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Database: UniProt
Entry: A0A1U8JGX1_GOSHI
LinkDB: A0A1U8JGX1_GOSHI
Original site: A0A1U8JGX1_GOSHI 
ID   A0A1U8JGX1_GOSHI        Unreviewed;       924 AA.
AC   A0A1U8JGX1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE            EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN   Name=LOC107906901 {ECO:0000313|RefSeq:XP_016689540.1};
OS   Gossypium hirsutum (Upland cotton) (Gossypium mexicanum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Gossypium.
OX   NCBI_TaxID=3635 {ECO:0000313|Proteomes:UP000189702, ECO:0000313|RefSeq:XP_016689540.1};
RN   [1] {ECO:0000313|Proteomes:UP000189702}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. TM-1 {ECO:0000313|Proteomes:UP000189702};
RX   PubMed=25893780; DOI=10.1038/nbt.3208;
RA   Li F., Fan G., Lu C., Xiao G., Zou C., Kohel R.J., Ma Z., Shang H., Ma X.,
RA   Wu J., Liang X., Huang G., Percy R.G., Liu K., Yang W., Chen W., Du X.,
RA   Shi C., Yuan Y., Ye W., Liu X., Zhang X., Liu W., Wei H., Wei S., Huang G.,
RA   Zhang X., Zhu S., Zhang H., Sun F., Wang X., Liang J., Wang J., He Q.,
RA   Huang L., Wang J., Cui J., Song G., Wang K., Xu X., Yu J.Z., Zhu Y., Yu S.;
RT   "Genome sequence of cultivated Upland cotton (Gossypium hirsutum TM-1)
RT   provides insights into genome evolution.";
RL   Nat. Biotechnol. 33:524-530(2015).
RN   [2] {ECO:0000313|RefSeq:XP_016689540.1}
RP   IDENTIFICATION.
RC   TISSUE=Leaf {ECO:0000313|RefSeq:XP_016689540.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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|ARBA:ARBA00000707,
CC         ECO:0000256|RuleBase:RU366025};
CC   -!- SIMILARITY: Belongs to the peptidase C19 family.
CC       {ECO:0000256|ARBA:ARBA00009085, ECO:0000256|RuleBase:RU366025}.
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DR   RefSeq; XP_016689540.1; XM_016834051.1.
DR   AlphaFoldDB; A0A1U8JGX1; -.
DR   GeneID; 107906901; -.
DR   OrthoDB; 227085at2759; -.
DR   Proteomes; UP000189702; Chromosome 19.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF758; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 36; 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   ECO:0000313|RefSeq:XP_016689540.1};
KW   Protease {ECO:0000256|RuleBase:RU366025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000189702};
KW   Thiol protease {ECO:0000256|RuleBase:RU366025};
KW   Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT   DOMAIN          116..420
FT                   /note="USP"
FT                   /evidence="ECO:0000259|PROSITE:PS50235"
FT   REGION          630..718
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..787
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          810..848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          876..924
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        677..691
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        703..717
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        810..824
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..843
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   924 AA;  102304 MW;  B2A75BE29A2C6DC3 CRC64;
     MEATVISCSE LRIEAETEEC SDLGNFSSAS GSTSVGLSKR RIVFHPARKP LNGFNDCADE
     DFKIETLNPG RDPMRVNGVR SAQVGATGWK GDASDIWENG MDPGLSLRTT FRKIGAGLEN
     LGNTCFLNSV LQCLTYTEPL VAYLQSGKHQ NSCHIAGFCA LCAIQKHVSR ALKSTGRILA
     PNDLVSNLRC ISRNFRNSRQ EDAHEYMVNL LESMHKCCLP SGVPSESPRA YEKSLVHKIF
     GGRLRSQVKC LQCSYCSNTF DPFLDLSLEI VKADSLLKAL KNFTTAELLD GGERQYQCLR
     CKQKVRAIKQ LTVYNAPHVL TIHLKRFQAH NLGQKIDRKV EFGPTIDMKP FVSGSNEGYL
     KYTLYGVLVH RGWSTHSGHY YCFVRTSSGM WYTLDDNRVF QVSEKTVLEQ KAYMLFYVRD
     RRNTATKNSV DILQRDNVKA SVDGKSIFNQ NPGEHVQTVP IQNKLSAAVP QKDIINGGLS
     KGTIMKEVPS QQNNVQLMEE GLVLKKEAIL PSFDVPLLKD PSKASASNLI HGENLQPSAG
     SVVGNVASSK IENPTVSTGA KDSYCNESGN CKREFGVPEM VPLNCGGLLK SCTDKIVTKE
     TLQKINLASN IEVSNTVTLD DSIDKAVKTA PGEASKNVHA IRSPNKPHCD SNKIGDVSYQ
     SSRDKSLNEK GDDNSQKTIS RSPSSMPNGS LETEDPEYAP CRKSKKKHLK RKPKNMPLGL
     KSKFFMASLL MHGKKKRKRS KDKDCCSLDL GPSTCEKFST ITLGSVHGRK RTADDTTQKN
     GDNSASSLMN TVDVASKERI CENGTVLATN QHVGSSSGSV SEANRHNSRE TDSLKHHKTV
     PRWDDIGLTS PMQTAESNGM DGLEIGYVPD EWDEEYDRGK RKKIRQNKHQ FGGPNPFQQI
     ATKKTQLKKD KWDRSSSGNR PFRI
//
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