT SSNSVRHGSG NGGVCLLGLT GLRNLGNTCF MNSAIQCLAH
TPEIVDYFLG DYQKEINYEN PLGLNGELAL AFGDLIRKLW APGGIPVAPR MFKLKLANFA
PQFSGYNQHD SQEFLAFLLD GLHEDLNRVK CKPYLEAKDA EGRPEEEVAE EYWRNHRARN
DSIIVDLCQG QYRSMLVCPV CNKVSVTFDP LMYLSLPIPS TTMRTMTVTV LSTDGSTMPA
PFTVTVPKYG RFQDLIDALS TKCFLRNDEK LLVAEIYRSK IFRVLDEPSD LLGLIRDEDK
LVAYRLPKDS ETPSLVLFLH ERKEESCHLG RLSLEWKIFG TPLVGRLSDL TNGSDIRKLF
LKLLDPFLMP VGDDSDFSDE AGKIDNGDSI VEDVTSSRVS DNDAVSDSSE AGDEPHLSDD
FRFYRLDSIR PTEIKMNEPL SISDFAKPLT IHVQWPEKMI EKYDTCLLSS LMEVCKPQLF
TRMPPESVSL YKCLEAFLKE EPLGPEDMYC PRCKKHWQAS KKLDLWRSPD ILVIHLKRFS
FSRYFKSKLD TYVDFPIDDL DLSNYVCCKN SQLSNRYVLY AISNHYGGMG GGHYTAFVDI
DYHSAFKQYE YLKTQITSVQ LGHKRWFEFD DDRVYPVSED NIKTSAAYVL FYKRVSDVK
//