UCH2_ARATH
ID UCH2_ARATH Reviewed; 330 AA.
AC O04482; Q945M7; Q9SHY9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 2 {ECO:0000303|PubMed:17559514};
DE EC=3.4.19.12 {ECO:0000305};
GN Name=UCH2 {ECO:0000303|PubMed:17559514};
GN OrderedLocusNames=At1g65650 {ECO:0000312|Araport:AT1G65650};
GN ORFNames=F5I14.18 {ECO:0000312|EMBL:AAB60914.1};
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 FUNCTION, MUTAGENESIS OF CYS-82, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP GENE FAMILY, NOMENCLATURE, AND DISRUPTION PHENOTYPE.
RX PubMed=17559514; DOI=10.1111/j.1365-313x.2007.03154.x;
RA Yang P., Smalle J., Lee S., Yan N., Emborg T.J., Vierstra R.D.;
RT "Ubiquitin C-terminal hydrolases 1 and 2 affect shoot architecture in
RT Arabidopsis.";
RL Plant J. 51:441-457(2007).
RN [5]
RP INTERACTION WITH UCH1; DSS1(V); DSS1(I); EER5; RPN3A; RPN3B; RPN12A;
RP RPN12B; SAC3B; CML20 AND NUP1, SUBCELLULAR LOCATION, AND SUBUNIT.
RX PubMed=22951400; DOI=10.4161/psb.21899;
RA Tian G., Lu Q., Kohalmi S.E., Rothstein S.J., Cui Y.;
RT "Evidence that the Arabidopsis Ubiquitin C-terminal Hydrolases 1 and 2
RT associate with the 26S proteasome and the TREX-2 complex.";
RL Plant Signal. Behav. 7:1415-1419(2012).
CC -!- FUNCTION: Ubiquitin-protein hydrolase involved in the release of
CC ubiquitin attached via both peptide and isopeptide linkages. Able to
CC cleave 'Lys-48'-linked polyubiquitin chains. Involved in the direct or
CC indirect regulation of AUX/IAA proteins stability (PubMed:17559514).
CC Acts as a linker between the TREX-2 complex and 26S proteasome
CC (PubMed:22951400). {ECO:0000269|PubMed:17559514,
CC ECO:0000269|PubMed:22951400}.
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:0000305};
CC -!- SUBUNIT: Heterodimer (PubMed:22951400). Interacts with UCH1, EER5,
CC DSS1(V), DSS1(I), RPN3A, RPN3B, RPN12A, RPN12B, SAC3B, CML20 and NUP1
CC (PubMed:22951400). {ECO:0000269|PubMed:22951400}.
CC -!- INTERACTION:
CC O04482; Q39016: CPK11; NbExp=4; IntAct=EBI-2298606, EBI-979321;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17559514,
CC ECO:0000269|PubMed:22951400}. Cytoplasm {ECO:0000269|PubMed:17559514,
CC ECO:0000269|PubMed:22951400}.
CC -!- TISSUE SPECIFICITY: Expressed in leaves, stems, sepals, stamens,
CC petals, roots, hypocotyls and cotyledons.
CC {ECO:0000269|PubMed:17559514}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Uch1 and uch2 double
CC mutants are less fertile, accumulated less chlorophyll and have
CC slightly fewer and shorter cauline branches.
CC {ECO:0000269|PubMed:17559514}.
CC -!- MISCELLANEOUS: UCH1 and UCH2 are not integral polypeptides of the 26S
CC proteasome, unlike their S.pombe and animal orthologs
CC (PubMed:17559514). However, they interact with the 26S proteasome lid
CC complex as well as to the TREX-2 complex (PubMed:22951400).
CC {ECO:0000269|PubMed:17559514, ECO:0000269|PubMed:22951400}.
CC -!- SIMILARITY: Belongs to the peptidase C12 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF23845.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC001229; AAB60914.1; -; Genomic_DNA.
DR EMBL; AC007234; AAF23845.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE34407.1; -; Genomic_DNA.
DR EMBL; AY065083; AAL38259.1; -; mRNA.
DR EMBL; AY114549; AAM47868.1; -; mRNA.
DR EMBL; AF412059; AAL06512.1; -; mRNA.
DR RefSeq; NP_564858.1; NM_105238.3.
DR AlphaFoldDB; O04482; -.
DR SMR; O04482; -.
DR IntAct; O04482; 1.
DR STRING; 3702.AT1G65650.1; -.
DR MEROPS; C12.A02; -.
DR PaxDb; O04482; -.
DR PRIDE; O04482; -.
DR ProteomicsDB; 243220; -.
DR EnsemblPlants; AT1G65650.1; AT1G65650.1; AT1G65650.
DR GeneID; 842876; -.
DR Gramene; AT1G65650.1; AT1G65650.1; AT1G65650.
DR KEGG; ath:AT1G65650; -.
DR Araport; AT1G65650; -.
DR TAIR; locus:2018516; AT1G65650.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; O04482; -.
DR OMA; DGAGNWC; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; O04482; -.
DR PRO; PR:O04482; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04482; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0031011; C:Ino80 complex; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:TAIR.
DR GO; GO:0016579; P:protein deubiquitination; IDA:TAIR.
DR GO; GO:0010016; P:shoot system morphogenesis; IGI:TAIR.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.532.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001578; Peptidase_C12_UCH.
DR InterPro; IPR036959; Peptidase_C12_UCH_sf.
DR InterPro; IPR017390; Ubiquitinyl_hydrolase_UCH37.
DR InterPro; IPR041507; UCH_C.
DR PANTHER; PTHR10589; PTHR10589; 1.
DR Pfam; PF01088; Peptidase_C12; 1.
DR Pfam; PF18031; UCH_C; 1.
DR PIRSF; PIRSF038120; Ubiquitinyl_hydrolase_UCH37; 1.
DR PRINTS; PR00707; UBCTHYDRLASE.
DR SUPFAM; SSF54001; SSF54001; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..330
FT /note="Ubiquitin carboxyl-terminal hydrolase 2"
FT /id="PRO_0000435407"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:17559514"
FT ACT_SITE 157
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 172
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT MUTAGEN 82
FT /note="C->S: Loss of deubiquitination activity."
FT /evidence="ECO:0000269|PubMed:17559514"
FT CONFLICT 176
FT /note="E -> K (in Ref. 3; AAL06512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 37499 MW; 2720D590539B155A CRC64;
MSWCTIESDP GVFTELIQQM QVKGVQVEEL YSLDSDSLNN LRPVYGLIFL FKWQAGEKDE
RPTIQDQVSN LFFANQVINN ACATQAILAI LLNSPEVDIG PELSALKEFT KNFPSDLKGL
AINNSDSIRA AHNSFARPEP FVPEEQKAAT KDDDVYHFIS YIPVDGVLYE LDGLKEGPIS
LGPCPGDQTG IEWLQMVQPV IQERIERYSQ SEIRFNLLAV IKNRKDIYTA ELKELQRQRE
QLLQQANTCV DKSEAEAVNA LIAEVGSGIE AASDKIVMEE EKFMKWRTEN IRRKHNYIPF
LFNFLKLLAE KKQLKPLIEK AKKQKTESST
