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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
 
 
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