UBP25_ARATH
ID UBP25_ARATH Reviewed; 661 AA.
AC Q9FPS2; Q8VZF5; Q9LUK9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 25;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 25;
DE Short=AtUBP25;
DE AltName: Full=Ubiquitin thioesterase 25;
DE AltName: Full=Ubiquitin-specific-processing protease 25;
GN Name=UBP25; OrderedLocusNames=At3g14400; ORFNames=MLN21.18;
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).
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=BAB01045.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AF302673; AAG42763.1; -; mRNA.
DR EMBL; AB022220; BAB01045.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE75513.1; -; Genomic_DNA.
DR EMBL; AY064992; AAL57643.1; -; mRNA.
DR EMBL; BT021128; AAX22263.1; -; mRNA.
DR RefSeq; NP_566486.1; NM_112299.4.
DR AlphaFoldDB; Q9FPS2; -.
DR SMR; Q9FPS2; -.
DR BioGRID; 5996; 1.
DR IntAct; Q9FPS2; 1.
DR STRING; 3702.AT3G14400.1; -.
DR MEROPS; C19.A13; -.
DR iPTMnet; Q9FPS2; -.
DR PaxDb; Q9FPS2; -.
DR PRIDE; Q9FPS2; -.
DR ProteomicsDB; 234093; -.
DR EnsemblPlants; AT3G14400.1; AT3G14400.1; AT3G14400.
DR GeneID; 820662; -.
DR Gramene; AT3G14400.1; AT3G14400.1; AT3G14400.
DR KEGG; ath:AT3G14400; -.
DR Araport; AT3G14400; -.
DR TAIR; locus:2090985; AT3G14400.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_029502_0_0_1; -.
DR InParanoid; Q9FPS2; -.
DR OMA; PQKFIGP; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9FPS2; -.
DR PRO; PR:Q9FPS2; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9FPS2; baseline and differential.
DR Genevisible; Q9FPS2; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 Gene3D; 1.10.246.140; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR038212; TF_EnY2_sf.
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..661
FT /note="Ubiquitin carboxyl-terminal hydrolase 25"
FT /id="PRO_0000313051"
FT DOMAIN 24..335
FT /note="USP"
FT REGION 387..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 458..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 33
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 294
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT CONFLICT 114
FT /note="Q -> E (in Ref. 4; AAL57643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 661 AA; 73293 MW; D47DEAD85E8D9B8E CRC64;
MGFKLQMSWM PSLLSQKRRN GPPLGLRNLG NTCYLNSVLQ CLTFTPPLAN FCLTHKHSSH
CDTYVDGERK RDCPFCIVEK RIARSLSVDL TTDAPNKISS CLKIFAEHFK LGRQEDAHEF
LRYVIDACHN TSLRLKKLRY NGNEPFNGNS VVKEIFGGAL QSQVKCLSCG AESNKADEIM
DISLEILQSS SVKESLQKFF QSEILDGNNK YRCESCEKLV TARKQMSILQ APNILVIQLK
RFGGIFGGKI DKAISFGEIL VLSNFMSKAS KDPQPEYKLF GIIVHSGFSP ESGHYYAYVK
DSLGRWYCCN DSFVSLSTLQ EVLSEKAYIL FFSRSNQRPA SAKTLVTSNG TTSHEVNGCE
TSNPQKFIGP LNGFNMKPQA EQSFQKGNLA SSKPHKFIRP KPRAEQAPLE DNLLSSKVEK
APLRPHAKVS ISVNLGAKRV SPVNGRLSFH QDENIAPKAN KENSVSVLPT KVNSGTERKF
GTENGGNGVK ENGSAPGSSN HKVALHPHER SNGSSNGGDH HKDNLHPCGS NGSQNGTAHP
ETERNGVSTT QSKGLCSSTK EDPCILLRKD ESSRNELEAI KESLKKDALS HLRSCGWYDK
VLISMHAKKR LRTEQSGGED GSDLKRRLIE DVKSSLKSQI PEELKADLVN RIWEISKKKY
S
