ID A0A078FPC0_BRANA Unreviewed; 899 AA.
AC A0A078FPC0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000256|RuleBase:RU366025};
DE EC=3.4.19.12 {ECO:0000256|RuleBase:RU366025};
GN Name=BnaC04g47510D {ECO:0000313|EMBL:CDY14754.1};
GN ORFNames=GSBRNA2T00084606001 {ECO:0000313|EMBL:CDY14754.1};
OS Brassica napus (Rape).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CDY14754.1, ECO:0000313|Proteomes:UP000028999};
RN [1] {ECO:0000313|EMBL:CDY14754.1, ECO:0000313|Proteomes:UP000028999}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Darmor-bzh {ECO:0000313|Proteomes:UP000028999};
RX PubMed=25146293; DOI=10.1126/science.1253435;
RA Chalhoub B., Denoeud F., Liu S., Parkin I.A., Tang H., Wang X., Chiquet J.,
RA Belcram H., Tong C., Samans B., Correa M., Da Silva C., Just J.,
RA Falentin C., Koh C.S., Le Clainche I., Bernard M., Bento P., Noel B.,
RA Labadie K., Alberti A., Charles M., Arnaud D., Guo H., Daviaud C.,
RA Alamery S., Jabbari K., Zhao M., Edger P.P., Chelaifa H., Tack D.,
RA Lassalle G., Mestiri I., Schnel N., Le Paslier M.C., Fan G., Renault V.,
RA Bayer P.E., Golicz A.A., Manoli S., Lee T.H., Thi V.H., Chalabi S., Hu Q.,
RA Fan C., Tollenaere R., Lu Y., Battail C., Shen J., Sidebottom C.H.,
RA Wang X., Canaguier A., Chauveau A., Berard A., Deniot G., Guan M., Liu Z.,
RA Sun F., Lim Y.P., Lyons E., Town C.D., Bancroft I., Wang X., Meng J.,
RA Ma J., Pires J.C., King G.J., Brunel D., Delourme R., Renard M., Aury J.M.,
RA Adams K.L., Batley J., Snowdon R.J., Tost J., Edwards D., Zhou Y., Hua W.,
RA Sharpe A.G., Paterson A.H., Guan C., Wincker P.;
RT "Plant genetics. Early allopolyploid evolution in the post-Neolithic
RT Brassica napus oilseed genome.";
RL Science 345:950-953(2014).
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|ARBA:ARBA00037450, 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}.
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DR EMBL; LK032047; CDY14754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A078FPC0; -.
DR STRING; 3708.A0A078FPC0; -.
DR PaxDb; 3708-A0A078FPC0; -.
DR EnsemblPlants; CDY14754; CDY14754; GSBRNA2T00084606001.
DR Gramene; CDY14754; CDY14754; GSBRNA2T00084606001.
DR OMA; RRKHALM; -.
DR Proteomes; UP000028999; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02674; Peptidase_C19R; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 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 PANTHER; PTHR21646; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR PANTHER; PTHR21646:SF18; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 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 Reference proteome {ECO:0000313|Proteomes:UP000028999};
KW Thiol protease {ECO:0000256|RuleBase:RU366025};
KW Ubl conjugation pathway {ECO:0000256|RuleBase:RU366025}.
FT DOMAIN 16..146
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 317..890
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
SQ SEQUENCE 899 AA; 101041 MW; 2B8739FD21A26408 CRC64;
MAEVSMGSSG SSSTDLSPEE ERVFIKEIAI AAESNSKEGD TFYLIAQRWW HEWIEYVNQD
QPCNTNDGSS LSEHCDSAGS TTLKKPSMID NSDLIYDSAL EDPSSAGEII DTLQEGRDYV
LLPQEVWNQL HSWYGGGPTL ARRVISSGLS QTELAVEVYP LRLQLLLMPK NDQSAIRISK
KETIRELHRR ACEIFDLNSD HVRIWDYYGQ QKYSLMNDLD KTLDDANLQM DQDILVEVLD
MNGAASNAHI QPLHENGLVD EDSTSVLIDP SKSSLTVAGG FSSNRNAFRS GGVEGSQSFD
STYTTGVTTR GSTAGLTGLL NLGNTCFMNS AIQCLVHTPE FASYFQDDYH QEINWQNPLG
MVGELALAFG DLLRKLWAPG RTPIAPRPFK AKLARFAPQF SGYNQHDSQE LLAFLLDGLH
EDLNRVKHKP YINSRDADGR PDEEVADEFW ANHIARNDSI IVDVCQGQYK STLVCPICNK
VSVTFDPFMY LSLPLQFNTT RAITVTVFSC DKTALPSTIT VNISKQGRCR DLMQALTNAC
SLKQSEELKL AEIRNNLIHR LFEDPLIPLS TIKDDDHLAA YKLSKSSENS ALLKLVLRRR
DQKAGERENP VQLKPYGTPL LSLASRENAL TKGKIQCIVE NLLSPFRKEE SIMSEKGKKA
KKSSSSEVIA SKLSLQLDEN NKTVKLPDNE AEAIKLPPSA AVTIYLDWTP ELSGMYDITC
LEGLPEVLKY GPATKKARSE PLSLYACLEA FLREEPLVPD EMWFCPQCNE RRQASKKLDL
WRLPEVLVIH LKRFSYSRSM KHKLETFVNF PIHDLDLTKY VANKNLSQPQ LYELYALTNH
YGGMGSGHYT AYIKLLEENR WYNFDDSHIS HINEDDVKSG AAYVLFYRRK SDDAGGNTK
//
