ULP2B_ARATH
ID ULP2B_ARATH Reviewed; 931 AA.
AC Q8L7S0; F4I132;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 3.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Probable ubiquitin-like-specific protease 2B;
DE EC=3.4.22.-;
GN Name=ULP2B; OrderedLocusNames=At1g09730; ORFNames=F21M12.12, F21M12.29;
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 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 IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=16920872; DOI=10.1104/pp.106.085415;
RA Colby T., Matthai A., Boeckelmann A., Stuible H.P.;
RT "SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis.";
RL Plant Physiol. 142:318-332(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- FUNCTION: Protease that catalyzes two essential functions in the SUMO
CC pathway: processing of full-length SUMOs to their mature forms and
CC deconjugation of SUMO from targeted proteins. {ECO:0000250}.
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=Q8L7S0-1; Sequence=Displayed;
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM91101.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=AAN46793.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AC000132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002684; AEE28486.1; -; Genomic_DNA.
DR EMBL; AY128293; AAM91101.1; ALT_SEQ; mRNA.
DR EMBL; BT001039; AAN46793.1; ALT_SEQ; mRNA.
DR RefSeq; NP_001184951.1; NM_001198022.2. [Q8L7S0-1]
DR AlphaFoldDB; Q8L7S0; -.
DR SMR; Q8L7S0; -.
DR STRING; 3702.AT1G09730.1; -.
DR MEROPS; C48.035; -.
DR iPTMnet; Q8L7S0; -.
DR PaxDb; Q8L7S0; -.
DR PRIDE; Q8L7S0; -.
DR EnsemblPlants; AT1G09730.2; AT1G09730.2; AT1G09730. [Q8L7S0-1]
DR GeneID; 837501; -.
DR Gramene; AT1G09730.2; AT1G09730.2; AT1G09730. [Q8L7S0-1]
DR KEGG; ath:AT1G09730; -.
DR Araport; AT1G09730; -.
DR eggNOG; KOG0779; Eukaryota.
DR InParanoid; Q8L7S0; -.
DR OMA; NDMMSAI; -.
DR BRENDA; 3.4.22.B67; 399.
DR PRO; PR:Q8L7S0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8L7S0; baseline and differential.
DR Genevisible; Q8L7S0; AT.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; ISS:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; ISS:UniProtKB.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR003653; Peptidase_C48_C.
DR Pfam; PF02902; Peptidase_C48; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50600; ULP_PROTEASE; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Hydrolase; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..931
FT /note="Probable ubiquitin-like-specific protease 2B"
FT /id="PRO_0000395974"
FT REGION 204..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 825..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 870..898
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..931
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 489
FT /evidence="ECO:0000250"
FT ACT_SITE 522
FT /evidence="ECO:0000250"
FT ACT_SITE 577
FT /evidence="ECO:0000250"
SQ SEQUENCE 931 AA; 106013 MW; A2D701B3AD2CE535 CRC64;
MKKNFEVFDF KEEDELAESA AGKLLEKFTN PSPCNSPVLQ RQRIQSFCNE KRVEEEEMEG
PSCAEPATAV ESDDHQCEDD STLVTEAKES RTILTFGLET TDHLEETDAE HVNQGLMLGL
KTEDLAKETD IDHDNHGLMF GLNSEDDIEE TDVDHRVESF SCQLGGNSFY AETSSYSQRQ
LNSPFSDSSS SEEQIDMMSA IDESLSDRSA LSEASDSEDD EEDWMTEHCF NDEEKIDLST
AVIMTSEYVI LKDMHCAASL VIFSCNGIKI KSFLANNEEV PFSCEFGVED IVSIQYNWYQ
NVGLIILRIR VLLKDENCHE DMEELKIAVK EHNWPNKQQK INSLHVKYPA VWNTDLEDDV
EVSGYNLNQQ KRYFPSFDEP FEDVVYPKGD PDAVSICKRD VELLQPETFV NDTIIDFYIN
YLKNQIQTEE KHRFHFFNSF FFRKLADLDK DPSSIADGKA AFLRVRKWTR KVDMFGKDYI
FVPVNYNLHW SLIVICHPGE VANRTDLDLD DSKKVPCILH MDSIKGSHAG LKNLVQTYLC
EEWKERHKET SDDISSRFMN LRFVSLELPQ QENSFDCGLF LLHYLELFLA EAPLNFSPFK
IYNASNFLYL NWFPPAEASL KRTLIQKLIF ELLENRSREV SNEQNQSCES PVAVNDDMGI
EVLSERCSPL IDCNGDMTQT QDDQGIEMTL LERSSMRHIQ AANDSGMVLR DLFDSGSNNT
GSLLEQLQQP FEDPSSFYHL SNDSSAREQV DMETGEQFMC LNAGEGNFQC ITETTSPRAS
NSFSSWNLGI PLVQKEDETD LLSETSNSSN DSIGIIEDNP IENTHEEEID ESPPRETVSL
KSATVGSNTA DHTTENEEPV STHIELVVPS SQNDRDEEKP LEHDLEIGDK TSEDVGDDCD
QKEPMEEEDE KRAAKRPRLS SPTGEAEEME K
