UBP1_ARATH
ID UBP1_ARATH Reviewed; 1083 AA.
AC Q9FPT5; O48839;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 1;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 1;
DE Short=AtUBP1;
DE AltName: Full=Ubiquitin thioesterase 1;
DE AltName: Full=Ubiquitin-specific-processing protease 1;
GN Name=UBP1; OrderedLocusNames=At2g32780; ORFNames=F24L7.8;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 872-1025, GENE FAMILY ORGANIZATION,
RP NOMENCLATURE, FUNCTION, AND MUTAGENESIS OF CYS-211.
RC STRAIN=cv. Columbia;
RX PubMed=11115897; DOI=10.1104/pp.124.4.1828;
RA Yan N., Doelling J.H., Falbel T.G., Durski A.M., Vierstra R.D.;
RT "The ubiquitin-specific protease family from Arabidopsis. AtUBP1 and 2 are
RT required for the resistance to the amino acid analog canavanine.";
RL Plant Physiol. 124:1828-1843(2000).
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. Is involved in
CC resistance to the arginine analog canavanine (CAN).
CC {ECO:0000269|PubMed:11115897}.
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;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AC003974; AAC04485.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08739.1; -; Genomic_DNA.
DR EMBL; AF302658; AAG42749.1; -; mRNA.
DR PIR; T00790; T00790.
DR RefSeq; NP_565753.1; NM_128838.2.
DR AlphaFoldDB; Q9FPT5; -.
DR BioGRID; 3186; 2.
DR STRING; 3702.AT2G32780.1; -.
DR MEROPS; C19.091; -.
DR PaxDb; Q9FPT5; -.
DR PRIDE; Q9FPT5; -.
DR EnsemblPlants; AT2G32780.1; AT2G32780.1; AT2G32780.
DR GeneID; 817839; -.
DR Gramene; AT2G32780.1; AT2G32780.1; AT2G32780.
DR KEGG; ath:AT2G32780; -.
DR Araport; AT2G32780; -.
DR TAIR; locus:2046392; AT2G32780.
DR eggNOG; KOG1873; Eukaryota.
DR HOGENOM; CLU_005952_1_0_1; -.
DR InParanoid; Q9FPT5; -.
DR OMA; TETLMHD; -.
DR OrthoDB; 278083at2759; -.
DR PhylomeDB; Q9FPT5; -.
DR PRO; PR:Q9FPT5; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9FPT5; baseline and differential.
DR Genevisible; Q9FPT5; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.40.10; -; 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 InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR001607; Znf_UBP.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF02148; zf-UBP; 1.
DR SMART; SM00290; ZnF_UBP; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
DR PROSITE; PS50271; ZF_UBP; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Metal-binding; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..1083
FT /note="Ubiquitin carboxyl-terminal hydrolase 1"
FT /id="PRO_0000080692"
FT DOMAIN 202..1083
FT /note="USP"
FT ZN_FING 30..165
FT /note="UBP-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT REGION 387..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..476
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 211
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 1029
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT BINDING 32
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 34
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 56
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 59
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 95
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 98
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 103
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 119
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 139
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00502"
FT MUTAGEN 211
FT /note="C->S: Confers CAN sensitivity."
FT /evidence="ECO:0000269|PubMed:11115897"
SQ SEQUENCE 1083 AA; 120771 MW; 55B881F9971199D9 CRC64;
MRFAATVSEK QSEQSVEVTE EFAVTMTEKR SCVHFDKYVD LDKLLKIIKS YQQIKCGECN
ERVHVKRGSR WGASNRRDWY SSSDQNCARN AIWLCLECGY YVCGDVGLPT EAQSHVMGHN
RLTRHRLVIQ CKNPQLRWCF SCQSLLPFDN EENGEKKDLL LEVVKLIRER SPNTYSASFE
TEFSCSGSIY GGIEARDGYA VRGLVNLGNT CFFNSVMQNL LSLDQLREHF LKEDLSVSGP
LVSSLKELFA ESNSEASVFR NEINPRDLFF SVCSQAPQFR GYQQHDSHEL LRCLLDGLSI
EESSLRKKLG VSDSNDSSTY QKPTLIDSVF GGEISSTVSC LECGHFSKVY EPFMDLSLPV
PSMKLPPKKQ QILSQAKEVL KNGAVSKDSE VVSAKPASDH NSTVPLFPSD HKIQSRPETS
DNETDLVLLS DVSDTAPSTE AKGVNQILVG STETLMHDND RTGKTVPDKE DVRATQSNEE
TSASGISAVI DEAQVCGCPD LEQSSSSANQ GADEELALMV ADSQVLYMPY KDHLFYDDYM
VAEASSSFVS GDHEPKKDYF DFSSFLDEPE IREGPVFRPL SKSEVYEAGF KADCSDDKTV
SAGKGEASSS FISSDHEQNI DYVDFSSFFD EPEISERPFF RPLSKSEVSE AGFKADCSDD
KTVSAGKGEA SSSFVSSDHE QNIDYVDFSS FFDEPEISER PFFRPLSKSE VSEAGFMAVS
GNDKTVRAGK GETFSSFMSG DNERNIDYVE FTNRIFDDRG TSERPVFGPP SKAKVSEAGF
VAVSSDSDPA VLDESDSPVS VDRCLAQFTK HEILSEDNAW HCENCSKNLK LQRLREKRRT
KEGLSNRWVN ENGASSAFDE CRDSSLNQSC IDLENGYKAA PPITKLPNCK EEESAIDDGF
VGEENTKQAP ITSVTETPLL GGETISSQPA SDNECENWED LAVDSEEVIV KRDARKKVLI
NKAPPVLTIH LKRFSQDARG RVSKLSGHVD FQEFIDLSKY MDTRCSEEDE PVYRLAGLVE
HLGAMSRGHY VSYIRGGHKE RRDSDTKEPN SSIWYHASDS QVRPASLEEV LRSEAYILFY
ERI
