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Database: UniProt
Entry: A0A2H5MZW5_CITUN
LinkDB: A0A2H5MZW5_CITUN
Original site: A0A2H5MZW5_CITUN 
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
//
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