ID   SUMO3_ARATH             Reviewed;         111 AA.
AC   Q9FLP5;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Small ubiquitin-related modifier 3;
DE            Short=AtSUMO3;
GN   Name=SUMO3; Synonyms=SUM3; OrderedLocusNames=At5g55170; ORFNames=MCO15.12;
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].
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA   Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT   features of the regions of 1,456,315 bp covered by nineteen physically
RT   assigned P1 and TAC clones.";
RL   DNA Res. 5:41-54(1998).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT   "Arabidopsis ORF clones.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with SAE2, SCE1, SIZ1 and MMS21 Covalently attached
CC       to a number of proteins. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q9FLP5; O81313: IND; NbExp=3; IntAct=EBI-25512645, EBI-4446992;
CC       Q9FLP5; Q9LQF0: TCP23; NbExp=3; IntAct=EBI-25512645, EBI-15192297;
CC       Q9FLP5; Q5CCK4: VAL2; NbExp=3; IntAct=EBI-25512645, EBI-15193683;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
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}.
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DR   EMBL; AB010071; BAB08586.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED96595.1; -; Genomic_DNA.
DR   EMBL; AF510521; AAN03847.1; -; mRNA.
DR   EMBL; BT024755; ABD59093.1; -; mRNA.
DR   RefSeq; NP_200328.1; NM_124899.4.
DR   AlphaFoldDB; Q9FLP5; -.
DR   SMR; Q9FLP5; -.
DR   BioGRID; 20854; 129.
DR   IntAct; Q9FLP5; 3.
DR   STRING; 3702.AT5G55170.1; -.
DR   PaxDb; Q9FLP5; -.
DR   EnsemblPlants; AT5G55170.1; AT5G55170.1; AT5G55170.
DR   GeneID; 835610; -.
DR   Gramene; AT5G55170.1; AT5G55170.1; AT5G55170.
DR   KEGG; ath:AT5G55170; -.
DR   Araport; AT5G55170; -.
DR   TAIR; locus:2161695; AT5G55170.
DR   eggNOG; KOG1769; Eukaryota.
DR   HOGENOM; CLU_148322_4_0_1; -.
DR   InParanoid; Q9FLP5; -.
DR   OMA; GDEIDAC; -.
DR   OrthoDB; 1583700at2759; -.
DR   PhylomeDB; Q9FLP5; -.
DR   PRO; PR:Q9FLP5; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FLP5; baseline and differential.
DR   Genevisible; Q9FLP5; AT.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0016925; P:protein sumoylation; IDA: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   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..111
FT                   /note="Small ubiquitin-related modifier 3"
FT                   /id="PRO_0000397034"
FT   DOMAIN          16..93
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
SQ   SEQUENCE   111 AA;  12580 MW;  79544A00709B67EC CRC64;
     MSNPQDDKPI DQEQEAHVIL KVKSQDGDEV LFKNKKSAPL KKLMYVYCDR RGLKLDAFAF
     IFNGARIGGL ETPDELDMED GDVIDACRAM SGGLRANQRQ WSYMLFDHNG L