UBP11_ARATH
ID UBP11_ARATH Reviewed; 892 AA.
AC Q9MAQ3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Putative ubiquitin carboxyl-terminal hydrolase 11;
DE EC=3.4.19.12;
DE AltName: Full=Deubiquitinating enzyme 11;
DE Short=AtUBP11;
DE AltName: Full=Ubiquitin thioesterase 11;
DE AltName: Full=Ubiquitin-specific-processing protease 11;
GN Name=UBP11; OrderedLocusNames=At1g32850; ORFNames=F9L11.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 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 -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF31287.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006424; AAF31287.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE31532.1; -; Genomic_DNA.
DR PIR; C86453; C86453.
DR RefSeq; NP_174562.2; NM_103019.3.
DR AlphaFoldDB; Q9MAQ3; -.
DR SMR; Q9MAQ3; -.
DR STRING; 3702.AT1G32850.1; -.
DR MEROPS; C19.A04; -.
DR PaxDb; Q9MAQ3; -.
DR PRIDE; Q9MAQ3; -.
DR ProteomicsDB; 234127; -.
DR EnsemblPlants; AT1G32850.1; AT1G32850.1; AT1G32850.
DR GeneID; 840179; -.
DR Gramene; AT1G32850.1; AT1G32850.1; AT1G32850.
DR KEGG; ath:AT1G32850; -.
DR Araport; AT1G32850; -.
DR TAIR; locus:2037985; AT1G32850.
DR eggNOG; KOG1870; Eukaryota.
DR HOGENOM; CLU_001060_7_1_1; -.
DR InParanoid; Q9MAQ3; -.
DR OMA; QVWRKLV; -.
DR OrthoDB; 1283205at2759; -.
DR PhylomeDB; Q9MAQ3; -.
DR PRO; PR:Q9MAQ3; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9MAQ3; baseline and differential.
DR Genevisible; Q9MAQ3; AT.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016579; P:protein deubiquitination; IEA:InterPro.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.30.2230.10; -; 1.
DR InterPro; IPR035927; DUSP-like_sf.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00443; UCH; 1.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF143791; SSF143791; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 3: Inferred from homology;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..892
FT /note="Putative ubiquitin carboxyl-terminal hydrolase 11"
FT /id="PRO_0000313038"
FT DOMAIN 17..132
FT /note="DUSP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00613"
FT DOMAIN 301..880
FT /note="USP"
FT REGION 69..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 310
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT ACT_SITE 838
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
SQ SEQUENCE 892 AA; 101175 MW; 8377D6A44BD26A67 CRC64;
MTLITDSESI GVCESSYTPE EERRIVTELN NEAEADLKEG NLYFVISNRW YTRWQRFVGL
LTEEFRSGEP SEVTRPGPID NHDIIDSESD ASDPQLRMML EEGVDYTLVQ QEVWRKLVKW
YKGGPPVPRK LISQGFYTKS FSVEVYLLCL TLTDSRDEST TIIRLSKQAS IGQLYEMVCA
GKGVAKEKAR IWDYFEKKKS VLLDPSSEQS VEEAGLQFNQ DILLEVDGSA SSQFVMSLAE
NELAMVPLEP MRSDAMDIVR GGGTLSNGHS NGFKFSFFGR NTFKDDVSSR TFGKGEKRGL
GGLQNLGNTC FMNSTLQCLA HTPPIVEYFL QDYRSDINAK NPLGMRGELA IAFGELLRKL
WSSGQNTVAP RAFKTKLARF APQFSGYNQH DSQEMLAFLL DGLHEDLNKV KRKPYIEAKD
SDGRPDDEVA EEKWKYHKAR NDSVIVDVFQ GQYKSTLVCP DCGKISITFD PFMYLSLPLP
SSRTRSMTVT VFYGDGSHLP MPYTVTVPKD GSCRDLSNAL GTACCLDNDE SLLLAEVYDH
KVFKYYENPR ELLNGIKDNE HIVAYRFKQM HKGPGKVKLE ILHGEQEKSS DRGPKCFGTP
LVTYINKEPL SGTDIATSIS GLLSPLRRVH MSCVVNSGNE NGHVPDESSR SILSRDTETE
DNDRELSLSL LRDYYSFNLQ PLESDSVVNP GSVTKVLVKW NEKEHEKYDS SYLNDLPKVH
KNVLAKKTMQ EGISLFSCLE AFLAEEPLGP DDMWYCPGCK EHRQANKKLD LWKLPDILVF
HLKRFTYSRY FKNKIDTLVN FHIHDLDLSK YVKNEDGQSY LYELYAISNH YGGLGGGHYT
AYAKLMDETK WYNFDDSRVS AVNESEIKTS AAYVLFYQRV KSDSETSDMK MD
