UBP17_ARATH
ID UBP17_ARATH Reviewed; 731 AA.
AC Q9FKP5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 17;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 17;
DE Short=AtUBP17;
DE AltName: Full=Ubiquitin thioesterase 17;
DE AltName: Full=Ubiquitin-specific-processing protease 17;
GN Name=UBP17; OrderedLocusNames=At5g65450; ORFNames=MNA5.19;
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] (ISOFORM 2), 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9679202; DOI=10.1093/dnares/5.2.131;
RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence
RT features of the regions of 1,381,565 bp covered by twenty one physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:131-145(1998).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9FKP5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9FKP5-2; Sequence=VSP_029990, VSP_029991;
CC -!- MISCELLANEOUS: [Isoform 2]: May be due to a competing acceptor splice
CC site. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AF302667; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB011479; BAB11567.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98058.1; -; Genomic_DNA.
DR RefSeq; NP_201348.1; NM_125943.2. [Q9FKP5-1]
DR AlphaFoldDB; Q9FKP5; -.
DR SMR; Q9FKP5; -.
DR STRING; 3702.AT5G65450.1; -.
DR MEROPS; C19.A06; -.
DR PaxDb; Q9FKP5; -.
DR PRIDE; Q9FKP5; -.
DR EnsemblPlants; AT5G65450.1; AT5G65450.1; AT5G65450. [Q9FKP5-1]
DR GeneID; 836670; -.
DR Gramene; AT5G65450.1; AT5G65450.1; AT5G65450. [Q9FKP5-1]
DR KEGG; ath:AT5G65450; -.
DR Araport; AT5G65450; -.
DR TAIR; locus:2168282; AT5G65450.
DR eggNOG; KOG1865; Eukaryota.
DR HOGENOM; CLU_007397_1_0_1; -.
DR InParanoid; Q9FKP5; -.
DR OMA; PYPPAES; -.
DR PhylomeDB; Q9FKP5; -.
DR PRO; PR:Q9FKP5; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FKP5; baseline and differential.
DR Genevisible; Q9FKP5; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 Alternative splicing; Hydrolase; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..731
FT /note="Ubiquitin carboxyl-terminal hydrolase 17"
FT /id="PRO_0000313043"
FT DOMAIN 329..633
FT /note="USP"
FT ZN_FING 57..94
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 171..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 637..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 673..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 338
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT ACT_SITE 592
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT BINDING 57
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 60
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 68
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 71
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 77
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 81
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 90
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 94
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT VAR_SEQ 421..448
FT /note="CAVDTMQSVFLKEAPAAGPFAEETTLVG -> MPGVLLIQCNLFFSKRLLQL
FT VRLLKKLL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11115897"
FT /id="VSP_029990"
FT VAR_SEQ 449..731
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11115897"
FT /id="VSP_029991"
SQ SEQUENCE 731 AA; 81999 MW; D17844AC368057B5 CRC64;
MMLVFLLIRR QWRSASVRRE EVIRLIALAT EESYLAEEVR PATVDYGGDS VSDVYRCAVC
LYPTTTRCSQ CKSVRYCSSK CQILHWRRGH KEECRSPDYD EEKEEYVQSD YDAKESNVDF
PSRGTAYESS SNVSVDVACD MSTSRPSIHK VQPRSEAVDF TTSLNIKDNL YETRPLSRKK
SRNRTDKVES ASNYSKGKTD AKLRKLGNQN SRRSGDSANM SISDQFLSVG FEEEMNALKH
ERITSEPSSA SAAMSSSSTL LLPSKANSKP KVSQASSSGL KTSVQKVVQH FRPPQSSKKS
QPSSSIDEMS FSYELFVKLY CDRVELQPFG LVNLGNSCYA NAVLQCLAFT RPLISYLIRG
LHSKTCRKKS WCFVCEFEHL ILKARGGESP LSPIKILSKL QKIGKHLGPG KEEDAHEFLR
CAVDTMQSVF LKEAPAAGPF AEETTLVGLT FGGYLHSKIK CMACLHKSER PELMMDLTVE
IDGDIGSLEE ALAQFTAYEV LDGENRYFCG RCKSYQKAKK KLMILEGPNI LTVVLKRFQS
DNFGKLSKPI HFPELLDISP YMSDPNHGDH PVYSLYAVVV HLDAMSTLFS GHYVCYIKTL
DGDWFKIDDS NVFPVQLETV LLEGAYMLLY ARDSPRPVSK NGGRKSKQRR NLAAIPSRKG
NKKQRDGDNN SLLPRVDWSS GSLSSMFSSS DTTSSCSTKD SSGIENLSDY LFGGVEPVWK
WDRHNKSQTF D
