ULP1C_ARATH
ID ULP1C_ARATH Reviewed; 571 AA.
AC Q8RWN0; Q3EDF1; Q9XIJ4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Ubiquitin-like-specific protease 1C;
DE EC=3.4.22.-;
DE AltName: Full=Protein OVERLY TOLERANT TO SALT 2;
GN Name=ULP1C; Synonyms=OTS2; OrderedLocusNames=At1g10570; ORFNames=T10O24.20;
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] (ISOFORM 1).
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=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, MUTAGENESIS OF CYS-512, 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 [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND 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 ULP1D. {ECO:0000269|PubMed:16740136, ECO:0000269|PubMed:16920872,
CC ECO:0000269|PubMed:18849491}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:18849491}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8RWN0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8RWN0-2; Sequence=VSP_039563;
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=AAD39580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007067; AAD39580.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE28595.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28596.1; -; Genomic_DNA.
DR EMBL; AY092981; AAM12980.1; -; mRNA.
DR EMBL; AY128798; AAM91198.1; -; mRNA.
DR RefSeq; NP_172527.2; NM_100932.4. [Q8RWN0-1]
DR RefSeq; NP_973802.1; NM_202073.4. [Q8RWN0-2]
DR AlphaFoldDB; Q8RWN0; -.
DR SMR; Q8RWN0; -.
DR STRING; 3702.AT1G10570.1; -.
DR MEROPS; C48.A05; -.
DR PaxDb; Q8RWN0; -.
DR PRIDE; Q8RWN0; -.
DR ProteomicsDB; 245308; -. [Q8RWN0-1]
DR EnsemblPlants; AT1G10570.1; AT1G10570.1; AT1G10570. [Q8RWN0-1]
DR EnsemblPlants; AT1G10570.2; AT1G10570.2; AT1G10570. [Q8RWN0-2]
DR GeneID; 837598; -.
DR Gramene; AT1G10570.1; AT1G10570.1; AT1G10570. [Q8RWN0-1]
DR Gramene; AT1G10570.2; AT1G10570.2; AT1G10570. [Q8RWN0-2]
DR KEGG; ath:AT1G10570; -.
DR Araport; AT1G10570; -.
DR TAIR; locus:2194574; AT1G10570.
DR eggNOG; KOG0779; Eukaryota.
DR InParanoid; Q8RWN0; -.
DR OMA; STNIHKE; -.
DR OrthoDB; 714807at2759; -.
DR PhylomeDB; Q8RWN0; -.
DR PRO; PR:Q8RWN0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q8RWN0; baseline and differential.
DR Genevisible; Q8RWN0; AT.
DR GO; GO:0005654; C:nucleoplasm; 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 Alternative splicing; Hydrolase; Nucleus; Protease; Reference proteome;
KW Thiol protease; Ubl conjugation pathway.
FT CHAIN 1..571
FT /note="Ubiquitin-like-specific protease 1C"
FT /id="PRO_0000395970"
FT REGION 221..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 426
FT /evidence="ECO:0000250"
FT ACT_SITE 449
FT /evidence="ECO:0000250"
FT ACT_SITE 512
FT /evidence="ECO:0000250"
FT VAR_SEQ 113
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_039563"
FT MUTAGEN 512
FT /note="C->A,S: Loss of peptidase activity."
FT /evidence="ECO:0000269|PubMed:16920872"
SQ SEQUENCE 571 AA; 66079 MW; 3EE2DB01C9AC2BA5 CRC64;
MKRQRAIELD RVKKTMLNID WDDALGDEEV PELEIIATDK IPPREPTLSG YEPAVSVRSL
RDNELDDHLK RQRSLLTRLG DKLADKGEKI RNRIGELEYE KQRRMFQQRT KMQDADNGCQ
ILEKPKSSDV FMRASTASKD TSGQGTSGSK DVSRSTFAAH FSDNLKMGPQ PVKLVNDKLQ
DLGRGSWISK ANRDSIIEKN NVWRSLPRLS KCKVSLKNFY SESKDPKGDR RPNEAYGKGK
PNESSPYLLV DDDDGDDDKV IGYETPRHWS LKASPLQSSS CRKKSDDKVI NLDEDEPLSP
MVVEEACELP EGLPEDIYYP SSDQSDGRDL VQVSLKDLKC LSPGEYLTSP VINFYIRYVQ
HHVFSADKTA ANCHFFNTFF YKKLTEAVSY KGNDRDAYFV KFRRWWKGFD LFCKSYIFIP
IHEDLHWSLV IICIPDKEDE SGLTIIHLDS LGLHPRNLIF NNVKRFLREE WNYLNQDAPL
DLPISAKVWR DLPNMINEAE VQVPQQKNDF DCGLFLLFFI RRFIEEAPQR LTLQDLKMIH
KKWFKPEEAS ALRIKIWNIL VDLFRKGNQT D
