UBP19_ARATH
ID UBP19_ARATH Reviewed; 672 AA.
AC Q9SJA1; Q9C5D8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 19;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 19;
DE Short=AtUBP19;
DE AltName: Full=Ubiquitin thioesterase 19;
DE AltName: Full=Ubiquitin-specific-processing protease 19;
GN Name=UBP19; OrderedLocusNames=At2g24640; ORFNames=F25P17.6;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(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 reference
RT 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., 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).
RN [4]
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 are
RT 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-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=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q9SJA1-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
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DR EMBL; AC006954; AAD23896.2; -; Genomic_DNA.
DR EMBL; CP002685; AEC07607.1; -; Genomic_DNA.
DR EMBL; AF360315; AAK26025.1; -; mRNA.
DR EMBL; AY056366; AAL07252.1; -; mRNA.
DR PIR; B84639; B84639.
DR RefSeq; NP_565576.1; NM_128025.4. [Q9SJA1-1]
DR AlphaFoldDB; Q9SJA1; -.
DR SMR; Q9SJA1; -.
DR STRING; 3702.AT2G24640.1; -.
DR MEROPS; C19.A09; -.
DR iPTMnet; Q9SJA1; -.
DR PaxDb; Q9SJA1; -.
DR PRIDE; Q9SJA1; -.
DR ProteomicsDB; 233061; -. [Q9SJA1-1]
DR EnsemblPlants; AT2G24640.1; AT2G24640.1; AT2G24640. [Q9SJA1-1]
DR GeneID; 817000; -.
DR Gramene; AT2G24640.1; AT2G24640.1; AT2G24640. [Q9SJA1-1]
DR KEGG; ath:AT2G24640; -.
DR Araport; AT2G24640; -.
DR TAIR; locus:2046678; AT2G24640.
DR eggNOG; KOG1865; Eukaryota.
DR InParanoid; Q9SJA1; -.
DR OrthoDB; 561804at2759; -.
DR PhylomeDB; Q9SJA1; -.
DR PRO; PR:Q9SJA1; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9SJA1; baseline and differential.
DR Genevisible; Q9SJA1; 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: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; Membrane; Metal-binding; Protease;
KW Reference proteome; Thiol protease; Transmembrane; Transmembrane helix;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1..672
FT /note="Ubiquitin carboxyl-terminal hydrolase 19"
FT /id="PRO_0000313045"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 174..480
FT /note="USP"
FT ZN_FING 64..101
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 484..672
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..531
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 554..593
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 602..622
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 623..672
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 183
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT ACT_SITE 439
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 75
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 97
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 101
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
SQ SEQUENCE 672 AA; 75720 MW; 0A3B1BDA29F3FB30 CRC64;
MHEVGLFVDL NSFTQLILTL FFVSIGLLYF VKRTAAKYFE VGGGSGGFDR DHRRDFMVSD
TAECSVCGKA TTKKCSRCKS VRYCSAACQT SDWKSGHKLK CKGFRSTDSS PVRRDDIDFE
ASLFGNRSAS KKTRIALVPQ QSQSKATLKP TDVLFPYESF VRYYNWDRPI MAPCGLTNCG
NSCFANVVLQ CLSWTRPLVA YLLERGHKRE CRRNDWCFLC EFENHLDRAN YSRFPFSPMN
IISRLPNIGG NLGYGRQEDA HELMRFAIDM MQSVCLDEFG GEKVVPPRAQ ETTLIQYIFG
GLLQSQVQCT ACSNVSDQYE NMMDLTVEIH GDAVSLEECL DQFTAKEWLQ GDNLYKCDRC
DDYVKACKRL SIRCAPNILT IALKRFQGGR FGKLNKRISF PETFDLGPYM SGGGEGSDVY
KLYAVIVHLD MLNASFFGHY ICYVKDFRGN WYRIDDSEVE KVELEDVLSQ RAYMLLYSRV
QPRPSNLRSE ESQDEKKTDT LNTESNQDGS VESSGVGTND TSVSSLCNGI ISHSEDPEYE
KESSLSASVP VSEEGKEVDV KVDTVDSESN RSIDMEHDSG TDHQEEEANG KEDPTVENLA
VDSSCLDITT PSPSAATEFI PQENERSDTE SKPLEKEHSD TESNKPLEKE HLDSESKPLE
KEHSDTEMID AQ
