SUMO_CAEEL
ID SUMO_CAEEL Reviewed; 91 AA.
AC P55853;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Small ubiquitin-related modifier;
DE Short=SUMO;
DE AltName: Full=Ubiquitin-like protein SMT3;
DE Flags: Precursor;
GN Name=smo-1 {ECO:0000312|WormBase:K12C11.2};
GN Synonyms=smt3 {ECO:0000312|WormBase:K12C11.2},
GN sumo {ECO:0000303|PubMed:15466489};
GN ORFNames=K12C11.2 {ECO:0000312|WormBase:K12C11.2};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
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 [GENOMIC DNA / MRNA].
RX PubMed=9175795; DOI=10.1006/bbrc.1997.6709;
RA Choudhury B.K., Li S.S.;
RT "Identification and characterization of the SMT3 cDNA and gene from
RT nematode Caenorhabditis elegans.";
RL Biochem. Biophys. Res. Commun. 234:788-791(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [4]
RP FUNCTION, AND INTERACTION WITH LIN-11.
RX PubMed=11806825; DOI=10.1186/gb-2001-3-1-research0002;
RA Jones D., Crowe E., Stevens T.A., Candido E.P.M.;
RT "Functional and phylogenetic analysis of the ubiquitylation system in
RT Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating
RT enzymes, and ubiquitin-like proteins.";
RL Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002).
RN [5]
RP FUNCTION, AND INTERACTION WITH SOP-2.
RX PubMed=15466489; DOI=10.1101/gad.1227104;
RA Broday L., Kolotuev I., Didier C., Bhoumik A., Gupta B.P., Sternberg P.W.,
RA Podbilewicz B., Ronai Z.;
RT "The small ubiquitin-like modifier (SUMO) is required for gonadal and
RT uterine-vulval morphogenesis in Caenorhabditis elegans.";
RL Genes Dev. 18:2380-2391(2004).
RN [6]
RP FUNCTION, AND INTERACTION WITH LIN-1.
RX PubMed=15107848; DOI=10.1038/ng1336;
RA Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S.,
RA Haber D.A.;
RT "SUMO modification is required for in vivo Hox gene regulation by the
RT Caenorhabditis elegans Polycomb group protein SOP-2.";
RL Nat. Genet. 36:507-511(2004).
RN [7]
RP FUNCTION, AND INTERACTION WITH TBX-2.
RX PubMed=15689373; DOI=10.1242/dev.01664;
RA Leight E.R., Glossip D., Kornfeld K.;
RT "Sumoylation of LIN-1 promotes transcriptional repression and inhibition of
RT vulval cell fates.";
RL Development 132:1047-1056(2005).
RN [8]
RP FUNCTION.
RX PubMed=15990876; DOI=10.1038/sj.emboj.7600726;
RA Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.;
RT "Chromatin regulation and sumoylation in the inhibition of Ras-induced
RT vulval development in Caenorhabditis elegans.";
RL EMBO J. 24:2613-2623(2005).
RN [9]
RP FUNCTION.
RX PubMed=16701625; DOI=10.1016/j.ydbio.2006.04.001;
RA Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.;
RT "The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required
RT for ABa-derived pharyngeal muscle in C. elegans.";
RL Dev. Biol. 295:664-677(2006).
RN [10]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21408209; DOI=10.1371/journal.pgen.1002010;
RA Nelson M.D., Zhou E., Kiontke K., Fradin H., Maldonado G., Martin D.,
RA Shah K., Fitch D.H.;
RT "A bow-tie genetic architecture for morphogenesis suggested by a genome-
RT wide RNAi screen in Caenorhabditis elegans.";
RL PLoS Genet. 7:E1002010-E1002010(2011).
RN [11]
RP FUNCTION, INTERACTION WITH BET-1, AND DISRUPTION PHENOTYPE.
RX PubMed=24285704; DOI=10.1242/bio.20136007;
RA Fisher K., Gee F., Wang S., Xue F., Knapp S., Philpott M., Wells C.,
RA Rodriguez M., Snoek L.B., Kammenga J., Poulin G.B.;
RT "Maintenance of muscle myosin levels in adult C. elegans requires both the
RT double bromodomain protein BET-1 and sumoylation.";
RL Biol. Open 2:1354-1363(2013).
RN [12]
RP FUNCTION, INTERACTION WITH BET-1, AND DISRUPTION PHENOTYPE.
RX PubMed=24349540; DOI=10.1371/journal.pone.0083659;
RA Gee F., Fisher K., Klemstein U., Poulin G.B.;
RT "An RNAi-based dimorphic genetic screen identified the double bromodomain
RT protein BET-1 as a sumo-dependent attenuator of RAS-mediated signalling.";
RL PLoS ONE 8:E83659-E83659(2013).
RN [13]
RP SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25475837; DOI=10.1038/ncomms6485;
RA Pelisch F., Sonneville R., Pourkarimi E., Agostinho A., Blow J.J.,
RA Gartner A., Hay R.T.;
RT "Dynamic SUMO modification regulates mitotic chromosome assembly and cell
RT cycle progression in Caenorhabditis elegans.";
RL Nat. Commun. 5:5485-5485(2014).
RN [14]
RP DISRUPTION PHENOTYPE.
RX PubMed=25873636; DOI=10.1534/g3.115.018101;
RA Milton A.C., Okkema P.G.;
RT "Caenorhabditis elegans TBX-2 Directly Regulates Its Own Expression in a
RT Negative Autoregulatory Loop.";
RL G3 (Bethesda) 5:1177-1186(2015).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30642431; DOI=10.7554/elife.41792;
RA Gao K., Li Y., Hu S., Liu Y.;
RT "SUMO peptidase ULP-4 regulates mitochondrial UPR-mediated innate immunity
RT and lifespan extension.";
RL Elife 8:0-0(2019).
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 (PubMed:11806825). Plays a role in a number of
CC cellular processes such as nuclear transport, DNA replication and
CC repair, mitosis and signal transduction (PubMed:11806825,
CC PubMed:25475837). Covalent attachment to its substrates requires prior
CC activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme
CC ubc-9, and can be promoted by an E3 ligase such as gei-17
CC (PubMed:15107848, PubMed:16701625). Required for embryonic development,
CC fertility, vulval morphogenesis and inhibition of vulval cell fates
CC (PubMed:15466489, PubMed:15689373, PubMed:15990876, PubMed:24349540).
CC Probably by sumoylating bet-1, prevents muscle myosin depletion in
CC aging adults probably by preventing myoblast growth factor receptor
CC egl-15 overexpression (PubMed:24285704). Plays a role in the
CC attenuation of the let-60/ras pathway (PubMed:24349540,
CC PubMed:24285704). Plays a role in male tail tip morphogenesis
CC (PubMed:21408209). Plays a role in the mitochondrial stress response
CC with its covalent attachment to transcription factors dve-1 and afts-1
CC negatively regulating the mitochondrial unfolded protein response
CC (PubMed:30642431). {ECO:0000269|PubMed:11806825,
CC ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:15466489,
CC ECO:0000269|PubMed:15689373, ECO:0000269|PubMed:15990876,
CC ECO:0000269|PubMed:16701625, ECO:0000269|PubMed:21408209,
CC ECO:0000269|PubMed:24285704, ECO:0000269|PubMed:24349540,
CC ECO:0000269|PubMed:30642431}.
CC -!- SUBUNIT: Covalently attached to tbx-2 (PubMed:16701625). Covalently
CC attached to lin-1 (PubMed:15689373). Covalently attached to lin-11
CC (PubMed:15466489). Covalently attached to sop-2 (PubMed:15107848).
CC Covalently attached to bet-1 (PubMed:24349540, PubMed:24285704).
CC {ECO:0000269|PubMed:15107848, ECO:0000269|PubMed:15466489,
CC ECO:0000269|PubMed:15689373, ECO:0000269|PubMed:16701625,
CC ECO:0000269|PubMed:24285704, ECO:0000269|PubMed:24349540}.
CC -!- INTERACTION:
CC P55853; Q23158: atn-1; NbExp=3; IntAct=EBI-313647, EBI-314014;
CC P55853; Q21209: brd-1; NbExp=3; IntAct=EBI-313647, EBI-3895480;
CC P55853; P90740: fan-1; NbExp=3; IntAct=EBI-313647, EBI-313626;
CC P55853; Q94420: mel-26; NbExp=5; IntAct=EBI-313647, EBI-320790;
CC P55853; P55853: smo-1; NbExp=4; IntAct=EBI-313647, EBI-313647;
CC P55853; Q95017: ubc-9; NbExp=5; IntAct=EBI-313647, EBI-328938;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25475837}. Nucleus
CC {ECO:0000269|PubMed:25475837}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:25475837}. Chromosome
CC {ECO:0000269|PubMed:25475837}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000269|PubMed:25475837}. Note=At
CC the first embryonic mitotic division, enriched in the nucleus and
CC released to the cytoplasm when the nuclear envelope breaks down at the
CC start of mitosis. During mitosis, localizes to the metaphase plate and
CC to the centrosomal region. Also localizes to segregating chromosomes at
CC the beginning of anaphase. At late anaphase and telophase, observed in
CC the spindle midzone and in the two daughter nuclei.
CC {ECO:0000269|PubMed:25475837}.
CC -!- PTM: Cleavage of precursor form by ulp-1 is necessary for function.
CC {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown reduces survival
CC (PubMed:30642431). RNAi-mediated knockdown disrupts tail tip
CC morphogenesis resulting in retention of the pointed larval tail tip in
CC adult males (also known as the Lep phenotype) (PubMed:21408209). RNAi-
CC mediated knockdown causes chromosome misalignment and anaphase bridges
CC during the first embryonic mitotic division (PubMed:25475837). RNAi-
CC mediated knockdown results in impaired locomotion in 23% of animals
CC (PubMed:24285704). RNAi-mediated knockdown results in ectopic
CC expression of egl-17 in multiple vulva precursor cells and a moderate
CC increase in phosphorylation of mpk-1 (PubMed:24349540). RNAi-mediated
CC knockdown results in impaired activation of the mitochondrial unfolded
CC protein response following the inhibition of respiration induced by
CC antimycin A (PubMed:30642431). RNAi-mediated knockdown results in
CC ectopic tbx-2 expression in seam cells and in the syncytial hypodermis
CC (PubMed:25873636). RNAi-mediated knockdown in a bet-1 mutant background
CC results in decreased myo-3 levels in muscles and increased
CC transcription levels of egl-15, sur-1 and let-60 (PubMed:24285704).
CC {ECO:0000269|PubMed:21408209, ECO:0000269|PubMed:24285704,
CC ECO:0000269|PubMed:24349540, ECO:0000269|PubMed:25475837,
CC ECO:0000269|PubMed:25873636, ECO:0000269|PubMed:30642431}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; X99600; CAA67914.1; -; mRNA.
DR EMBL; U94830; AAB67608.1; -; Genomic_DNA.
DR EMBL; BX284601; CCD72942.1; -; Genomic_DNA.
DR PIR; JC5582; JC5582.
DR RefSeq; NP_490842.1; NM_058441.4.
DR PDB; 5XQM; NMR; -; A=1-90.
DR PDBsum; 5XQM; -.
DR AlphaFoldDB; P55853; -.
DR BMRB; P55853; -.
DR SMR; P55853; -.
DR BioGRID; 57309; 73.
DR DIP; DIP-25461N; -.
DR IntAct; P55853; 36.
DR STRING; 6239.K12C11.2; -.
DR MoonDB; P55853; Predicted.
DR iPTMnet; P55853; -.
DR EPD; P55853; -.
DR PaxDb; P55853; -.
DR PeptideAtlas; P55853; -.
DR EnsemblMetazoa; K12C11.2.1; K12C11.2.1; WBGene00004888.
DR GeneID; 266820; -.
DR KEGG; cel:CELE_K12C11.2; -.
DR UCSC; K12C11.2.1; c. elegans.
DR CTD; 266820; -.
DR WormBase; K12C11.2; CE18056; WBGene00004888; smo-1.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_4_2_1; -.
DR InParanoid; P55853; -.
DR OMA; DQMVHIN; -.
DR OrthoDB; 1583700at2759; -.
DR PhylomeDB; P55853; -.
DR Reactome; R-CEL-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-CEL-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-CEL-3065679; SUMO is proteolytically processed.
DR Reactome; R-CEL-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-CEL-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-CEL-3232118; SUMOylation of transcription factors.
DR Reactome; R-CEL-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-CEL-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-CEL-4090294; SUMOylation of intracellular receptors.
DR Reactome; R-CEL-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-CEL-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-CEL-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-CEL-8866904; Negative regulation of activity of TFAP2 (AP-2) family transcription factors.
DR Reactome; R-CEL-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR SignaLink; P55853; -.
DR PRO; PR:P55853; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00004888; Expressed in embryo and 4 other tissues.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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:0009792; P:embryo development ending in birth or egg hatching; IMP:WormBase.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:WormBase.
DR GO; GO:0051306; P:mitotic sister chromatid separation; IMP:WormBase.
DR GO; GO:0071965; P:multicellular organismal locomotion; IMP:UniProtKB.
DR GO; GO:0046716; P:muscle cell cellular homeostasis; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:WormBase.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IGI:UniProtKB.
DR GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR GO; GO:0110039; P:positive regulation of nematode male tail tip morphogenesis; IMP:UniProtKB.
DR GO; GO:0034502; P:protein localization to chromosome; IMP:WormBase.
DR GO; GO:0016925; P:protein sumoylation; IMP:WormBase.
DR GO; GO:0010468; P:regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR GO; GO:0070194; P:synaptonemal complex disassembly; IMP:WormBase.
DR CDD; cd16114; Ubl_SUMO1; 1.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR046332; SUMO1_Ubl.
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 3D-structure; Chromosome; Cytoplasm; Cytoskeleton; Developmental protein;
KW Isopeptide bond; Nucleus; Reference proteome; Ubl conjugation pathway.
FT CHAIN 1..90
FT /note="Small ubiquitin-related modifier"
FT /id="PRO_0000114890"
FT PROPEP 91
FT /evidence="ECO:0000250"
FT /id="PRO_0000271227"
FT DOMAIN 13..91
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)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:5XQM"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:5XQM"
FT HELIX 37..48
FT /evidence="ECO:0007829|PDB:5XQM"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5XQM"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:5XQM"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:5XQM"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:5XQM"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:5XQM"
SQ SEQUENCE 91 AA; 10222 MW; 0894E99B6F7B37F5 CRC64;
MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV AVNSLRFLFD
GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F
