ULP1A_ARATH
ID ULP1A_ARATH Reviewed; 502 AA.
AC Q8GYL3; Q9M908;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 2.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Ubiquitin-like-specific protease 1A;
DE EC=3.4.22.-;
GN Name=ULP1A; OrderedLocusNames=At3g06910; ORFNames=F17A9.6;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
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 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).
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, and very inefficiently of SUM3. Seems to be the only
CC ULP1 able to cleave SUM3 precursors. Cleaves SUMO peptides better than
CC SUMO-conjugated proteins. {ECO:0000269|PubMed:16740136}.
CC -!- DOMAIN: The N-terminal regulatory domain is required for peptidase
CC activity in vitro.
CC -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF26995.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC016827; AAF26995.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002686; AEE74475.1; -; Genomic_DNA.
DR EMBL; AK117529; BAC42191.1; -; mRNA.
DR RefSeq; NP_187347.2; NM_111571.3.
DR AlphaFoldDB; Q8GYL3; -.
DR SMR; Q8GYL3; -.
DR STRING; 3702.AT3G06910.1; -.
DR MEROPS; C48.A02; -.
DR iPTMnet; Q8GYL3; -.
DR PaxDb; Q8GYL3; -.
DR PRIDE; Q8GYL3; -.
DR ProteomicsDB; 245306; -.
DR EnsemblPlants; AT3G06910.1; AT3G06910.1; AT3G06910.
DR GeneID; 819876; -.
DR Gramene; AT3G06910.1; AT3G06910.1; AT3G06910.
DR KEGG; ath:AT3G06910; -.
DR Araport; AT3G06910; -.
DR TAIR; locus:2077632; AT3G06910.
DR eggNOG; KOG0778; Eukaryota.
DR HOGENOM; CLU_024324_6_2_1; -.
DR InParanoid; Q8GYL3; -.
DR OMA; TEEHMAY; -.
DR OrthoDB; 1480705at2759; -.
DR BRENDA; 3.4.22.68; 399.
DR PRO; PR:Q8GYL3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q8GYL3; baseline and differential.
DR Genevisible; Q8GYL3; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0016929; F:deSUMOylase activity; IDA:TAIR.
DR GO; GO:0016926; P:protein desumoylation; IDA: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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..502
FT /note="Ubiquitin-like-specific protease 1A"
FT /id="PRO_0000395968"
FT ACT_SITE 393
FT /evidence="ECO:0000250"
FT ACT_SITE 410
FT /evidence="ECO:0000250"
FT ACT_SITE 461
FT /evidence="ECO:0000250"
FT CONFLICT 349
FT /note="F -> I (in Ref. 3; BAC42191)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 58169 MW; 07B2C74277EA77FC CRC64;
MKNQSRVLNS ELGDFDLSVL WDQILNFEGY GSYCFRPMDM DGYHKRSAGL NPCKHSGFSH
SSRPMAPGIY RYPEVKSSLR RQVHAPVRIL NSGRDRSTRQ GSGNVLGTFL TRNNDMWKRN
ALDSSLRYRT DREVIDVDDE LGDVEMISDD TSREGVENVA MEVDEVEEKA EMGNGLFSEV
ASLKNGSLRV GECSKANSSS LVVNRPVTDV TSFEAYRKVL ESAVNRTSKL KDRGFVDFFK
ERGRALLRSL SSFWRQDEEP VEVVQREAFV PLSREEETAV RRAFSANDSN ILVTHKNSNI
DITGKILRCL KPGKWLNDEV INLYMVLLKE REAREPKKFL KCHFFNTFFF TKLVNSATGY
NYGAVRRWTS MKRLGYHLKD CDKIFIPIHM NIHWTLAVIN IKDQKFQYLD SFKGREPKIL
DALARYFVDE VRDKSEVDLD VSRWRQEFVQ DLPMQRNGFD CGMFMVKYID FYSRGLDLCF
TQEQMPYFRA RTAKEILQLK AE
