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Database: UniProt
Entry: Q67XW5
LinkDB: Q67XW5
Original site: Q67XW5 
ID   UBP18_ARATH             Reviewed;         631 AA.
AC   Q67XW5; O81780; Q682A0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 2.
DT   08-MAY-2019, entry version 95.
DE   RecName: Full=Ubiquitin carboxyl-terminal hydrolase 18;
DE            EC=3.4.19.12;
DE   AltName: Full=Deubiquitinating enzyme 18;
DE            Short=AtUBP18;
DE   AltName: Full=Ubiquitin thioesterase 18;
DE   AltName: Full=Ubiquitin-specific-processing protease 18;
GN   Name=UBP18; OrderedLocusNames=At4g31670; ORFNames=F28M20.140;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
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
RT   are 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-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin precursors as well as that of ubiquitinated proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting signal).; EC=3.4.19.12;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
DR   EMBL; AL031004; CAA19756.1; -; Genomic_DNA.
DR   EMBL; AL161579; CAB79885.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85943.1; -; Genomic_DNA.
DR   EMBL; AY142532; AAN13075.1; -; mRNA.
DR   EMBL; AK175467; BAD43230.1; -; mRNA.
DR   EMBL; AK176703; BAD44466.1; -; mRNA.
DR   PIR; T05103; T05103.
DR   RefSeq; NP_194895.1; NM_119316.5.
DR   SMR; Q67XW5; -.
DR   BioGrid; 14581; 1.
DR   STRING; 3702.AT4G31670.1; -.
DR   MEROPS; C19.A08; -.
DR   PaxDb; Q67XW5; -.
DR   PRIDE; Q67XW5; -.
DR   EnsemblPlants; AT4G31670.1; AT4G31670.1; AT4G31670.
DR   GeneID; 829295; -.
DR   Gramene; AT4G31670.1; AT4G31670.1; AT4G31670.
DR   KEGG; ath:AT4G31670; -.
DR   Araport; AT4G31670; -.
DR   TAIR; locus:2124809; AT4G31670.
DR   eggNOG; KOG1865; Eukaryota.
DR   eggNOG; ENOG410XQ92; LUCA.
DR   HOGENOM; HOG000097839; -.
DR   InParanoid; Q67XW5; -.
DR   KO; K11855; -.
DR   OMA; SATDHQE; -.
DR   OrthoDB; 561804at2759; -.
DR   PhylomeDB; Q67XW5; -.
DR   PRO; PR:Q67XW5; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q67XW5; baseline and differential.
DR   Genevisible; Q67XW5; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IBA:GO_Central.
DR   GO; GO:0016579; P:protein deubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
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   InterPro; IPR002893; Znf_MYND.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   PROSITE; PS01360; ZF_MYND_1; 1.
DR   PROSITE; PS50865; ZF_MYND_2; 1.
PE   2: Evidence at transcript level;
KW   Complete proteome; Hydrolase; Membrane; Metal-binding; Protease;
KW   Reference proteome; Thiol protease; Transmembrane;
KW   Transmembrane helix; Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    631       Ubiquitin carboxyl-terminal hydrolase 18.
FT                                /FTId=PRO_0000313044.
FT   TRANSMEM     10     30       Helical. {ECO:0000255}.
FT   DOMAIN      168    474       USP.
FT   ZN_FING      61     98       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   ACT_SITE    177    177       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10092}.
FT   ACT_SITE    433    433       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10092}.
FT   CONFLICT    432    432       G -> S (in Ref. 4; BAD43230).
FT                                {ECO:0000305}.
FT   CONFLICT    550    550       S -> P (in Ref. 4; BAD44466).
FT                                {ECO:0000305}.
SQ   SEQUENCE   631 AA;  70753 MW;  4C875C228588A0BE CRC64;
     MHEVGFPLDL SVFTRLIATL FFLAVGVFYF LKNTAAKYFD IGAAAAGGFD RDFMAVDAED
     CSVCGNFSTK KCSRCKSVRY CSAECQRSDW SSGHQRNCRD YGITTLTPSA KNGLRFRASP
     FGDSSASSIA LISERGQNKS SLKPREVLFP YEEFVEYFNW DNPELAPCGL MNCGNSCFAN
     VILQCLSWTR PLVAYLLEKG HKRECMRNDW CFLCEFQTHV ERASQSRFPF SPMNIISRLT
     NIGGTLGYGR QEDAHEFMRY AIDMMQSVCL DEFGGEKIVP PRSQETTLIQ YIFGGLLQSQ
     VQCTVCNHVS DQYENMMDLI VEMHGDAGSL EECLDQFTAE EWLHGDNMYK CDRCSDYVKA
     CKRLTIRRAP NILTIALKRY QGGRYGKLNK RISFPETLDL NPYMSEGGDG SDVYKLYAVI
     VHLDMLNASF FGHYICYIKD FCGNWYRIDD SEIESVELED VLSQRAYMLL YSRIQARSSS
     SCLRSEVKDE KKTDTLDTES CVKELVESSM VGAIESRSST HATIEDPVCE QSPSPSPSPS
     PSPSPSPSPS VLASECCSEV ERIDTLDSES NSSIDDSATD HQEDVANGNK DPEVKYQAAD
     SWSDPTTSTP LVCTKSKPPV RDMDTKMIDA Q
//
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