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 16-JUN-2009, entry version 58. DE RecName: Full=Small ubiquitin-related modifier; DE Short=SUMO; DE AltName: Full=Ubiquitin-like protein SMT3; DE Flags: Precursor; GN Name=smo-1; Synonyms=smt3, sumo; ORFNames=K12C11.2; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97237059; 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 MEDLINE=97318858; 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 MEDLINE=99069613; 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 RT investigating biology."; RL Science 282:2012-2018(1998). RN [4] RP FUNCTION. RX PubMed=11806825; 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- RT activating enzymes, and ubiquitin-like proteins."; RL Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002). RN [5] RP FUNCTION. RX PubMed=15466489; DOI=10.1101/gad.1227104; RA Broday L., Kolotuev I., Didier C., Bhoumik A., Gupta B.P., RA Sternberg P.W., 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. 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. 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 RT inhibition of 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 RT required for ABa-derived pharyngeal muscle in C. elegans."; RL Dev. Biol. 295:664-677(2006). CC -!- FUNCTION: Ubiquitin-like protein which can be covalently attached CC to target lysines as a monomer. Does not seem to be involved in CC protein degradation and may function as an antagonist of ubiquitin CC in the degradation process. Plays a role in a number of cellular CC processes such as nuclear transport, DNA replication and repair, CC mitosis and signal transduction. Covalent attachment to its CC substrates requires prior activation by the E1 complex aos-1-uba-2 CC and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 CC ligase such as gei-17. Required for embryonic development, CC fertility, vulval morphogenesis and inhibition of vulval cell CC fates. CC -!- SUBUNIT: Covalently attached to a number of proteins such as tbx- CC 2, lin-1, lin-11 and sop-2. CC -!- INTERACTION: CC O62195:-; NbExp=1; IntAct=EBI-313647, EBI-315940; CC P90740:-; NbExp=1; IntAct=EBI-313647, EBI-313626; CC Q23158:atn-1; NbExp=1; IntAct=EBI-313647, EBI-314014; CC Q22799:dlc-1; NbExp=1; IntAct=EBI-313647, EBI-328324; CC O16299:figl-1; NbExp=1; IntAct=EBI-313647, EBI-320880; CC Q94420:mel-26; NbExp=1; IntAct=EBI-313647, EBI-320790; CC Q19905:sqv-4; NbExp=1; IntAct=EBI-313647, EBI-320696; CC -!- PTM: Cleavage of precursor form by ulp-1 is necessary for function CC (Probable). CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily. CC -!- SIMILARITY: Contains 1 ubiquitin-like domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X99600; CAA67914.1; -; mRNA. DR EMBL; U94830; AAB67608.1; -; Genomic_DNA. DR EMBL; AF043701; AAK18969.1; -; Genomic_DNA. DR PIR; JC5582; JC5582. DR RefSeq; NP_490842.1; -. DR UniGene; Cel.18381; -. DR HSSP; Q93068; 1A5R. DR DIP; DIP:25461N; -. DR IntAct; P55853; 18. DR Ensembl; K12C11.2; Caenorhabditis elegans. DR GeneID; 266820; -. DR KEGG; cel:K12C11.2; -. DR NMPDR; fig|6239.3.peg.221; -. DR WormBase; WBGene00004888; smo-1. DR WormPep; K12C11.2; CE18056. DR OMA; P55853; DNAEYIK. DR NextBio; 953156; -. DR ArrayExpress; P55853; -. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0010171; P:body morphogenesis; IMP:WormBase. DR GO; GO:0040002; P:collagen and cuticulin-based cuticle develo...; IMP:WormBase. DR GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase. DR GO; GO:0001703; P:gastrulation with mouth forming first; IMP:WormBase. DR GO; GO:0040035; P:hermaphrodite genitalia development; IMP:WormBase. DR GO; GO:0019941; P:modification-dependent protein catabolic pr...; IEA:UniProtKB-KW. DR GO; GO:0040027; P:negative regulation of vulval development; IMP:WormBase. DR GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase. DR InterPro; IPR000626; Ubiquitin. DR InterPro; IPR019955; Ubiquitin_supergroup. DR Pfam; PF00240; ubiquitin; 1. DR SMART; SM00213; UBQ; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Developmental protein; Isopeptide bond; KW Ubl conjugation pathway. FT CHAIN 1 91 Small ubiquitin-related modifier. FT /FTId=PRO_0000114890. FT PROPEP 91 91 By similarity. FT /FTId=PRO_0000271227. FT DOMAIN 13 91 Ubiquitin-like. FT CROSSLNK 90 90 Glycyl lysine isopeptide (Gly-Lys) FT (interchain with K-? in acceptor FT proteins) (By similarity). SQ SEQUENCE 91 AA; 10222 MW; 0894E99B6F7B37F5 CRC64; MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV AVNSLRFLFD GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F //