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
//