UCH1_ARATH
ID UCH1_ARATH Reviewed; 334 AA.
AC Q9FFF2;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase {ECO:0000303|PubMed:17559514};
DE EC=3.4.19.12 {ECO:0000305};
GN Name=UCH1 {ECO:0000303|PubMed:17559514};
GN OrderedLocusNames=At5g16310 {ECO:0000312|Araport:AT5G16310};
GN ORFNames=MQK4.3 {ECO:0000312|EMBL:BAC42635.1};
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=9330910; DOI=10.1093/dnares/4.3.215;
RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence
RT features of the 1.6 Mb regions covered by twenty physically assigned P1
RT clones.";
RL DNA Res. 4:215-230(1997).
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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
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 [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, NOMENCLATURE, AND
RP 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 [6]
RP INTERACTION WITH EER5.
RX PubMed=19843313; DOI=10.1111/j.1365-313x.2009.04048.x;
RA Lu Q., Tang X., Tian G., Wang F., Liu K., Nguyen V., Kohalmi S.E.,
RA Keller W.A., Tsang E.W., Harada J.J., Rothstein S.J., Cui Y.;
RT "Arabidopsis homolog of the yeast TREX-2 mRNA export complex: components
RT and anchoring nucleoporin.";
RL Plant J. 61:259-270(2010).
RN [7]
RP INTERACTION WITH UCH2; 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 (Probable). Acts as a
CC linker between the TREX-2 complex and 26S proteasome (PubMed:22951400).
CC {ECO:0000269|PubMed:22951400, ECO:0000303|PubMed:17559514}.
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 EER5
CC (PubMed:19843313, PubMed:22951400). Interacts with UCH2, DSS1(V),
CC DSS1(I), RPN3A, RPN3B, RPN12A, RPN12B, SAC3B, CML20 and NUP1
CC (PubMed:22951400). {ECO:0000269|PubMed:19843313,
CC ECO:0000269|PubMed:22951400}.
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}.
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DR EMBL; AB005242; BAB09598.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92278.1; -; Genomic_DNA.
DR EMBL; AK118002; BAC42635.1; -; mRNA.
DR EMBL; BT005312; AAO63376.1; -; mRNA.
DR RefSeq; NP_197135.1; NM_121636.3.
DR AlphaFoldDB; Q9FFF2; -.
DR SMR; Q9FFF2; -.
DR IntAct; Q9FFF2; 3.
DR STRING; 3702.AT5G16310.1; -.
DR MEROPS; C12.A01; -.
DR PaxDb; Q9FFF2; -.
DR PRIDE; Q9FFF2; -.
DR ProteomicsDB; 243219; -.
DR EnsemblPlants; AT5G16310.1; AT5G16310.1; AT5G16310.
DR GeneID; 831492; -.
DR Gramene; AT5G16310.1; AT5G16310.1; AT5G16310.
DR KEGG; ath:AT5G16310; -.
DR Araport; AT5G16310; -.
DR TAIR; locus:2171312; AT5G16310.
DR eggNOG; KOG2778; Eukaryota.
DR HOGENOM; CLU_018316_0_1_1; -.
DR InParanoid; Q9FFF2; -.
DR OMA; DFGARKM; -.
DR OrthoDB; 1363547at2759; -.
DR PhylomeDB; Q9FFF2; -.
DR PRO; PR:Q9FFF2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FFF2; 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; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
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..334
FT /note="Ubiquitin carboxyl-terminal hydrolase"
FT /id="PRO_0000435406"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT ACT_SITE 163
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P09936"
FT SITE 178
FT /note="Important for enzyme activity"
FT /evidence="ECO:0000250|UniProtKB:P09936"
SQ SEQUENCE 334 AA; 38539 MW; E47D938864E44BED CRC64;
MSWLPVESDP GIFTEIIQQM QVKGVQVEEL YSLDFNSLDE IRPVYGLILL YKWRPEEKEN
RVVITEPNPN FFFASQIINN ACATQAILSV LMNSSSIDIG SELSELKQFA KEFPPELKGL
AINNNEAIRA AHNTFARPDP SSIMEDEELA AAKNLDEDDD VYHYISYLPV DGILYELDGL
KEGPISLGQC LGEPEGIEWL RMVQPVVQEQ IDRYSQNEIR FSLLAVVKNR KEMYVAELKE
YQRKRERVLQ QLGALQADKY AEKSSYEALD RELSEVNIGI ETVSQKIVME EEKSKNWKKE
NMRRKHNYVP FLFNFLKILA DKKKLKPLIA KHHP
