UBP7_ARATH
ID UBP7_ARATH Reviewed; 477 AA.
AC Q84WC6; F4IXI8; Q9FPT3; Q9LU31;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 7;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 7;
DE Short=AtUBP7;
DE AltName: Full=Ubiquitin thioesterase 7;
DE AltName: Full=Ubiquitin-specific-processing protease 7;
GN Name=UBP7; OrderedLocusNames=At3g21280; ORFNames=MXL8.15;
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], GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(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].
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 INTERACTION WITH CALMODULIN.
RX PubMed=15987637; DOI=10.1016/j.febslet.2005.05.080;
RA Moon B.C., Choi M.S., Kang Y.H., Kim M.C., Cheong M.S., Park C.Y.,
RA Yoo J.H., Koo S.C., Lee S.M., Lim C.O., Cho M.J., Chung W.S.;
RT "Arabidopsis ubiquitin-specific protease 6 (AtUBP6) interacts with
RT calmodulin.";
RL FEBS Lett. 579:3885-3890(2005).
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 -!- SUBUNIT: Interacts with calmodulin (CaM).
CC {ECO:0000269|PubMed:15987637}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEE76487.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB01721.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302661; AAG42752.1; -; mRNA.
DR EMBL; AB023045; BAB01721.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE76487.1; ALT_INIT; Genomic_DNA.
DR EMBL; BT003992; AAO42031.1; -; mRNA.
DR RefSeq; NP_566680.2; NM_113023.4.
DR AlphaFoldDB; Q84WC6; -.
DR SMR; Q84WC6; -.
DR BioGRID; 7014; 6.
DR STRING; 3702.AT3G21280.1; -.
DR MEROPS; C19.A05; -.
DR PaxDb; Q84WC6; -.
DR PRIDE; Q84WC6; -.
DR ProteomicsDB; 245288; -.
DR EnsemblPlants; AT3G21280.1; AT3G21280.1; AT3G21280.
DR GeneID; 821682; -.
DR Gramene; AT3G21280.1; AT3G21280.1; AT3G21280.
DR KEGG; ath:AT3G21280; -.
DR Araport; AT3G21280; -.
DR eggNOG; KOG1872; Eukaryota.
DR HOGENOM; CLU_017549_2_1_1; -.
DR InParanoid; Q84WC6; -.
DR OrthoDB; 600543at2759; -.
DR PhylomeDB; Q84WC6; -.
DR PRO; PR:Q84WC6; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q84WC6; baseline and differential.
DR Genevisible; Q84WC6; AT.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0070628; F:proteasome binding; IBA:GO_Central.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IBA:GO_Central.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR044635; UBP14-like.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR43982; PTHR43982; 1.
DR Pfam; PF00240; ubiquitin; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW Calmodulin-binding; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..477
FT /note="Ubiquitin carboxyl-terminal hydrolase 7"
FT /id="PRO_0000313034"
FT DOMAIN 2..77
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 104..473
FT /note="USP"
FT REGION 171..190
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 364..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 380..400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 425
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 209
FT /note="S -> F (in Ref. 1; AAG42752)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="P -> A (in Ref. 1; AAG42752)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 477 AA; 53516 MW; 82B469EE366B5E13 CRC64;
MLTVSVKWQK KVFESIEIDT SQPPFVFKAQ LYDLSGVPPE RQKIMVKGGL LKDDADWSTL
GLKNGQKLMM MGTADEIVKA PEKGPVFMED LPEEQQAANL GYSAGLVNLG NTCYMNSTMQ
CLISVPELKS ELSNYQSART KDVDQTSHML TVATRELFSE LDKSVKAVAP MPFWMVLQKK
YPQFAQLHNG NHMQQDAEEC WTQMLYTLSQ SLKLPSPSED PDAVKALFGL NLLNRLHCQE
SSEESSETES VFSLKCHISH EVNHLHEGLK HGLKGELEKT SPSLGRTAVY VKESLIDSLP
RYLTVQFVRF FWKRESNQKA KILRKVDYPL ELDIYDLCSE DLRKKLEAPR QKLRDIEGQK
LGLQASAKSS SKGDDVKMTD AEGSSNQSGE SSTGDQQEGA SPHMTGIYDL VSVLTHKGRS
ADSGHYVAWV KQESGKWVQY DDANTSLQRG EDIIKLSGGG DWHMAYIVMY KARLISM
