UBP8_ARATH
ID UBP8_ARATH Reviewed; 871 AA.
AC Q9C585; F4K8E0; Q0WVQ0; Q9FPT2;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 8;
DE Short=AtUBP8;
DE AltName: Full=Ubiquitin thioesterase 8;
DE AltName: Full=Ubiquitin-specific-processing protease 8;
GN Name=UBP8; OrderedLocusNames=At5g22030; ORFNames=T6G21.4;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 402-871, GENE FAMILY ORGANIZATION, AND
RP 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).
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=AED92970.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=BAE98798.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact leading to an insertion into the sequence.; Evidence={ECO:0000305};
CC Sequence=CAC34496.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL589883; CAC34496.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92970.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002688; AED92971.2; -; Genomic_DNA.
DR EMBL; AK226691; BAE98798.1; ALT_SEQ; mRNA.
DR EMBL; AF302662; AAG42753.1; -; mRNA.
DR RefSeq; NP_001318617.1; NM_001343718.1.
DR RefSeq; NP_568411.4; NM_122126.5.
DR AlphaFoldDB; Q9C585; -.
DR SMR; Q9C585; -.
DR STRING; 3702.AT5G22030.1; -.
DR MEROPS; C19.A01; -.
DR iPTMnet; Q9C585; -.
DR PRIDE; Q9C585; -.
DR ProteomicsDB; 228476; -.
DR EnsemblPlants; AT5G22030.1; AT5G22030.1; AT5G22030.
DR GeneID; 832263; -.
DR Gramene; AT5G22030.1; AT5G22030.1; AT5G22030.
DR KEGG; ath:AT5G22030; -.
DR Araport; AT5G22030; -.
DR TAIR; locus:505006627; AT5G22030.
DR eggNOG; KOG1870; Eukaryota.
DR InParanoid; Q9C585; -.
DR OMA; SGTCNEA; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q9C585; -.
DR PRO; PR:Q9C585; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9C585; baseline and differential.
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; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 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..871
FT /note="Ubiquitin carboxyl-terminal hydrolase 8"
FT /id="PRO_0000313035"
FT DOMAIN 4..99
FT /note="DUSP"
FT DOMAIN 279..869
FT /note="USP"
FT REGION 615..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..649
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 288
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 828
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 414
FT /note="N -> P (in Ref. 4; AAG42753)"
FT /evidence="ECO:0000305"
FT CONFLICT 618
FT /note="E -> K (in Ref. 3; BAE98798)"
FT /evidence="ECO:0000305"
FT CONFLICT 703
FT /note="L -> F (in Ref. 4; AAG42753)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 871 AA; 98171 MW; A669206C1AA3C5F6 CRC64;
MNGTSPDESP DSTTQRIDSF NGEQRVYFVP LRWWKDAQDS MPSESVEKRE ILYTASCGSS
YGGPMKLINN IFNSDILFDL RREGDALQNG ETGEASVSGR DFALVSSDMW LQALKWYHDD
KNTEKGVKSF SAGGVDRGDV YPVQLRLSVL QETNSLAVKI CKKDNSVECF RRACKIFSLD
SEQLRIWDIS GQTTLFFESD VSNSKDCQQQ ADQEILLELQ IYGLSDSIKL KESKKEDGST
QQTNGITNGM NGGTVFRFGR SNSLSFLGKA GEAGTLGLTG LQNLGNTCFM NSSLQCLAHT
PKLVDFFLGE YSKEINLDNP LGMKGEIALA FGDLLRSLWA PGASTVAPRT FKAKLARFAP
QFSGFNQHDS QELLAFLLDG LHEDLNRVKN KPYVEAKDGD GRPDAEVADE YWRNHVARND
SIIVDVCQGQ YKSTLVCPIC KKVSVMFDPF MYLSLPLPCT SMRTMDLTVM SADGSSLPIP
LTVNVPKFGK FEDLHKALVT ACSLPEEETL LVTEVYNNRI IRFLEEPTDS LTLIRDGDKL
VVYRLKKDAN NSPLIVYMHQ KLEEQFISGK SSPTWKAFGI PLVSRLCDVE NGSDVENLYL
KLLSSFKMPT EFFTENLENP TEEEATDKTD TDGTTSVEDT NSTDVKETTE SLPDPVLRLY
LTDDRGNSIE AEMLKEKPVN KSKRLNVLAR WPVKELDVYD TCLLSSLPEV SKSGTKRPQE
SVSLFKCLEA FLTEEPLGPD DMWYCPGCKE HRQAIKKLDL WRLPEILVIH LKRFSYSRFM
KNKLEAYVDF PLDNLDLSSY ISYKNGQTTY RYMLYAISNH YGSMGGGHYT AYVHHGGDRW
YDFDDSHVHQ ISQEKIKTSA AYVLFYKRLV D
