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A0A0K3AUE4 · SEA2_CAEEL

  • Protein
    Signal element on autosome protein 2
  • Gene
    sea-2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

RNA-binding protein, which regulates the expression of proteins required to control developmental timing of events during the L2 to L3 larval stage switch (PubMed:21471153).
Binds to the 3'UTR of the transcript of the heterochronic protein lin-28 to post-transcriptionally negatively regulate its expression in certain tissue types in the later larval stages (PubMed:21471153).
During larval development, controls the timing of seam cell division and terminal differentiation into adult alae (PubMed:21471153).
In vitro, it can also bind to DNA through its first zinc finger (PubMed:21471153).
May bind directly or indirectly to the promoter of the sex-determining factor xol-1 to activate its transcription (PubMed:23666922).
Its activation of xol-1 transcription controls sex determination and X chromosome dosage compensation to promote male development (PubMed:23666922).
Through the negative regulation of lin-28 transcript, it also has a role in the fox-1-sex-1-mediated determination of sexual fate (PubMed:21471153).
Acts in the intestine to play a role in regulating adult lifespan (PubMed:21471153).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytoplasm
Cellular Componentmediator complex
Cellular Componentnucleus
Molecular FunctionDNA binding
Molecular Functiondouble-stranded RNA binding
Molecular Functionmetal ion binding
Molecular Functionsingle-stranded RNA binding
Molecular Functiontranscription coactivator activity
Biological Processcell differentiation
Biological Processdetermination of adult lifespan
Biological Processnegative regulation of gene expression
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processregulation of development, heterochronic
Biological Processregulation of translation
Biological Processresponse to heat
Biological Processsex differentiation
Biological Processsex-chromosome dosage compensation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Signal element on autosome protein 2

Gene names

    • Name
      sea-2
    • ORF names
      K10G6.3

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • Bristol N2
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis

Accessions

  • Primary accession
    A0A0K3AUE4
  • Secondary accessions
    • A0A0K3AQV3
    • A0A0K3AR28
    • A0A0K3AR30
    • A0A0K3ARE6
    • A0A0K3ARN1

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Note: In embryos, diffusely accumulates in the nucleus at the 20- to 30-cell stage, but nuclear localization decreases after the 200-cell stage (PubMed:23666922).
Diffusely localized in the nucleus and cytoplasm during the L3 larval stage (PubMed:21471153).

Keywords

Phenotypes & Variants

Disruption phenotype

RNAi mediated knockdown at early larval stages and in young adults results in an extended lifespan (PubMed:21471153).
RNAi-mediated knockdown results in delayed developmental defects with an increased number of seam cells in young adults (PubMed:21471153).
RNAi-mediated knockdown suppresses the embryonic lethality of hermaphrodites in the double fox-1 y303 and sex-1 y263 mutant background (PubMed:23666922).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis415-418Abolishes RNA-binding.
Mutagenesis415-435Does not affect expression pattern. Does not rescue the seam developmental timing defects of the sea-2 b283 mutant.
Mutagenesis1398In bp283; extended lifespan, and a slow accumulation of dcap-1-positive P-bodies compared to wild-type, indicative of a slower ageing rate. Delays the L2 to L3 larval stage switch. Defective seam cell development due to delayed divisions and failed fusions during the L2 and L3 larval stages. This increases the number of seam cells at later larval stages and delays their terminal differentiation, resulting in discontinuous alae formation. Ectopic expression of the heterochronic protein lin-28 whereby, in contrast to wild-type, lin-28 is expressed in the head, tail and in seam cells of L3 and L4 larvae. Prominent nuclear localization of the transcription factor daf-16 in the intestine resulting in the transcription of daf-16 targets. The seam cell development defects are enhanced in a daf-2 e1370 mutant background. The seam cell development defects are suppressed in a lin-28 n719 mutant background. Partially suppresses the premature alae formation defect in a hbl-1 RNAi mutant background. Suppresses the embryonic lethality of hermaphrodites in the double fox-1 and sex-1 RNAi mutant background.
Mutagenesis1670-1673Abolishes RNA-binding.
Mutagenesis1670-1690Does not affect expression pattern. Does not rescue the seam cell developmental timing defects of the sea-2 bp283 mutant.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004505201-1968Signal element on autosome protein 2

Proteomic databases

Expression

Tissue specificity

Expressed in seam cells, intestine cells, pharyngeal muscles and nerve ring neurons.

Developmental stage

In embryos, expressed in 20- to 30-cell stage and expression decreases after the 200-cell stage (PubMed:23666922).
Expressed in seam cells, intestine cells, pharyngeal muscles and nerve ring neurons in L3 stage larvae and expression persists into adults (PubMed:21471153).

Gene expression databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for compositional bias, region, zinc finger.

Type
IDPosition(s)Description
Compositional bias72-109Polar residues
Region72-252Disordered
Compositional bias117-208Polar residues
Compositional bias271-286Polar residues
Region271-364Disordered
Compositional bias293-360Polar residues
Zinc finger413-440C2H2-type 1
Region451-499Disordered
Compositional bias468-499Polar residues
Region538-601Disordered
Compositional bias540-560Basic and acidic residues
Compositional bias571-596Basic and acidic residues
Zinc finger651-672C2H2-type 2; degenerate
Region681-712Disordered
Compositional bias785-810Polar residues
Region785-854Disordered
Compositional bias826-854Polar residues
Zinc finger856-875C2H2-type 3; degenerate
Region882-906Disordered
Compositional bias975-1014Polar residues
Region975-1069Disordered
Compositional bias1027-1049Polar residues
Region1083-1227Disordered
Compositional bias1093-1129Polar residues
Compositional bias1146-1227Polar residues
Region1246-1273Disordered
Compositional bias1251-1268Polar residues
Zinc finger1274-1297C2H2-type 4
Region1333-1478Disordered
Compositional bias1377-1401Basic and acidic residues
Compositional bias1410-1445Pro residues
Region1569-1608Disordered
Compositional bias1624-1639Polar residues
Region1624-1671Disordered
Zinc finger1668-1694C2H2-type 5; degenerate
Region1769-1822Disordered
Compositional bias1796-1822Polar residues
Zinc finger1826-1858C2H2-type 6

Domain

The Zinc finger domains 1 and 5 bind single-stranded and double-stranded RNAs (PubMed:21471153).
The Zinc finger domain 1 binds DNA in vitro (PubMed:21471153).

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

This entry describes 19 isoforms produced by Alternative splicing.

A0A0K3AUE4-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    1,968
  • Mass (Da)
    215,234
  • Last updated
    2015-11-11 v1
  • MD5 Checksum
    5165CA66AADD5C4B7FA98AE7242EAD73
MGREYKFTGIAAKLNPLNCRLKLEIAEDLDERVPTTSTSCSVASVAAATATINTTAPTVLTKSELQKTLQKTSSSFSSSLATTTTTSSHLNAPVESMEGHSSLASYSHHHPSSSHHHHPGQQQSSSSSSSSHLQDFQSPPSASHPYYHQQQPQHQHQQAQQYGQATGSTNGGGQQQMTSMYGGNDYDQHQLHHQNQQHQASTSTQQFHHPQRPPPPQYDQPSSSTGSSLPPLHTVRYEQLPPPPSNQRTPTQQLQYPVKVVEAGGQAYAQQVQQAQQSNRSGAAGVNSALQPKPLPPLSSITSISSSAAGSSISAPSTSQPSTTSSLITSPPSTSSSSMAPRKTPPNASSSSLIKRQSQDVQEQQRVDFEVARNVSQIMSKNGLKVMHEPLLTGSLPQLAPLAPLPPPKSGVYQCPNCNRNLANARNLQRHRQTCGSAQHAAPQLAAMLQRSPPPCASAPPVAPPTAPSTSFQHHNSTGNLTLSYSSSSSRHQSSLYSPQLEHQDLVGNPNVMLSDGYEYKDDPMLYQGPSGLSDSIWSRDDSFHSEPPSASHDQLDMDHLGFPDPLQDPLHHLDSFDSADHRKETPRECHEPDELMTLDPTPPQCGSERFYGINIDDMPLSLDCDEPLMRSESASLSSSSQGRNTPAAVFTCEACKKSVSSERSLRRHYNTCKMFQTELAASGEERPPTTKRKPATKRPSKKKEASEGPEKNSAILAALRKEPAAPQQPQQLQFQQNYQPSPQFQAPYGGGSLPSISASWLHSASTSAAAAAPERSEMFTSPIVTSAPNPYIHQLPHQQPQQQKSSPLEDLLNEQDESADDDGDSRSSSGTVSNSTTTTTTATTTSSKSTGNPLFTCEHCARQLCSMSNLKRHRATCKVAASSSSNSAASRPPSQPSTPATAPATPMLQASQAPQPLQAPPQSPMETTATVTYTKTTVPPSVANTWNTEKAQLISPKPRSQTIFSEASSSMTVGDALRAQQHQQKMDQQIQIQFQQQQQQRFQHHQQQQQAGRIPPRPPNPILNQVQNPPQQVQHNQHQNQMLNPIRQPLLQSPPPPPPKKGLIEHKNTDLVLITSEPLAERMDAKRRSSEGLVAVTSTPLPPIQLPQRSQAPAPSRQQQQQPPVAYQVQFNGRPLPPMQLPPLQNPHNQQQQHQMLHQSQMNYQQVQQVQQVQHVQQQQNLQNQHHHQQQHHQQNQQQAPGNRSRSHSNVGKMEQEAQRQGSPLDSIITSVPLSIEVHHHIMKPGPLEQGQSSVDSQSTAEPSPRKASQQAYICPECKKTYASRKNVKRHRMAVHKLTLDEILANPEQPALDPLSAVGGAGRRHTVAGLETPDSALKPAPTKRKASEAPSAGVATKKGKAMAASVDEIQVKEEEEDQKEETVGSVERQEPPKKPVADDHKSAIAPLPPANTIMPPPPPYNQASAVPLNPPRTALPPLQLPPLQPLQSESPSWASMSAPPTALIPRTPRSSEFADEEDTRAMAKIAAELKRSAEDWPVLAVIEGVAAEPTNGEDIDEDEILIKRLRQGGVLEDVGDVSDLLRDVQGGVDGEPFSEDMLLEKNLSTASSVGLPSLASPGEQFGYQQYSQHPQQHPQQHPQQHPQQQQQVWNPNYEFQGYMQQQHPPMPVSQQFQQPLLQRPASQPPPARPIVKNSRRPSTTPKPPPNLTCSGCKKILGSDYSLRRHRAGCADVQQALNPEYPRPPKRKAAREAQKINEAEILASMPDPQMVAERSAAVAEAAAAEAAVERIGALPPPSVVHEIVHQVNADRQSMKKHNKTTSPPPAQEAPPTCAPDDPMSSSSSSSTSSASPLQGGAKPSTNQARHYCQFPECGKNFSSEWNLARHTRESCKMTTRAHSYEPTSAADKIDLIFMDKSKRRVSRTFLCTVSSLISYWLGEQGDRLELDTKWEHFQLLLDVHTLKVAITADNINLIAEQSKKYQLEHVIRMADQFMMNTNYTTPPTHVQL

A0A0K3AUE4-2

  • Name
    a
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A0K3AUE4-3

A0A0K3AUE4-4

A0A0K3AUE4-5

A0A0K3AUE4-6

A0A0K3AUE4-7

A0A0K3AUE4-8

A0A0K3AUE4-9

  • Name
    i
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A0K3AUE4-10

A0A0K3AUE4-11

A0A0K3AUE4-12

A0A0K3AUE4-13

A0A0K3AUE4-14

  • Name
    n
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A0K3AUE4-15

A0A0K3AUE4-16

  • Name
    p
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A0K3AUE4-17

A0A0K3AUE4-18

  • Name
    r
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A0K3AUE4-19

  • Name
    s
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for alternative sequence, compositional bias.

Type
IDPosition(s)Description
Alternative sequenceVSP_0606361-96in isoform a, isoform b, isoform c and isoform j
Alternative sequenceVSP_0606351-176in isoform k, isoform l, isoform n and isoform o
Alternative sequenceVSP_0606341-338in isoform d, isoform m, isoform q and isoform r
Alternative sequenceVSP_0606331-867in isoform e and isoform s
Alternative sequenceVSP_0606321-1852in isoform p
Compositional bias72-109Polar residues
Compositional bias117-208Polar residues
Compositional bias271-286Polar residues
Compositional bias293-360Polar residues
Compositional bias468-499Polar residues
Compositional bias540-560Basic and acidic residues
Compositional bias571-596Basic and acidic residues
Alternative sequenceVSP_060637687-831in isoform b, isoform h, isoform i, isoform j, isoform l, isoform m, isoform o and isoform q
Compositional bias785-810Polar residues
Compositional bias826-854Polar residues
Compositional bias975-1014Polar residues
Compositional bias1027-1049Polar residues
Compositional bias1093-1129Polar residues
Compositional bias1146-1227Polar residues
Compositional bias1251-1268Polar residues
Compositional bias1377-1401Basic and acidic residues
Compositional bias1410-1445Pro residues
Compositional bias1624-1639Polar residues
Compositional bias1796-1822Polar residues
Alternative sequenceVSP_0606381816-1825in isoform c, isoform d, isoform e, isoform f, isoform h, isoform j, isoform k, isoform l and isoform m
Alternative sequenceVSP_0606391823-1828in isoform b
Alternative sequenceVSP_0606401826-1968in isoform c, isoform d, isoform e, isoform f, isoform h, isoform j, isoform k, isoform l and isoform m

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284602
EMBL· GenBank· DDBJ
CDG24088.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CDG24089.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CDG24090.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CDG24091.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CDG24092.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86419.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86420.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86421.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86422.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86503.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86504.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86505.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86506.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86507.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86508.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86509.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86510.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86511.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284602
EMBL· GenBank· DDBJ
CTQ86512.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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