SUMO1_ARATH
ID SUMO1_ARATH Reviewed; 100 AA.
AC P55852; Q547B9; Q9SZ24;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 25-MAY-2022, entry version 147.
DE RecName: Full=Small ubiquitin-related modifier 1;
DE Short=AtSUMO1;
DE AltName: Full=Ubiquitin-like protein SMT3;
GN Name=SUMO1; Synonyms=SMT3, SUM1; OrderedLocusNames=At4g26840;
GN ORFNames=F10M23.180;
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], AND SUBCELLULAR LOCATION.
RX PubMed=9119407; DOI=10.1006/geno.1996.4556;
RA Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F.,
RA Brahe C.;
RT "SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to
RT chromosome 21qter and defines a novel gene family.";
RL Genomics 40:362-367(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Columbia;
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 [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION.
RX PubMed=17041025; DOI=10.1104/pp.106.088831;
RA Yoo C.Y., Miura K., Jin J.B., Lee J., Park H.C., Salt D.E., Yun D.J.,
RA Bressan R.A., Hasegawa P.M.;
RT "SIZ1 small ubiquitin-like modifier E3 ligase facilitates basal
RT thermotolerance in Arabidopsis independent of salicylic acid.";
RL Plant Physiol. 142:1548-1558(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17644626; DOI=10.1104/pp.107.102285;
RA Saracco S.A., Miller M.J., Kurepa J., Vierstra R.D.;
RT "Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and
RT SUMO2 to nuclear proteins is essential.";
RL Plant Physiol. 145:119-134(2007).
RN [9]
RP FUNCTION, INTERACTION WITH HSFA2, AND SUBCELLULAR LOCATION.
RX PubMed=20521085; DOI=10.1007/s11103-010-9652-1;
RA Cohen-Peer R., Schuster S., Meiri D., Breiman A., Avni A.;
RT "Sumoylation of Arabidopsis heat shock factor A2 (HsfA2) modifies its
RT activity during acquired thermotholerance.";
RL Plant Mol. Biol. 74:33-45(2010).
CC -!- FUNCTION: Ubiquitin-like protein which can be covalently attached to
CC target lysines as a monomer. Does not seem to be involved in protein
CC degradation and may function as an antagonist of ubiquitin in the
CC degradation process. Required for the massive protein sumoylation in
CC the nucleus induced by heat shock and controlled by SIZ1. Involved in
CC the regulation of the heat stress transcription factor HSFA2 in
CC acquired thermotolerance. {ECO:0000269|PubMed:17041025,
CC ECO:0000269|PubMed:17644626, ECO:0000269|PubMed:20521085}.
CC -!- SUBUNIT: Interacts with SAE2, SCE1, SIZ1 and MMS21 (By similarity).
CC Interacts with HSFA2. Covalently attached to ABI5, FLD, GTE3, HSFA2 and
CC ICE1. {ECO:0000250, ECO:0000269|PubMed:20521085}.
CC -!- INTERACTION:
CC P55852; Q9SJN0: ABI5; NbExp=2; IntAct=EBI-15763381, EBI-1778690;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:17644626}.
CC -!- MISCELLANEOUS: Stress conditions rapidly and substantially elevates the
CC amount of SUMO1 and SUMO2 conjugates with a concomitant reduction in
CC the amount of free SUMO proteins. The SUMO conjugation system plays an
CC important function in stress protection and/or repair.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA67923.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; X99609; CAA67923.1; ALT_SEQ; mRNA.
DR EMBL; AF510519; AAN03845.1; -; mRNA.
DR EMBL; AL035440; CAB36530.1; -; Genomic_DNA.
DR EMBL; AL161565; CAB79539.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85259.1; -; Genomic_DNA.
DR EMBL; AY072368; AAL62360.1; -; mRNA.
DR EMBL; BT008437; AAP37796.1; -; mRNA.
DR EMBL; AY086914; AAM64478.1; -; mRNA.
DR PIR; T04807; T04807.
DR RefSeq; NP_194414.1; NM_118818.4.
DR AlphaFoldDB; P55852; -.
DR SMR; P55852; -.
DR BioGRID; 14078; 145.
DR DIP; DIP-48780N; -.
DR IntAct; P55852; 1.
DR STRING; 3702.AT4G26840.1; -.
DR PaxDb; P55852; -.
DR PRIDE; P55852; -.
DR ProteomicsDB; 228433; -.
DR EnsemblPlants; AT4G26840.1; AT4G26840.1; AT4G26840.
DR GeneID; 828791; -.
DR Gramene; AT4G26840.1; AT4G26840.1; AT4G26840.
DR KEGG; ath:AT4G26840; -.
DR Araport; AT4G26840; -.
DR TAIR; locus:2116332; AT4G26840.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_4_2_1; -.
DR InParanoid; P55852; -.
DR OMA; AYCERAS; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; P55852; -.
DR PRO; PR:P55852; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; P55852; baseline and differential.
DR Genevisible; P55852; AT.
DR GO; GO:0005737; C:cytoplasm; IDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031386; F:protein tag; IDA:TAIR.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0010286; P:heat acclimation; IMP:UniProtKB.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IMP:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IDA:TAIR.
DR GO; GO:0009408; P:response to heat; IEP:TAIR.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW Ubl conjugation pathway.
FT CHAIN 1..100
FT /note="Small ubiquitin-related modifier 1"
FT /id="PRO_0000114891"
FT DOMAIN 16..93
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CROSSLNK 93
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
SQ SEQUENCE 100 AA; 10976 MW; 6F1E8721E7734A4A CRC64;
MSANQEEDKK PGDGGAHINL KVKGQDGNEV FFRIKRSTQL KKLMNAYCDR QSVDMNSIAF
LFDGRRLRAE QTPDELDMED GDEIDAMLHQ TGGSGGGATA
