ULP1D_ARATH
ID ULP1D_ARATH Reviewed; 584 AA.
AC Q2PS26; O80745;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Ubiquitin-like-specific protease 1D;
DE EC=3.4.22.-;
DE AltName: Full=Protein OVERLY TOLERANT TO SALT 1;
GN Name=ULP1D; Synonyms=OTS1; OrderedLocusNames=At1g60220; ORFNames=T13D8.11;
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 [MRNA], FUNCTION, 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 [2]
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 [3]
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 [4]
RP IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
RX PubMed=12482876; DOI=10.1074/jbc.m209694200;
RA Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J., Durham T.L.,
RA Sung D.Y., Vierstra R.D.;
RT "The small ubiquitin-like modifier (SUMO) protein modification system in
RT Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased by
RT stress.";
RL J. Biol. Chem. 278:6862-6872(2003).
RN [5]
RP FUNCTION.
RX PubMed=16740136; DOI=10.1042/bj20060426;
RA Chosed R., Mukherjee S., Lois L.M., Orth K.;
RT "Evolution of a signalling system that incorporates both redundancy and
RT diversity: Arabidopsis SUMOylation.";
RL Biochem. J. 398:521-529(2006).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF CYS-525, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=18849491; DOI=10.1105/tpc.108.058669;
RA Conti L., Price G., O'Donnell E., Schwessinger B., Dominy P.,
RA Sadanandom A.;
RT "Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2
RT regulate salt stress responses in Arabidopsis.";
RL Plant Cell 20:2894-2908(2008).
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. Cleaves precursors of
CC SUM1 and SUM2, but not of SUM3 or SUM5. Able to release SUM1 and SUM2
CC from conjugates, but unable to cleave SUM3. Protease activity mainly
CC directed at deconjugating SUM1 and SUM2 from their target proteins.
CC Regulates salt stress responses and flowering time. Redundant with
CC ULP1C. {ECO:0000269|PubMed:16740136, ECO:0000269|PubMed:16920872,
CC ECO:0000269|PubMed:18849491}.
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:18849491}.
CC -!- INDUCTION: Constitutively expressed. Proteasomally degraded upon salt
CC stress. {ECO:0000269|PubMed:18849491}.
CC -!- DOMAIN: The N-terminal regulatory domain is not required for peptidase
CC activity in vitro.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype in terms of overall growth,
CC salt sensitivity and flowering time. Early flowering time and salt
CC sensitivity in ulp1d/ots1 and ulp1c/ots2 double mutants.
CC {ECO:0000269|PubMed:18849491}.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24055.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; DQ304543; ABC02400.1; -; mRNA.
DR EMBL; AC004473; AAC24055.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE33667.1; -; Genomic_DNA.
DR PIR; T02274; T02274.
DR RefSeq; NP_176228.3; NM_104712.5.
DR AlphaFoldDB; Q2PS26; -.
DR SMR; Q2PS26; -.
DR BioGRID; 27541; 2.
DR STRING; 3702.AT1G60220.1; -.
DR MEROPS; C48.A04; -.
DR PaxDb; Q2PS26; -.
DR PRIDE; Q2PS26; -.
DR ProteomicsDB; 245309; -.
DR EnsemblPlants; AT1G60220.1; AT1G60220.1; AT1G60220.
DR GeneID; 842317; -.
DR Gramene; AT1G60220.1; AT1G60220.1; AT1G60220.
DR KEGG; ath:AT1G60220; -.
DR Araport; AT1G60220; -.
DR TAIR; locus:2195598; AT1G60220.
DR eggNOG; KOG0779; Eukaryota.
DR HOGENOM; CLU_027032_0_0_1; -.
DR InParanoid; Q2PS26; -.
DR OMA; HETPREW; -.
DR OrthoDB; 714807at2759; -.
DR PhylomeDB; Q2PS26; -.
DR PRO; PR:Q2PS26; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q2PS26; baseline and differential.
DR Genevisible; Q2PS26; AT.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:TAIR.
DR GO; GO:0070139; F:SUMO-specific endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
DR GO; GO:0009651; P:response to salt stress; IGI:TAIR.
DR GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
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 Hydrolase; Nucleus; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..584
FT /note="Ubiquitin-like-specific protease 1D"
FT /id="PRO_0000395971"
FT REGION 28..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..199
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..274
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 438
FT /evidence="ECO:0000250"
FT ACT_SITE 461
FT /evidence="ECO:0000250"
FT ACT_SITE 525
FT /evidence="ECO:0000250"
FT MUTAGEN 525
FT /note="C->S: Loss of peptidase activity."
FT /evidence="ECO:0000269|PubMed:18849491"
SQ SEQUENCE 584 AA; 67191 MW; 65E9FE09354CF48E CRC64;
MTKRKKEVID VDCSEKKDFV IDWSSAMDKE DEVPELEIVN TTKPTPPPPP TFFSDDQTDS
PKLLTDRDLD EQLERKKAIL TLGPGLPDKG EKIRLKIADL EEEKQRRVLE GSKMEVDRSS
KVVSSTSSGS DVLPQGNAVS KDTSRGNADS KDTSRQGNAD SKEVSRSTFS AVFSKPKTDS
QSKKAFGKEL EDLGCERRKH KAGRKPVTRL SNGWRLLPDV GKAEHSAKQF DSGLKESKGN
KKSKEPYGKK RPMESSTYSL IDDDDDDDDD DDNDTSGHET PREWSWEKSP SQSSRRRKKS
EDTVINVDEE EAQPSTVAEQ AAELPEGLQE DICYPTRDDP HFVQVCLKDL ECLAPREYLT
SPVMNFYMRF LQQQISSSNQ ISADCHFFNT YFYKKLSDAV TYKGNDKDAF FVRFRRWWKG
IDLFRKAYIF IPIHEDLHWS LVIVCIPDKK DESGLTILHL DSLGLHSRKS IVENVKRFLK
DEWNYLNQDD YSLDLPISEK VWKNLPRRIS EAVVQVPQQK NDFDCGPFVL FFIKRFIEEA
PQRLKRKDLG MFDKKWFRPD EASALRIKIR NTLIELFRVS DQTE
