Q8BGS1 · E41L5_MOUSE

  • Protein
    Band 4.1-like protein 5
  • Gene
    Epb41l5
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role in the formation and organization of tight junctions during the establishment of polarity in epithelial cells.

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 Componentadherens junction
Cellular Componentcell leading edge
Cellular Componentcytoskeleton
Cellular Componentcytosol
Cellular Componentfocal adhesion
Cellular Componentnucleoplasm
Cellular Componentphotoreceptor inner segment
Cellular Componentplasma membrane
Cellular Componentruffle membrane
Molecular Functioncytoskeletal protein binding
Molecular Functionprotein domain specific binding
Biological Processactin cytoskeleton organization
Biological Processactomyosin structure organization
Biological Processapical constriction
Biological Processaxial mesoderm development
Biological Processaxial mesoderm morphogenesis
Biological Processcell morphogenesis
Biological Processcellular response to transforming growth factor beta stimulus
Biological Processectoderm development
Biological Processembryonic foregut morphogenesis
Biological Processendoderm development
Biological Processepithelial cell morphogenesis
Biological Processepithelial to mesenchymal transition
Biological Processin utero embryonic development
Biological Processleft/right axis specification
Biological Processmesoderm development
Biological Processmesoderm migration involved in gastrulation
Biological Processnegative regulation of cell-cell adhesion
Biological Processneural plate morphogenesis
Biological Processparaxial mesoderm development
Biological Processpositive regulation of cell-matrix adhesion
Biological Processpositive regulation of epithelial cell migration
Biological Processpositive regulation of focal adhesion assembly
Biological Processpost-transcriptional regulation of gene expression
Biological Processregulation of establishment of protein localization
Biological Processsomite rostral/caudal axis specification
Biological Processsomitogenesis
Biological Processsubstrate-dependent cell migration, cell attachment to substrate
Biological Processunidimensional cell growth

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Band 4.1-like protein 5
  • Alternative names
    • Erythrocyte membrane protein band 4.1-like 5

Gene names

    • Name
      Epb41l5
    • Synonyms
      Epb4.1l5, Kiaa1548

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • Czech II
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q8BGS1
  • Secondary accessions
    • Q3TJG0
    • Q69ZG8
    • Q8BSC9
    • Q99KZ8

Proteomes

Organism-specific databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003303551-731Band 4.1-like protein 5
Modified residue455In isoform Q8BGS1-2; Omega-N-methylarginine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

In the retina, expressed at the outer limiting membrane, retinal pigment epithelium, outer nuclear layer and outer plexiform layer (at protein level) (PubMed:17920587).
Also detected in the inner segments (at protein level) (PubMed:17920587).
Expressed at the basolateral and apical sides of the mesonephric tubules in the kidney (at protein level) (PubMed:17920587).

Developmental stage

At 10.5 dpc, strongly expressed in the developing neural tube and optic vesicle, as well as in the branchial arches and kidney (PubMed:17920587).
In the developing kidney, detected in the mesonephrotic tubules (PubMed:17920587).
At 11.5 dpc, expressed along the entire cranial-caudal length of the developing neural tube, including the anterior forebrain and the posterior spinal cord (PubMed:17920587).
Always restricted to the ventricular layer, where proliferative cells are located (PubMed:17920587).
Conversely, not detected in postmitotic neural compartments (PubMed:17920587).
In the developing lung, at 11.5 dpc, expressed in the internal endodermal layer and in particular in the nascent bronchial tips (PubMed:17920587).
At 12.5 dpc, expressed in the optic vesicle, detected mainly in the retinal layer (PubMed:17920587).
The retinal pigment epithelium shows only background levels (PubMed:17920587).
At 15.5 dpc expressed at the basolateral side of the plasma membrane in brain, spinal cord, kidney, testis, intestine, skin, and muscles (PubMed:17920587).

Gene expression databases

Interaction

Subunit

Component of a complex composed of PALS1, CRB1 and EPB41L5 (By similarity).
Within the complex, interacts (via FERM domain) with PALS1 (via HOOK domain) and with CRB1 (via intracellular domain) (By similarity).
Interacts with CRB2 (via intracellular domain) (By similarity).
Interacts with CRB3 (via intracellular domain) (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region29-119Required for interaction with CRB1
Domain43-327FERM
Region352-388Disordered

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q8BGS1-1

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
    731
  • Mass (Da)
    81,636
  • Last updated
    2003-03-01 v1
  • Checksum
    77348A1F68EF596A
MLSFLRRTLGRRSMRKHAEKERLREAQRAATHIPAAGDAKSIITCRVSLLDGTDVSVDLPKKAKGQELFDQIMYHLDLIESDYFGLRFMDSAQVAHWLDGTKSIKKQVKIGSPYCLHLRVKFYSSEPNNLREELTRYLFVLQLKQDILSGKLECPFDTAVQLAAYNLQAELGDYDLAEHSPELVSEFRFVPIQTEEMELAIFEKWKEYRGQTPAQAETNYLNKAKWLEMYGVDMHVVKARDGNDYSLGLTPTGVLVFEGETKIGLFFWPKITRLDFKKNKLTLVVVEDDDQGKEQEHTFVFRLDHPKACKHLWKCAVEHHAFFRLRGPVQKSSHRSGFIRLGSRFRYSGKTEYQTTKTNKARRSTSFERRPSKRYSRRTLQMKASTTQPEDLGVLNASAQKSDSQQAWGVMSPVPVTSSSSCGAVQVEIENLPQTSATEQHDRKCLPLSVDLLNSPDLLETTIGDVTRTSETSAPFPAPDTINVATRSNELEEFKAECETLKDDTEKLKQLETEQTILPSLRPTIDINVNSQEEVVKLTEKCLNNAIENPALNAVKVPPDFKSNILKAQVEAVHKVTREDSLLTHKNASVQDAATNSTAFNENDVPVCKDSLTPVHGTAADSASVLKDATDELDALLLSLTENLMDHTVTPQVSSPSMITPRWIIPQSATISNGLAGYGASLAGTDECSQKDGFSLISPPAPFLVDAVTSSAPPLPEDSTLKQKCLLTTEL

Q8BGS1-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 445-504: CLPLSVDLLNSPDLLETTIGDVTRTSETSAPFPAPDTINVATRSNELEEFKAECETLKDD → WLSATSDRCQRGGNQWNPRALPPPQTAYRNYTDFVHEHNVKNAGAHHDAQLSGRAAMTEI
    • 505-731: Missing

Q8BGS1-3

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

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A087WP93A0A087WP93_MOUSEEpb41l5114

Sequence caution

The sequence BAD32476.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict113in Ref. 2; BAE39535
Sequence conflict173in Ref. 2; BAC28794
Alternative sequenceVSP_033039393in isoform 3
Alternative sequenceVSP_033040445-504in isoform 2
Alternative sequenceVSP_033041505-731in isoform 2

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK173198
EMBL· GenBank· DDBJ
BAD32476.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK034676
EMBL· GenBank· DDBJ
BAC28794.1
EMBL· GenBank· DDBJ
mRNA
AK044959
EMBL· GenBank· DDBJ
BAC32159.1
EMBL· GenBank· DDBJ
mRNA
AK044996
EMBL· GenBank· DDBJ
BAC32177.1
EMBL· GenBank· DDBJ
mRNA
AK079301
EMBL· GenBank· DDBJ
BAC37601.1
EMBL· GenBank· DDBJ
mRNA
AK136125
EMBL· GenBank· DDBJ
BAE22832.1
EMBL· GenBank· DDBJ
mRNA
AK161141
EMBL· GenBank· DDBJ
BAE36211.1
EMBL· GenBank· DDBJ
mRNA
AK167449
EMBL· GenBank· DDBJ
BAE39535.1
EMBL· GenBank· DDBJ
mRNA
BC003937
EMBL· GenBank· DDBJ
AAH03937.1
EMBL· GenBank· DDBJ
mRNA
BC011476
EMBL· GenBank· DDBJ
AAH11476.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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