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   24-JAN-2024, entry version 137.
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.Q9SJA1; -.
DR   MEROPS; C19.A09; -.
DR   iPTMnet; Q9SJA1; -.
DR   PaxDb; 3702-AT2G24640-1; -.
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; AT2G24640; UBP19.
DR   eggNOG; KOG1865; Eukaryota.
DR   InParanoid; Q9SJA1; -.
DR   OrthoDB; 227085at2759; -.
DR   PhylomeDB; Q9SJA1; -.
DR   PRO; PR:Q9SJA1; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q9SJA1; baseline and differential.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd02661; Peptidase_C19E; 1.
DR   Gene3D; 6.10.140.2220; -; 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   InterPro; IPR002893; Znf_MYND.
DR   PANTHER; PTHR24006; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE; 1.
DR   PANTHER; PTHR24006:SF903; UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 19; 1.
DR   Pfam; PF00443; UCH; 1.
DR   Pfam; PF01753; zf-MYND; 1.
DR   SUPFAM; SSF54001; Cysteine proteinases; 1.
DR   SUPFAM; SSF144232; HIT/MYND zinc finger-like; 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.
DR   Genevisible; Q9SJA1; AT.
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
//