GenomeNet

Database: UniProt
Entry: Q9SJA1
LinkDB: Q9SJA1
Original site: Q9SJA1 
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   08-MAY-2019, entry version 120.
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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   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
RT   reference 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.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., 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
RT   are 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-
CC       terminal Gly of ubiquitin. Involved in the processing of poly-
CC       ubiquitin precursors as well as that of ubiquitinated proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Thiol-dependent hydrolysis of ester, thioester, amide,
CC         peptide and isopeptide bonds formed by the C-terminal Gly of
CC         ubiquitin (a 76-residue protein attached to proteins as an
CC         intracellular targeting 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}.
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   STRING; 3702.AT2G24640.1; -.
DR   MEROPS; C19.A09; -.
DR   iPTMnet; Q9SJA1; -.
DR   PaxDb; Q9SJA1; -.
DR   PRIDE; Q9SJA1; -.
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   eggNOG; ENOG410XQ92; LUCA.
DR   HOGENOM; HOG000097839; -.
DR   InParanoid; Q9SJA1; -.
DR   KO; K11855; -.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0004843; F:thiol-dependent ubiquitin-specific protease 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   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; Complete proteome; Hydrolase; Membrane;
KW   Metal-binding; Protease; Reference proteome; Thiol protease;
KW   Transmembrane; Transmembrane helix; Ubl conjugation pathway; Zinc;
KW   Zinc-finger.
FT   CHAIN         1    672       Ubiquitin carboxyl-terminal hydrolase 19.
FT                                /FTId=PRO_0000313045.
FT   TRANSMEM     11     31       Helical. {ECO:0000255}.
FT   DOMAIN      174    480       USP.
FT   ZN_FING      64    101       MYND-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00134}.
FT   ACT_SITE    183    183       Nucleophile. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10092}.
FT   ACT_SITE    439    439       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10092}.
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
//
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