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Ubiquitin-like-specific protease 1C (EC 3.4.22.-) (Protein OVERLY TOLERANT TO SALT 2)

 ULP1C_ARATH             Reviewed;         571 AA.
Q8RWN0; Q3EDF1; Q9XIJ4;
10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
20-JUN-2018, entry version 84.
RecName: Full=Ubiquitin-like-specific protease 1C;
EC=3.4.22.-;
AltName: Full=Protein OVERLY TOLERANT TO SALT 2;
Name=ULP1C; Synonyms=OTS2; OrderedLocusNames=At1g10570;
ORFNames=T10O24.20;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130712; DOI=10.1038/35048500;
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S.,
White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M.,
Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis
thaliana.";
Nature 408:816-820(2000).
[2]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=cv. Columbia;
PubMed=14593172; DOI=10.1126/science.1088305;
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
"Empirical analysis of transcriptional activity in the Arabidopsis
genome.";
Science 302:842-846(2003).
[4]
IDENTIFICATION, GENE FAMILY, AND NOMENCLATURE.
PubMed=12482876; DOI=10.1074/jbc.M209694200;
Kurepa J., Walker J.M., Smalle J., Gosink M.M., Davis S.J.,
Durham T.L., Sung D.Y., Vierstra R.D.;
"The small ubiquitin-like modifier (SUMO) protein modification system
in Arabidopsis. Accumulation of SUMO1 and -2 conjugates is increased
by stress.";
J. Biol. Chem. 278:6862-6872(2003).
[5]
FUNCTION.
PubMed=16740136; DOI=10.1042/BJ20060426;
Chosed R., Mukherjee S., Lois L.M., Orth K.;
"Evolution of a signalling system that incorporates both redundancy
and diversity: Arabidopsis SUMOylation.";
Biochem. J. 398:521-529(2006).
[6]
FUNCTION, MUTAGENESIS OF CYS-512, GENE FAMILY, AND NOMENCLATURE.
PubMed=16920872; DOI=10.1104/pp.106.085415;
Colby T., Matthai A., Boeckelmann A., Stuible H.P.;
"SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis.";
Plant Physiol. 142:318-332(2006).
[7]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=18849491; DOI=10.1105/tpc.108.058669;
Conti L., Price G., O'Donnell E., Schwessinger B., Dominy P.,
Sadanandom A.;
"Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and
-2 regulate salt stress responses in Arabidopsis.";
Plant Cell 20:2894-2908(2008).
-!- FUNCTION: Protease that catalyzes two essential functions in the
SUMO pathway: processing of full-length SUMOs to their mature
forms and deconjugation of SUMO from targeted proteins. Cleaves
precursors of SUM1 and SUM2, but not of SUM3 or SUM5. Able to
release SUM1 and SUM2 from conjugates, but unable to cleave SUM3.
Protease activity mainly directed at deconjugating SUM1 and SUM2
from their target proteins. Regulates salt stress responses and
flowering time. Redundant with ULP1D.
{ECO:0000269|PubMed:16740136, ECO:0000269|PubMed:16920872,
ECO:0000269|PubMed:18849491}.
-!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
{ECO:0000269|PubMed:18849491}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8RWN0-1; Sequence=Displayed;
Name=2;
IsoId=Q8RWN0-2; Sequence=VSP_039563;
Note=Derived from EST data. No experimental confirmation
available.;
-!- DOMAIN: The N-terminal regulatory domain is not required for
peptidase activity in vitro.
-!- DISRUPTION PHENOTYPE: No visible phenotype in terms of overall
growth, salt sensitivity and flowering time. Early flowering time
and salt sensitivity in ulp1d/ots1 and ulp1c/ots2 double mutants.
{ECO:0000269|PubMed:18849491}.
-!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD39580.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC007067; AAD39580.1; ALT_SEQ; Genomic_DNA.
EMBL; CP002684; AEE28595.1; -; Genomic_DNA.
EMBL; CP002684; AEE28596.1; -; Genomic_DNA.
EMBL; AY092981; AAM12980.1; -; mRNA.
EMBL; AY128798; AAM91198.1; -; mRNA.
RefSeq; NP_172527.2; NM_100932.4. [Q8RWN0-1]
RefSeq; NP_973802.1; NM_202073.4. [Q8RWN0-2]
UniGene; At.42174; -.
ProteinModelPortal; Q8RWN0; -.
SMR; Q8RWN0; -.
STRING; 3702.AT1G10570.1; -.
MEROPS; C48.A05; -.
PaxDb; Q8RWN0; -.
PRIDE; Q8RWN0; -.
EnsemblPlants; AT1G10570.1; AT1G10570.1; AT1G10570. [Q8RWN0-1]
EnsemblPlants; AT1G10570.2; AT1G10570.2; AT1G10570. [Q8RWN0-2]
GeneID; 837598; -.
Gramene; AT1G10570.1; AT1G10570.1; AT1G10570. [Q8RWN0-1]
Gramene; AT1G10570.2; AT1G10570.2; AT1G10570. [Q8RWN0-2]
KEGG; ath:AT1G10570; -.
Araport; AT1G10570; -.
TAIR; locus:2194574; AT1G10570.
eggNOG; KOG0779; Eukaryota.
eggNOG; COG5160; LUCA.
HOGENOM; HOG000128552; -.
InParanoid; Q8RWN0; -.
KO; K16287; -.
OMA; TAANCHF; -.
OrthoDB; EOG09360MY6; -.
PhylomeDB; Q8RWN0; -.
PRO; PR:Q8RWN0; -.
Proteomes; UP000006548; Chromosome 1.
ExpressionAtlas; Q8RWN0; baseline and differential.
Genevisible; Q8RWN0; AT.
GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:TAIR.
GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
GO; GO:0070139; F:SUMO-specific endopeptidase activity; IDA:UniProtKB.
GO; GO:0070140; F:SUMO-specific isopeptidase activity; IDA:TAIR.
GO; GO:0016926; P:protein desumoylation; IDA:UniProtKB.
GO; GO:0009651; P:response to salt stress; IGI:TAIR.
GO; GO:0010228; P:vegetative to reproductive phase transition of meristem; IGI:TAIR.
InterPro; IPR038765; Papain_like_cys_pep_sf.
InterPro; IPR003653; Peptidase_C48_C.
Pfam; PF02902; Peptidase_C48; 1.
SUPFAM; SSF54001; SSF54001; 1.
PROSITE; PS50600; ULP_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Hydrolase; Nucleus; Protease;
Reference proteome; Thiol protease; Ubl conjugation pathway.
CHAIN 1 571 Ubiquitin-like-specific protease 1C.
/FTId=PRO_0000395970.
COMPBIAS 251 258 Poly-Asp.
ACT_SITE 426 426 {ECO:0000250}.
ACT_SITE 449 449 {ECO:0000250}.
ACT_SITE 512 512 {ECO:0000250}.
VAR_SEQ 113 113 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_039563.
MUTAGEN 512 512 C->A,S: Loss of peptidase activity.
{ECO:0000269|PubMed:16920872}.
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


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