Q80W68 · KIRR1_MOUSE
- ProteinKin of IRRE-like protein 1
- GeneKirrel1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids789 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell projection membrane | |
Cellular Component | cell-cell junction | |
Cellular Component | dendritic shaft | |
Cellular Component | membrane raft | |
Cellular Component | perinuclear region of cytoplasm | |
Cellular Component | plasma membrane | |
Molecular Function | cell adhesion molecule binding | |
Molecular Function | myosin binding | |
Biological Process | cell-cell adhesion | |
Biological Process | cell-cell junction maintenance | |
Biological Process | glomerular filtration | |
Biological Process | negative regulation of protein phosphorylation | |
Biological Process | positive regulation of actin filament polymerization | |
Biological Process | renal protein absorption |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameKin of IRRE-like protein 1
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ80W68
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Single-pass type I membrane protein
Note: Predominantly located at podocyte slit diaphragm.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 48-531 | Extracellular | ||||
Sequence: LPGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIA | ||||||
Transmembrane | 532-552 | Helical | ||||
Sequence: GATIGAGILVVFSFAALVFFL | ||||||
Topological domain | 553-789 | Cytoplasmic | ||||
Sequence: YRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASISTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 633 | No effect on interaction with NPHS2. | ||||
Sequence: P → S | ||||||
Mutagenesis | 637 | Inhibits interaction with NPHS2. | ||||
Sequence: Y → A |
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.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-47 | |||||
Sequence: MTLESPSTRLMTCQSSLLPEKPRFLSQKMWAPHLVVAYLIFVTLALA | ||||||
Chain | PRO_0000015094 | 48-789 | Kin of IRRE-like protein 1 | |||
Sequence: LPGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGAGILVVFSFAALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTASISTATRVMKAIYSSFKDDVDLKQDLRCDTIDTREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV | ||||||
Disulfide bond | 74↔132 | |||||
Sequence: CVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYEC | ||||||
Glycosylation | 78 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 172 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 175↔232 | |||||
Sequence: CRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTC | ||||||
Disulfide bond | 276↔319 | |||||
Sequence: CQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSC | ||||||
Glycosylation | 329 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 361↔403 | |||||
Sequence: CVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTC | ||||||
Disulfide bond | 445↔504 | |||||
Sequence: CFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNC | ||||||
Glycosylation | 503 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 606 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 637 | Phosphotyrosine; by FYN | ||||
Sequence: Y | ||||||
Modified residue | 638 | Phosphotyrosine; by FYN | ||||
Sequence: Y | ||||||
Modified residue | 654 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 657 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 756 | Phosphotyrosine | ||||
Sequence: Y |
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
- PTM
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
Structure
Family & Domains
Features
Showing features for domain, motif, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-147 | Ig-like C2-type 1 | ||||
Sequence: PGTQTRFSQEPADQTVVAGQRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLT | ||||||
Domain | 152-248 | Ig-like C2-type 2 | ||||
Sequence: PEETRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIEPTDLDIGRVFTCRSMNEAIPNGKETSIE | ||||||
Domain | 255-331 | Ig-like C2-type 3 | ||||
Sequence: PTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVS | ||||||
Domain | 340-419 | Ig-like C2-type 4 | ||||
Sequence: PRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPL | ||||||
Domain | 424-520 | Ig-like C2-type 5 | ||||
Sequence: PPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLE | ||||||
Motif | 437-439 | Cell attachment site | ||||
Sequence: RGD | ||||||
Region | 687-713 | Disordered | ||||
Sequence: RAPASDYGTEPTPSGPSAPGGTDTTSQ |
Sequence similarities
Belongs to the immunoglobulin superfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe 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.
- Name1
- Length789
- Mass (Da)87,176
- Last updated2003-06-01 v1
- Checksum27FB31FFCCC25A2A
Q80W68-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 355 | in Ref. 2; AAN73043 | ||||
Sequence: S → F | ||||||
Sequence conflict | 442 | in Ref. 2; AAN73043 | ||||
Sequence: K → E | ||||||
Alternative sequence | VSP_011736 | 606-634 | in isoform 2 | |||
Sequence: SFKDDVDLKQDLRCDTIDTREEYEMKDPT → VRIMLLSTWPRLFIVLRPAPPAFNDFRYL | ||||||
Alternative sequence | VSP_011737 | 635-789 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 727 | in Ref. 2; AAN73043 | ||||
Sequence: F → L |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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. |