A0A1C3NSL9 · AJM1_CAEEL

  • Protein
    Apical junction molecule
  • Gene
    ajm-1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Controls adherens junction integrity (PubMed:11715019).
Required for the correct rate and completion of elongation of the embryos (PubMed:11715019).

Features

Showing features for binding site.

116442004006008001,0001,2001,4001,600
TypeIDPosition(s)Description
Binding site1445Zn2+ 1 (UniProtKB | ChEBI)
Binding site1448Zn2+ 1 (UniProtKB | ChEBI)
Binding site1464Zn2+ 2 (UniProtKB | ChEBI)
Binding site1467Zn2+ 2 (UniProtKB | ChEBI)
Binding site1472Zn2+ 1 (UniProtKB | ChEBI)
Binding site1476Zn2+ 1 (UniProtKB | ChEBI)
Binding site1484Zn2+ 2 (UniProtKB | ChEBI)
Binding site1488Zn2+ 2 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentadherens junction
Cellular Componentapical junction complex
Cellular Componentapical plasma membrane
Cellular Componentapicolateral plasma membrane
Cellular Componentcell-cell junction
Cellular Componentciliary basal body
Cellular Componentdendrite terminus
Cellular Componentplasma membrane
Molecular Functioncytoskeletal protein binding
Molecular Functionmetal ion binding
Biological Processcell-cell junction organization
Biological Processembryo development ending in birth or egg hatching

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Apical junction molecule

Gene names

    • Name
      ajm-1
    • ORF names
      C25A11.4
      , CELE_C25A11.4

Organism names

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

Accessions

  • Primary accession
    A0A1C3NSL9
  • Secondary accessions
    • A0A1C3NSK1
    • A0A1C3NSK9
    • A0A1C3NSL1
    • A0A1C3NSL6
    • A0A1C3NSM8

Proteomes

Organism-specific databases

Subcellular Location

Apical cell membrane
Note: grdn-1-dependent localization at sensory neuron dendritic tips (PubMed:27623382).
The coiled-coil domain is sufficient to localize to apical junctions (PubMed:11715019).

Keywords

Phenotypes & Variants

Disruption phenotype

Mutant embryos enclose normally and initiate elongation without obvious morphological abnormalities, yet at a slower rate than the wild type. Elongation is consistently arrested at the 2-3-fold stage, accompanied by the formation of a large vacuole in the posterior region.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004429281-1644Apical junction molecule

Proteomic databases

Expression

Tissue specificity

Expressed by epithelial cells (PubMed:11715019).
Expressed in sensory neuron dendritic tips (PubMed:27623382).

Developmental stage

Expression occurs in the embryonic hypodermis, pharynx and intestine, as well as in postembryonic epithelia, including the vulva, uterus, spermathecae, pharynx, intestine, hindgut, hypodermis and male tail.

Gene expression databases

Interaction

Subunit

Interacts with dlj-1 (via L27 domain); the interaction regulates ajm-1 apical junction location.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, coiled coil, zinc finger.

TypeIDPosition(s)Description
Region1-20Disordered
Compositional bias30-45Basic and acidic residues
Region30-60Disordered
Compositional bias142-156Polar residues
Region142-339Disordered
Compositional bias157-171Basic and acidic residues
Compositional bias174-201Pro residues
Compositional bias202-234Polar residues
Compositional bias241-269Polar residues
Compositional bias284-307Polar residues
Region381-455Disordered
Compositional bias409-455Basic and acidic residues
Coiled coil428-924
Region561-583Disordered
Region647-678Disordered
Compositional bias744-800Basic and acidic residues
Region744-851Disordered
Compositional bias814-851Basic and acidic residues
Region977-1052Disordered
Compositional bias1008-1052Basic and acidic residues
Region1122-1198Disordered
Compositional bias1136-1198Basic and acidic residues
Region1292-1315Disordered
Compositional bias1295-1315Polar residues
Zinc finger1445-1488MYND-type

Domain

The coiled-coil domain is sufficient to localize to apical junctions.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

  • Sequence status
    Complete

This entry describes 11 isoforms produced by Alternative splicing.

A0A1C3NSL9-1

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
    1,644
  • Mass (Da)
    193,402
  • Last updated
    2016-11-02 v1
  • Checksum
    F57A629DDA31B700
MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHKLADADRDQEEELVFNEERRKTVTMDDNASLRSASITFDANRDEQDLLNESFASNPTDETVLMQKTKDEMDATSERPRSPLDLPPPPASVVLHPSAPPPPPPPLSSTEVVGNTTTTTTTHYAPKTWNDPSITTAPKIPVSLLSGAQPLPSVLTQRTTTSSYSAPNYSASSMSGVPSDVAPPPPLPIPNQSSSSAASYQHHHASSISKSISSSREDLLSEHATSRSTVREIPVHRAPSTAPSHSSVFEYHMMPTTTSTYHHVETPSDEYYRREVMTRTIITRSTEALSQTPLGRPASPLDRYLPYPTTTTTTSGDGRTREEKTVDYKVTYHRDIEEQERRIREDQARRQQEEQDRRDREDNARRILAQREHQEMERLREQQNLSERALAERERADKERLQQERLLRQQREKKRREEWDRLESIRLAEEEAELARRRALEKERIDREKAEEERKTMERLERERARLERERLEEERRQKEKAETERIERERREHERIEIERIERIKRERIERERREREEKKAEEDRLLRERLELERIERERRELEARERQELELQRREAEDRERQRLEDEAREMRRREEERREAELVADVHRQAEERERLRKRQEREEAERLERIRLEQQKIDMERIDAERRERERKEEERREFELIEAARRKKEARDRDRLDEMERERVREEEERREKERREQERRIAAEKERKRRQEEEEEIARLNELQRAAAARQAQRNAELDRQRQRDELDRKAQELSEREMREKERRDRERANEEAQLADLLERERHNQLIRENERREAVERANNRRLEDRRSRDKLDHIVRERSEKEQFELEKRRLLAEKEAMNRKKNHLLSSETLAKLTQPMYYTTREPEVTTKVERQVIERIDRNVWVEDVPYAPSQSAMGYLDNDENNRDRLYNPNDLNRNGSSRSRYQRAKNEKARRDFYHSSQDSADPVTERFRKSTDDLTTRSRPEYRGPLLQKFHDSEFRTTALNETDGLPYRRMGPSPYEQPFAKLLEETERRYAHYNSRASNPSIYQSSRYYYPERHGQPQHTDNTRAESVVAYERESRRESPADQAHIRSRSADYLMDRRIREETEVPENQLQKTRVEPHDQSPRESRISEYEMRFRKSTEKLTVPDWYRENRPQGQTAQTSTYRYGNGVEPMSTTTTTTTVINGTSSHQQAPPPVPPQPIGNIGLPRGMFDRYKDDIEELRRSRSSLHQTGQQETSNRQGSTLSVGGIVDQGHALPGYTVSEVPNAWNLHTSRTSRVVEVADTFVGTSSHEYGNFTNRYGGRVTIEEVLDSIFQKVTPTNQRLNFDRSYPQADELFQGNVDGPGIYTNNYSVMRQVLKSPERAEHILQNEELFVRCTECHRTRELSAARLFFVSCKHCYTYYCSRECRHNNWPNHSGRCSFARINTLCKDVIMKVREDEQAQAFMSKVARDGFSVSGRGSVNIRLSSPQLAQAYVSNGWRALSAYPNDQLLYYYTVKALIAERKEPSLIALCNRYEPREKFILSVSIIADIEHCPETPPPETRELSAVQFSSPRSRYEAIQNQNAPYFSEFAHNV

A0A1C3NSL9-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-96: MSTTTPEKPEEIIDATGTSDTAEKIEVVISKEEPAEQKNEVEEPDYAQVPAESEDDAAQELAPTDSAIQVVHVLEAPQKAELVTIPLAHSEAEDHK → MIPFDPTTSEIHTQKMSQFIV

A0A1C3NSL9-6

  • Name
    6
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MDIENLQSSNNRSQKSRPPDGFNAILQTAFSAILAFVLSLRIIVFATARKRLTTTAANPDIQVEEASSSSSDTSSDTEIVEEGVFIQRQGEPTMSEKKPAQGMPSVMSLLQTDEILSSCSDDEPTTSGLIPLPSLIQSNMSVLPNFLHTINEEESDEIRSLTGSSLASPRTVVDRRLSNISLLSPTPDEDFGLEQQEQQPENSEEVRGRESRTSLEEERIVVGEPRTTRQIEITQSASEDDRLDLLKELAKIGKSNTSTSQM

A0A1C3NSL9-7

  • Name
    7
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-8

  • Name
    8
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MDIENLQSSNNRSQKSRPPDGFNAILQTAFSAILAFVLSLRIIVFATARKRLTTTAANPDIQVEEASSSSSDTSSDTEIVEEGVFIQRQGEPTMSEKKPAQGMPSVMSLLQTDEILSSCSDDEPTTSGLIPLPSLIQSNMSVLPNFLHTINEEESDEIRSLTGSSLASPRTVVDRRLSNISLLSPTPDEDFGLEQQEQQPENSEEVRGRESRTSLEEERIVVGEPRTTRQIEITQSASEDDRLDLLKELAKIGKSNTSTSQM
    • 1088-1128: Missing

A0A1C3NSL9-9

  • Name
    9
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-10

  • Name
    10
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

A0A1C3NSL9-11

  • Name
    11
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H2KYC5H2KYC5_CAEELajm-11293
Q95ZY7Q95ZY7_CAEELajm-11573

Features

Showing features for alternative sequence, compositional bias.

TypeIDPosition(s)Description
Alternative sequenceVSP_0592931in isoform 6 and isoform 8
Alternative sequenceVSP_0592921-96in isoform 5
Alternative sequenceVSP_0592911-119in isoform 4
Alternative sequenceVSP_0592901-157in isoform 9
Alternative sequenceVSP_0592891-164in isoform 10
Alternative sequenceVSP_0592881-265in isoform 7
Alternative sequenceVSP_0592871-344in isoform 11
Alternative sequenceVSP_0592861-368in isoform 3
Alternative sequenceVSP_0592851-467in isoform 2
Compositional bias30-45Basic and acidic residues
Compositional bias142-156Polar residues
Compositional bias157-171Basic and acidic residues
Compositional bias174-201Pro residues
Compositional bias202-234Polar residues
Compositional bias241-269Polar residues
Compositional bias284-307Polar residues
Compositional bias409-455Basic and acidic residues
Compositional bias744-800Basic and acidic residues
Compositional bias814-851Basic and acidic residues
Compositional bias1008-1052Basic and acidic residues
Alternative sequenceVSP_0592941088-1128in isoform 8
Compositional bias1136-1198Basic and acidic residues
Compositional bias1295-1315Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
BX284606
EMBL· GenBank· DDBJ
SBV53382.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
CCD62273.2
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53392.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53384.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53383.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53380.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53390.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
CCD62272.2
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53381.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
CCD62269.1
EMBL· GenBank· DDBJ
Genomic DNA
BX284606
EMBL· GenBank· DDBJ
SBV53391.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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