ULP2A_ARATH
ID ULP2A_ARATH Reviewed; 774 AA.
AC Q0WKV8; F4JJ09; O81879;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Probable ubiquitin-like-specific protease 2A;
DE EC=3.4.22.-;
GN Name=ULP2A; OrderedLocusNames=At4g33620; ORFNames=T16L1.110;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
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;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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).
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 -!- SIMILARITY: Belongs to the peptidase C48 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAF02249.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=CAA20575.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80079.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL031394; CAA20575.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161583; CAB80079.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86254.2; -; Genomic_DNA.
DR EMBL; AK230453; BAF02249.1; ALT_SEQ; mRNA.
DR PIR; T04979; T04979.
DR RefSeq; NP_001320126.1; NM_001342223.1.
DR AlphaFoldDB; Q0WKV8; -.
DR SMR; Q0WKV8; -.
DR STRING; 3702.AT4G33620.1; -.
DR PaxDb; Q0WKV8; -.
DR PRIDE; Q0WKV8; -.
DR ProteomicsDB; 245269; -.
DR EnsemblPlants; AT4G33620.1; AT4G33620.1; AT4G33620.
DR GeneID; 829502; -.
DR Gramene; AT4G33620.1; AT4G33620.1; AT4G33620.
DR KEGG; ath:AT4G33620; -.
DR Araport; AT4G33620; -.
DR eggNOG; KOG0779; Eukaryota.
DR HOGENOM; CLU_353883_0_0_1; -.
DR InParanoid; Q0WKV8; -.
DR OMA; WCLEVET; -.
DR OrthoDB; 179156at2759; -.
DR BRENDA; 3.4.22.B67; 399.
DR PRO; PR:Q0WKV8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q0WKV8; baseline and differential.
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 2: Evidence at transcript level;
KW Hydrolase; Protease; Reference proteome; Thiol protease;
KW Ubl conjugation pathway.
FT CHAIN 1..774
FT /note="Probable ubiquitin-like-specific protease 2A"
FT /id="PRO_0000395973"
FT REGION 118..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 400
FT /evidence="ECO:0000250"
FT ACT_SITE 430
FT /evidence="ECO:0000250"
FT ACT_SITE 485
FT /evidence="ECO:0000250"
SQ SEQUENCE 774 AA; 87796 MW; 47B0300090271186 CRC64;
MTLRSVQSRS KRKPIDVFDY SDEDDRVEEE SKKLLRKFDS PVTKKHHCAI DKYEFLRCFA
KDTQSESKVL QHIVIDVEVP VKEEPSRCEL SGDGNSDLID VISNGSHRRI GIDSLTSSSL
SENDEVSTGE ATNPASDPHE VDPENAQVLI IPDVIIYGDI YCTNSKLTFS RNCMNVESSS
VNATKGTFSC QWTIEDIIKI ESQWCLEVET AFVNVLLKSR KPEGVDIAKD ISGIDLLKFS
VYDPKWSKEV ETIRSLDSRY KNIWFDTITE SEEIAFSGHD LGTSLTNLAD SFEDLVYPQG
EPDAVVVRKQ DIELLKPRRF INDTIIDFYI KYLKNRISPK ERGRFHFFNC FFFRKLANLD
KGTPSTCGGR EAYQRVQKWT KNVDLFEKDY IFIPINCSFH WSLVIICHPG ELVPSHVENP
QRVPCILHLD SIKGSHKGGL INIFPSYLRE EWKARHENTT NDSSRAPNMQ SISLELPQQE
NSFDCGLFLL HYLDLFVAQA PAKFNPSLIS RSANFLTRNW FPAKEASLKR RNILELLYNL
HKGHDPSILP ANSKSEPPHC GVSNRNDQET ESENVIECCN WIKPFDGSSS TVTDISQTKT
CSPDLILSKE VSYSGGYDPP SSKLRKVFMS PIVEEVQESC EKKDHLEMDI QKSTGHEIET
LRKEGCMLYI EDSDDEEAVS VEYVSDSQDS YEVEMKVEDD DDDELIVTGE SSGIHGSREI
KSDSASIERV NKSRDSTAAS CYNDFLLVLS DDERSSDDKE NILISSNVMA KPKT
