UBP10_ARATH
ID UBP10_ARATH Reviewed; 923 AA.
AC Q9ZSB5; Q9T0B6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 10;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 10;
DE Short=AtUBP10;
DE AltName: Full=Ubiquitin thioesterase 10;
DE AltName: Full=Ubiquitin-specific-processing protease 10;
GN Name=UBP10; OrderedLocusNames=At4g10570; ORFNames=F3H7.5, T4F9.30;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
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 (By similarity).
CC {ECO:0000250}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD03433.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BT004132; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB40023.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB78180.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF118222; AAD03433.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL049523; CAB40023.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161517; CAB78180.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE82900.1; -; Genomic_DNA.
DR EMBL; BT004132; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; T04192; T04192.
DR RefSeq; NP_192795.3; NM_117125.4.
DR AlphaFoldDB; Q9ZSB5; -.
DR SMR; Q9ZSB5; -.
DR STRING; 3702.AT4G10570.1; -.
DR MEROPS; C19.A02; -.
DR PaxDb; Q9ZSB5; -.
DR PRIDE; Q9ZSB5; -.
DR ProteomicsDB; 228465; -.
DR EnsemblPlants; AT4G10570.1; AT4G10570.1; AT4G10570.
DR GeneID; 826649; -.
DR Gramene; AT4G10570.1; AT4G10570.1; AT4G10570.
DR KEGG; ath:AT4G10570; -.
DR Araport; AT4G10570; -.
DR TAIR; locus:2139202; AT4G10570.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; Q9ZSB5; -.
DR OMA; VEQKKAC; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q9ZSB5; -.
DR PRO; PR:Q9ZSB5; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9ZSB5; baseline and differential.
DR Genevisible; Q9ZSB5; AT.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 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 Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..923
FT /note="Ubiquitin carboxyl-terminal hydrolase 10"
FT /id="PRO_0000313037"
FT DOMAIN 19..134
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 304..895
FT /note="USP"
FT REGION 65..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 853
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 923 AA; 103699 MW; BF90A1E6CFB474AF CRC64;
MTIPNSDFML ENGVCDLPFT PEEEKRIVSE LTSESEDNLK QGNLYFVISK RWYTSWQEYV
ENSANECSTG ESSEAPRPGP IDNHDIIESD SDINDPQLRR LLVEGEDYVL VPKQVWKRLV
EWYSGGPPIE RKLICQGFYT RSYSVEVYPL CLMLTDGRDE SRTVIRLGKQ ASIRELYEKV
CAMTGVPQEK AHIWDYFDKR KNGLLDPLSY KSLEESSLHM DQDILVEVDG LSSSSQSAMS
STGNELALVP LEPSRSIVTI AGGPTLSNGH STTSNFSLFP RITSEDDGRD SLSILGKGEK
GGLAGLSNLG NTCFMNSALQ CLAHTPPIVE YFLQDYSDDI NRDNPLGMCG ELAIAFGDLL
KKLWSSGRNA VAPRAFKTKL ARFAPQFSGY NQHDSQELLA FLLDGLHEDL NKVKRKPYIE
LKDSDSRPDD EVAEELWNYH KARNDSVIVD VCQGQYKSTL VCPVCGKISI TFDPFMYLSV
PLPSTLTRSM TITVFYCDGS RLPMPYTVIV PKQGSIRDLI TALGTACCLA EDESLLLAEV
YDHKIFRYFE IPLDSLSAIK DDEHIVAYRL NQIPKGSRKA KLEILHGGQE RAVLDSVRGS
DVKLFGTPFV TYVNTEPLSG TDIDAVISGF LSPLHKVHAP SKIHNGSDNG HLADATVDQA
SGILSSPDTE IDNASDRELS FRIFLTDERG LNIKPLQSES SISPGTVTRV LVEWNEGEHE
RYDSSYLSDL PEVHKTSFSA KKTRQESISL FSCLEAFLAE EPLGPDDMWF CPSCKEHRQA
NKKLDLWKLP DILVFHLKRF TYSRYLKNKI DTFVNFPVHD LDLSKYVKNK NGQSYLYELY
AVSNHYGGLG GGHYTAYAKL IDDNKWYHFD DSHVSSVNES EIRNSAAYVL FYRRVRSETE
TQTAEMSTDM DYSCLNSHND KAS
