SUMO7_ARATH
ID SUMO7_ARATH Reviewed; 95 AA.
AC Q3E8A8; F4K695;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Putative small ubiquitin-related modifier 7;
DE Short=AtSUMO7;
GN Name=SUMO7; Synonyms=SUM7; OrderedLocusNames=At5g55855; ORFNames=MWJ3;
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=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(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).
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; AB018120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; ANM71062.1; -; Genomic_DNA.
DR RefSeq; NP_001332619.1; NM_001345166.1.
DR AlphaFoldDB; Q3E8A8; -.
DR SMR; Q3E8A8; -.
DR PRIDE; Q3E8A8; -.
DR EnsemblPlants; AT5G55855.2; AT5G55855.2; AT5G55855.
DR GeneID; 835680; -.
DR Gramene; AT5G55855.2; AT5G55855.2; AT5G55855.
DR KEGG; ath:AT5G55855; -.
DR Araport; AT5G55855; -.
DR TAIR; locus:504954849; AT5G55855.
DR OMA; PSHITIK; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; Q3E8A8; -.
DR PRO; PR:Q3E8A8; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q3E8A8; baseline.
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..95
FT /note="Putative small ubiquitin-related modifier 7"
FT /id="PRO_0000397038"
FT DOMAIN 13..90
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 90
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
SQ SEQUENCE 95 AA; 10920 MW; EC94B89B7AFD9353 CRC64;
MSAADKKPLI PPSHITIKIK SQDDICVYFR IKRDVELRTM MQAYSDKVGQ QMSAFRFHCD
GIRIKPNQTP NELDLEDGDE IDAFVDQIAG FSHRH