UBP27_ARATH
ID UBP27_ARATH Reviewed; 494 AA.
AC Q9FPS0; Q3E9N3; Q9SVC0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 27;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 27;
DE Short=AtUBP27;
DE AltName: Full=Ubiquitin thioesterase 27;
DE AltName: Full=Ubiquitin-specific-processing protease 27;
GN Name=UBP27; OrderedLocusNames=At4g39370; ORFNames=F23K16.5;
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
RP (ISOFORM 1).
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., 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., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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: 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FPS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FPS0-2; Sequence=VSP_029992, VSP_029993;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB52824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80600.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302675; AAG42765.1; -; mRNA.
DR EMBL; AL078620; CAB52824.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161595; CAB80600.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE87062.1; -; Genomic_DNA.
DR EMBL; AF370208; AAK44023.1; -; mRNA.
DR EMBL; AY133770; AAM91704.1; -; mRNA.
DR PIR; B85466; B85466.
DR RefSeq; NP_568058.1; NM_120097.3. [Q9FPS0-1]
DR AlphaFoldDB; Q9FPS0; -.
DR SMR; Q9FPS0; -.
DR BioGRID; 15372; 1.
DR STRING; 3702.AT4G39370.3; -.
DR MEROPS; C19.002; -.
DR iPTMnet; Q9FPS0; -.
DR PaxDb; Q9FPS0; -.
DR PRIDE; Q9FPS0; -.
DR ProteomicsDB; 234094; -. [Q9FPS0-1]
DR EnsemblPlants; AT4G39370.1; AT4G39370.1; AT4G39370. [Q9FPS0-1]
DR GeneID; 830092; -.
DR Gramene; AT4G39370.1; AT4G39370.1; AT4G39370. [Q9FPS0-1]
DR KEGG; ath:AT4G39370; -.
DR Araport; AT4G39370; -.
DR eggNOG; KOG1868; Eukaryota.
DR HOGENOM; CLU_008279_14_0_1; -.
DR InParanoid; Q9FPS0; -.
DR OMA; CNETTTH; -.
DR PhylomeDB; Q9FPS0; -.
DR PRO; PR:Q9FPS0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9FPS0; baseline and differential.
DR Genevisible; Q9FPS0; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR GO; GO:0004197; F:cysteine-type endopeptidase 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 Pfam; PF00443; UCH; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Hydrolase; Membrane; Protease; Reference proteome;
KW Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway.
FT CHAIN 1..494
FT /note="Ubiquitin carboxyl-terminal hydrolase 27"
FT /id="PRO_0000313052"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 74..494
FT /note="USP"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT ACT_SITE 440
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT VAR_SEQ 314..361
FT /note="TEIEKLRSCGGEDQCDCKTSLHLQRMPWSNSYSHILKQLIIARFPKLL ->
FT VVNLSQLLMLLYFSFVHASRLYLTRVSWKRFQSDGNRKAQELWRRGPM (in
FT isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_029992"
FT VAR_SEQ 362..494
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_029993"
SQ SEQUENCE 494 AA; 55771 MW; B8CBDF5799FA9FA6 CRC64;
MVSRRGSETK AIVCVLTDRI RISNQWVSHL SFAGLLGVAG FVFAQQHGLF RNLNNLKLFS
GREKDSGDDS FLVPGLQNLG NNCFLNVILQ ALASCKDFRS FLQWVLEDAR GSLAGEQEEQ
LPLTFALSAL LQELGTVGSR RSVSNPRKVM VTLTDYAKNF NLTSQQDAAE ALLHLISSLQ
EEIVVCYRPS QSSNLSDILF SRNLRMLAPS EGLHGLMELK RWHKHLRGPF DGILGSTLMC
RTCSSQISLE FQFFHTLPLS PLLHHGGYNI MSGCTLEHCL KKFLNTEKVE NYFCYRCWHG
AALKYLSVIG AAETEIEKLR SCGGEDQCDC KTSLHLQRMP WSNSYSHILK QLIIARFPKL
LCIQVQRASF NMFEEFKLSG HIAFPLVLNL SLFTPSSIGV NIEERIEMSS EYQKPEASKN
HGMYRLVTVV EHFGRTGSGH YTVYRSVRVF SQEEEEEDCD EDLSWFSISD SEVCRVSESD
VLGAEASLLF YERL
