Reviewed, UniProtKB/Swiss-Prot P55853 (SUMO_CAEEL)

Names and origin

Protein names

Recommended name:
    Small ubiquitin-related modifier
      Short name=SUMO
Alternative name(s):
    Ubiquitin-like protein SMT3

Gene names

Name:	smo-1
Synonyms:	smt3, sumo
ORF Names:	K12C11.2

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	91 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Ubiquitin-like protein which can be covalently attached to target lysines as a monomer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex aos-1-uba-2 and linkage to the E2 enzyme ubc-9, and can be promoted by an E3 ligase such as gei-17. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9
Subunit structure	Covalently attached to a number of proteins such as tbx-2, lin-1, lin-11 and sop-2.
Post-translational modification	Cleavage of precursor form by ulp-1 is necessary for function Probable.
Sequence similarities	Belongs to the ubiquitin family. SUMO subfamily. Contains 1 ubiquitin-like domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Molecular function	Developmental protein
PTM	Isopeptide bond
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	body morphogenesis Inferred from mutant phenotype. Source: WormBase collagen and cuticulin-based cuticle development Inferred from mutant phenotype. Source: WormBase embryonic development ending in birth or egg hatching Ref.6 Ref.7 Inferred from mutant phenotype. Source: WormBase gastrulation with mouth forming first Inferred from mutant phenotype. Source: WormBase hermaphrodite genitalia development Ref.7 Inferred from mutant phenotype. Source: WormBase modification-dependent protein catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of vulval development Ref.7 Ref.8 Inferred from mutant phenotype. Source: WormBase positive regulation of growth rate Inferred from mutant phenotype. Source: WormBase
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	O62195	1	EBI-313647,EBI-315940
	P90740	1	EBI-313647,EBI-313626
atn-1	Q23158	1	EBI-313647,EBI-314014
dlc-1	Q22799	1	EBI-313647,EBI-328324
figl-1	O16299	1	EBI-313647,EBI-320880
mel-26	Q94420	1	EBI-313647,EBI-320790
sqv-4	Q19905	1	EBI-313647,EBI-320696

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 91	91	Small ubiquitin-related modifier		PRO_0000114890
	Propeptide	91	1	By similarity		PRO_0000271227
Regions
	Domain	13 – 91	79	Ubiquitin-like
Amino acid modifications
	Cross-link	90		Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P55853-1 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: 0894E99B6F7B37F5	FASTA	91	10,222
	10 20 30 40 50 60 MADDAAQAGD NAEYIKIKVV GQDSNEVHFR VKYGTSMAKL KKSYADRTGV AVNSLRFLFD 70 80 90 GRRINDDDTP KTLEMEDDDV IEVYQEQLGG F

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"SMT3A, a human homologue of the S. cerevisiae SMT3 gene, maps to chromosome 21qter and defines a novel gene family." Lapenta V., Chiurazzi P., van der Spek P.J., Pizzuti A., Hanaoka F., Brahe C. Genomics 40:362-367(1997) [PubMed: 9119407] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Identification and characterization of the SMT3 cDNA and gene from nematode Caenorhabditis elegans." Choudhury B.K., Li S.S. Biochem. Biophys. Res. Commun. 234:788-791(1997) [PubMed: 9175795] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Bristol N2.
[4]	"Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins." Jones D., Crowe E., Stevens T.A., Candido E.P.M. Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002) [PubMed: 11806825] [Abstract] Cited for: FUNCTION.
[5]	"The small ubiquitin-like modifier (SUMO) is required for gonadal and uterine-vulval morphogenesis in Caenorhabditis elegans." Broday L., Kolotuev I., Didier C., Bhoumik A., Gupta B.P., Sternberg P.W., Podbilewicz B., Ronai Z. Genes Dev. 18:2380-2391(2004) [PubMed: 15466489] [Abstract] Cited for: FUNCTION.
[6]	"SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2." Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S., Haber D.A. Nat. Genet. 36:507-511(2004) [PubMed: 15107848] [Abstract] Cited for: FUNCTION.
[7]	"Sumoylation of LIN-1 promotes transcriptional repression and inhibition of vulval cell fates." Leight E.R., Glossip D., Kornfeld K. Development 132:1047-1056(2005) [PubMed: 15689373] [Abstract] Cited for: FUNCTION.
[8]	"Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans." Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J. EMBO J. 24:2613-2623(2005) [PubMed: 15990876] [Abstract] Cited for: FUNCTION.
[9]	"The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required for ABa-derived pharyngeal muscle in C. elegans." Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G. Dev. Biol. 295:664-677(2006) [PubMed: 16701625] [Abstract] Cited for: FUNCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X99600 mRNA. Translation: CAA67914.1. U94830 Genomic DNA. Translation: AAB67608.1. AF043701 Genomic DNA. Translation: AAK18969.1.
PIR	JC5582.
RefSeq	NP_490842.1.
UniGene	Cel.18381
3D structure databases
HSSP	HSSP built from PDB template 1A5R based on UniProtKB Q93068.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:25461N.
IntAct	P55853. 18 interactions.
Genome annotation databases
Ensembl	K12C11.2. Caenorhabditis elegans. [Contig view]
GeneID	266820.
KEGG	cel:K12C11.2.
NMPDR	fig|6239.3.peg.221.
Organism-specific databases
WormBase	WBGene00004888. smo-1.
WormPep	K12C11.2. CE18056. [WorfDB]
Phylogenomic databases
OMA	P55853. DNAEYIK.
Gene expression databases
ArrayExpress	P55853.
Family and domain databases
InterPro	IPR000626. Ubiquitin. IPR019955. Ubiquitin_supergroup. [Graphical view]
Pfam	PF00240. ubiquitin. 1 hit. [Graphical view]
SMART	SM00213. UBQ. 1 hit. [Graphical view]
PROSITE	PS50053. UBIQUITIN_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	953156.

Entry information

Entry name

SUMO_CAEEL

Accession

Primary (citable) accession number: P55853

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	June 16, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project