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   24-JAN-2024, entry version 123.
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.Q9FPS0; -.
DR   MEROPS; C19.002; -.
DR   iPTMnet; Q9FPS0; -.
DR   PaxDb; 3702-AT4G39370-3; -.
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   TAIR; AT4G39370; UBP27.
DR   eggNOG; KOG1868; Eukaryota.
DR   HOGENOM; CLU_008279_14_0_1; -.
DR   InParanoid; Q9FPS0; -.
DR   OMA; CEREGND; -.
DR   PhylomeDB; Q9FPS0; -.
DR   PRO; PR:Q9FPS0; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9FPS0; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IBA:GO_Central.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02662; Peptidase_C19F; 1.
DR   Gene3D; 3.90.70.10; Cysteine proteinases; 1.
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   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF888; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   Pfam; PF00443; UCH; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   PROSITE; PS00972; USP_1; 1.
DR   PROSITE; PS50235; USP_3; 1.
DR   Genevisible; Q9FPS0; AT.
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
//