OTU7_ARATH
ID OTU7_ARATH Reviewed; 375 AA.
AC F4K3M6; F4K3M5; K9M8Y4; Q8GSJ9; Q9FH96;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 2.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 7 {ECO:0000303|PubMed:24659992};
DE Short=OTU domain-containing protein 7 {ECO:0000303|PubMed:24659992};
DE EC=3.4.19.12 {ECO:0000269|PubMed:24659992};
DE AltName: Full=Deubiquitinating enzyme OTU7 {ECO:0000303|PubMed:24659992};
GN Name=OTU7 {ECO:0000303|PubMed:24659992};
GN OrderedLocusNames=At5g67170 {ECO:0000312|Araport:AT5G67170};
GN ORFNames=K21H1.13 {ECO:0000312|EMBL:BAB10951.1};
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, MUTAGENESIS OF
RP CYS-48, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, GENE FAMILY, AND
RP NOMENCLATURE.
RX PubMed=24659992; DOI=10.3389/fpls.2014.00084;
RA Radjacommare R., Usharani R., Kuo C.-H., Fu H.;
RT "Distinct phylogenetic relationships and biochemical properties of
RT Arabidopsis ovarian tumor-related deubiquitinases support their functional
RT differentiation.";
RL Front. Plant Sci. 5:84-84(2014).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC in vitro and may therefore play an important regulatory role at the
CC level of protein turnover by preventing degradation (PubMed:24659992).
CC Cysteine protease with a preference for 'Lys-63' over 'Lys-48' over
CC 'Met-1' -linked ubiquitin (UB) tetramers as substrates
CC (PubMed:24659992). Cleaves also RUB-GST fusion (PubMed:24659992).
CC {ECO:0000269|PubMed:24659992}.
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:0000269|PubMed:24659992};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:24659992};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=F4K3M6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=F4K3M6-2; Sequence=VSP_060262, VSP_060263, VSP_060264;
CC -!- SIMILARITY: Belongs to the peptidase C85 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB10951.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; JQ013452; AFS88955.1; -; mRNA.
DR EMBL; JQ013453; AFS88956.1; -; mRNA.
DR EMBL; AB020742; BAB10951.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED98309.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98310.2; -; Genomic_DNA.
DR EMBL; BT000435; AAN17412.1; -; mRNA.
DR EMBL; BT002192; AAN72203.1; -; mRNA.
DR RefSeq; NP_001318894.1; NM_001345812.1. [F4K3M6-1]
DR RefSeq; NP_201518.2; NM_126117.3. [F4K3M6-1]
DR AlphaFoldDB; F4K3M6; -.
DR SMR; F4K3M6; -.
DR STRING; 3702.AT5G67170.1; -.
DR MEROPS; C85.003; -.
DR PRIDE; F4K3M6; -.
DR ProteomicsDB; 189182; -. [F4K3M6-1]
DR EnsemblPlants; AT5G67170.1; AT5G67170.1; AT5G67170. [F4K3M6-1]
DR EnsemblPlants; AT5G67170.2; AT5G67170.2; AT5G67170. [F4K3M6-1]
DR GeneID; 836852; -.
DR Gramene; AT5G67170.1; AT5G67170.1; AT5G67170. [F4K3M6-1]
DR Gramene; AT5G67170.2; AT5G67170.2; AT5G67170. [F4K3M6-1]
DR KEGG; ath:AT5G67170; -.
DR Araport; AT5G67170; -.
DR TAIR; locus:2155588; AT5G67170.
DR eggNOG; KOG2605; Eukaryota.
DR OMA; IEYMLAE; -.
DR OrthoDB; 1448656at2759; -.
DR PhylomeDB; F4K3M6; -.
DR PRO; PR:F4K3M6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; F4K3M6; baseline and differential.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR InterPro; IPR003323; OTU_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR004027; SEC_C_motif.
DR Pfam; PF02338; OTU; 1.
DR Pfam; PF02810; SEC-C; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50802; OTU; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Nucleus; Protease; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..375
FT /note="OVARIAN TUMOR DOMAIN-containing deubiquitinating
FT enzyme 7"
FT /id="PRO_0000447757"
FT DOMAIN 37..161
FT /note="OTU"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00139"
FT DOMAIN 202..250
FT /note="UBA-like"
FT /evidence="ECO:0000250|UniProtKB:Q5T2D3"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..315
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00768"
FT COMPBIAS 1..15
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 45
FT /evidence="ECO:0000305"
FT ACT_SITE 48
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:24659992"
FT ACT_SITE 154
FT /evidence="ECO:0000250|UniProtKB:Q96G74"
FT VAR_SEQ 18
FT /note="Missing (in isoform 2)"
FT /id="VSP_060262"
FT VAR_SEQ 176..232
FT /note="ADAKVSAASKQAKATESKSKNKADKCHVNAGAIKVVMSGSCCDNTEKAEQVL
FT LQVNG -> VLLQTLALCLSVIYINCLFFCPNKFQLCGRLMLKFQQHLNKRKLQRASPK
FT IKLISVM (in isoform 2)"
FT /id="VSP_060263"
FT VAR_SEQ 233..375
FT /note="Missing (in isoform 2)"
FT /id="VSP_060264"
FT MUTAGEN 48
FT /note="C->S: Abolished cleavage activities for 'Lys-
FT 48'- and 'Lys-63'-linked ubiquitin (UB) tetramers."
FT /evidence="ECO:0000269|PubMed:24659992"
FT CONFLICT 10
FT /note="K -> R (in Ref. 4; AAN17412/AAN72203)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 375 AA; 41534 MW; 973DD17D41082EE8 CRC64;
MAKTKQQKSK PKKQPHQKQG KDCDLSQFRA QLDALGLKII QVTADGNCFF RAIADQLEGN
EDEHNKYRNM IVLYIVKNRE MFEPFIEDDV PFEDYCKTMD DDGTWAGNME LQAASLVTRS
NICIHRNMSP RWYIRNFEDT RTRMIHLSYH DGEHYNSVRS KEDACGGPAR PVVIEADAKV
SAASKQAKAT ESKSKNKADK CHVNAGAIKV VMSGSCCDNT EKAEQVLLQV NGDVDAAIEF
LIADQGMESL TENDTETASA SDTINPKHAS DSPMENTEQA REELIEEESA SGNNSETVQA
KCTTQTDDKK IPRNKTCPCG SKKKYKSCCG TATGRSSVKL LVSQTMESKK GRKNLRRGTS
NEVEANAPDV GALCI
