Q80W68 · KIRR1_MOUSE

  • Protein
    Kin of IRRE-like protein 1
  • Gene
    Kirrel1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (PubMed:11416156).
Is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1

Miscellaneous

Knockout of this gene results in perinatal lethality accompanied by proteinuria, and effacement of glomerular podocytes.

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 Componentcell projection membrane
Cellular Componentcell-cell junction
Cellular Componentdendritic shaft
Cellular Componentmembrane raft
Cellular Componentperinuclear region of cytoplasm
Cellular Componentplasma membrane
Molecular Functioncell adhesion molecule binding
Molecular Functionmyosin binding
Biological Processcell-cell adhesion
Biological Processcell-cell junction maintenance
Biological Processglomerular filtration
Biological Processnegative regulation of protein phosphorylation
Biological Processpositive regulation of actin filament polymerization
Biological Processrenal protein absorption

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Kin of IRRE-like protein 1
  • Alternative names
    • Kin of irregular chiasm-like protein 1
    • Nephrin-like protein 1

Gene names

    • Name
      Kirrel1
    • Synonyms
      Kirrel, Neph1

Organism names

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

Accessions

  • Primary accession
    Q80W68
  • Secondary accessions
    • Q8CIJ4
    • Q8CJ59
    • Q923L4

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Single-pass type I membrane protein
Note: Predominantly located at podocyte slit diaphragm.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain48-531Extracellular
Transmembrane532-552Helical
Topological domain553-789Cytoplasmic

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis633No effect on interaction with NPHS2.
Mutagenesis637Inhibits interaction with NPHS2.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 40 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for signal, chain, disulfide bond, glycosylation, modified residue.

TypeIDPosition(s)Description
Signal1-47
ChainPRO_000001509448-789Kin of IRRE-like protein 1
Disulfide bond74↔132
Glycosylation78N-linked (GlcNAc...) asparagine
Glycosylation172N-linked (GlcNAc...) asparagine
Disulfide bond175↔232
Disulfide bond276↔319
Glycosylation329N-linked (GlcNAc...) asparagine
Disulfide bond361↔403
Disulfide bond445↔504
Glycosylation503N-linked (GlcNAc...) asparagine
Modified residue606Phosphoserine
Modified residue637Phosphotyrosine; by FYN
Modified residue638Phosphotyrosine; by FYN
Modified residue654Phosphotyrosine
Modified residue657Phosphotyrosine
Modified residue756Phosphotyrosine

Post-translational modification

Phosphorylation probably regulates the interaction with NPHS2. Phosphorylated at Tyr-637 and Tyr-638 by FYN, leading to GRB2 binding (By similarity).
N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Abundantly expressed in kidney. Specifically expressed in podocytes of kidney glomeruli.

Gene expression databases

Interaction

Subunit

Interacts with TJP1/ZO-1 and with NPHS2/podocin (via the C-terminus). Interacts with NPHS1/nephrin (via the Ig-like domains); this interaction is dependent on KIRREL1 glycosylation. Homodimer (via the Ig-like domains). Interacts when tyrosine-phosphorylated with GRB2 (By similarity).

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for domain, motif, region.

TypeIDPosition(s)Description
Domain49-147Ig-like C2-type 1
Domain152-248Ig-like C2-type 2
Domain255-331Ig-like C2-type 3
Domain340-419Ig-like C2-type 4
Domain424-520Ig-like C2-type 5
Motif437-439Cell attachment site
Region687-713Disordered

Sequence similarities

Belongs to the immunoglobulin superfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q80W68-1

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
    789
  • Mass (Da)
    87,176
  • Last updated
    2003-06-01 v1
  • Checksum
    27FB31FFCCC25A2A
MTLESPSTRLMTCQSSLLPEKPRFLSQKMWAPHLVVAYLIFVTLALALPGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGAGILVVFSFAALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASISTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV

Q80W68-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 606-634: SFKDDVDLKQDLRCDTIDTREEYEMKDPT → VRIMLLSTWPRLFIVLRPAPPAFNDFRYL
    • 635-789: Missing

Sequence caution

The sequence AAK00528.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence AAK00528.1 differs from that shown. Reason: Frameshift

Features

Showing features for sequence conflict, alternative sequence.

TypeIDPosition(s)Description
Sequence conflict355in Ref. 2; AAN73043
Sequence conflict442in Ref. 2; AAN73043
Alternative sequenceVSP_011736606-634in isoform 2
Alternative sequenceVSP_011737635-789in isoform 2
Sequence conflict727in Ref. 2; AAN73043

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF480411
EMBL· GenBank· DDBJ
AAN73043.1
EMBL· GenBank· DDBJ
mRNA
AY243095
EMBL· GenBank· DDBJ
AAO91769.1
EMBL· GenBank· DDBJ
mRNA
BC023765
EMBL· GenBank· DDBJ
AAH23765.3
EMBL· GenBank· DDBJ
mRNA
AY017368
EMBL· GenBank· DDBJ
AAK00528.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.

Genome annotation databases

Similar Proteins

Disclaimer

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