ID   SUMO6_ARATH             Reviewed;         117 AA.
AC   Q9FKC6;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Putative small ubiquitin-related modifier 6;
DE            Short=AtSUMO6;
GN   Name=SUMO6; Synonyms=SUM6; OrderedLocusNames=At5g48700; ORFNames=K24G6.3;
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=9734815; DOI=10.1093/dnares/5.3.203;
RA   Kotani H., Nakamura Y., Sato S., Asamizu E., Kaneko T., Miyajima N.,
RA   Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 5. VI. Sequence
RT   features of the regions of 1,367,185 bp covered by 19 physically assigned
RT   P1 and TAC clones.";
RL   DNA Res. 5:203-216(1998).
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).
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   -!- 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; AB012242; BAB09423.1; -; Genomic_DNA.
DR   EMBL; CP002688; AED95713.1; -; Genomic_DNA.
DR   RefSeq; NP_199681.1; NM_124247.1.
DR   AlphaFoldDB; Q9FKC6; -.
DR   SMR; Q9FKC6; -.
DR   STRING; 3702.AT5G48700.1; -.
DR   PaxDb; Q9FKC6; -.
DR   PRIDE; Q9FKC6; -.
DR   EnsemblPlants; AT5G48700.1; AT5G48700.1; AT5G48700.
DR   GeneID; 834928; -.
DR   Gramene; AT5G48700.1; AT5G48700.1; AT5G48700.
DR   KEGG; ath:AT5G48700; -.
DR   Araport; AT5G48700; -.
DR   TAIR; locus:2156499; AT5G48700.
DR   eggNOG; KOG1769; Eukaryota.
DR   HOGENOM; CLU_148322_4_0_1; -.
DR   InParanoid; Q9FKC6; -.
DR   OrthoDB; 1583700at2759; -.
DR   PhylomeDB; Q9FKC6; -.
DR   PRO; PR:Q9FKC6; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9FKC6; baseline and differential.
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; IBA:GO_Central.
DR   GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR   GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
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..117
FT                   /note="Putative small ubiquitin-related modifier 6"
FT                   /id="PRO_0000397037"
FT   DOMAIN          31..108
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..29
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        108
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
SQ   SEQUENCE   117 AA;  13528 MW;  24B9909A77387F59 CRC64;
     MSTKSSSIHG RNEVKMEGEK RKDVESESTH VTLNVKGQDE EGVKVFRVRR KARLLKLMEY
     YAKMRGIEWN TFRFLSDDGS RIREYHTADD MELKDGDQID ALLPQESGFG PSTVFRV