Kirrel2
entrez
243911
canonical
uniprot
Q7TSU7
canonical
ensembl
ENSMUSG00000036915
resolver
ensp
ENSMUSP00000039395
resolver
ensp
ENSMUSP00000184194
resolver
genesymbol
Kirrel2
resolver
genesymbol_syn
Neph3
resolver
uniprot
A0A4X8
resolver
uniprot
Q7TQ98
resolver
uniprot_entry
A0A4X8_MOUSE
resolver
uniprot_entry
KIRR2_MOUSE
resolver
uniprot_sec
Q7TQ98
resolver
amino_acid_sequence
MLASALLVFLCCFKGHAGSSPHFLQQPEDMVVLLGEEARLPCALGAYRGLVQWTKDGLALGGERDLPGWSRYWISGNSASGQHDLHIKPVELEDEASYECQASQAGLRSRPAQLHVMVPPEAPQVLGGPSVSLVAGVPGNLTCRSRGDSRPAPELLWFRDGIRLDGSSFHQTTLKDKATGTVENTLFLTPSSHDDGATLICRARSQALPTGRDTAVTLSLQYPPMVTLSAEPQTVQEGEKVTFLCQATAQPPVTGYRWAKGGSPVLGARGPRLEVVADATFLTEPVSCEVSNAVGSANRSTALEVLYGPILQAKPKSVSVDVGKDASFSCVWRGNPLPRITWTRMGGSQVLSSGPTLRLPSVALEDAGDYVCRAEPRRTGLGGGKAQARLTVNAPPVVTALQPAPAFLRGPARLQCVVFASPAPDSVVWSWDEGFLEAGSLGRFLVEAFPAPEVEGGQGPGLISVLHISGTQESDFTTGFNCSARNRLGEGRVQIHLGRRDLLPTVRIVAGAASAATSLLMVITGVVLCCWRHGSLSKQKNLVRIPGSSEGSSSRGPEEETGSSEDRGPIVHTDHSDLVLEEKEALETKDPTNGYYRVRGVSVSLSLGEAPGGGLFLPPPSPIGLPGTPTYYDFKPHLDLVPPCRLYRARAGYLTTPHPRAFTSYMKPTSFGPPELSSGTPPFPYATLSPPSHQRLQTHV
uniprot
proteins
function
FUNCTION: May regulate basal insulin secretion. {ECO:0000269|PubMed:26324709}.
uniprot
proteins
mass_dalton
74529
uniprot
proteins
mutagenesis
MUTAGEN 595..596; /note="YY->FF: Enhances stability. Modifies the structure of cell contacts. Localization at the plasma membrane is increased. Does not affect dimerization. No change in shedding activity."; /evidence="ECO:0000269|PubMed:26324709"; MUTAGEN 631..632; /note="YY->FF: Does not modify the structure of cell contacts. No effect on localization at the plasma membrane. No change in shedding activity."; /evidence="ECO:0000269|PubMed:26324709"; MUTAGEN 653; /note="Y->F: Does not modify the structure of cell contacts. No effect on localization at the plasma membrane. No change in shedding activity."; /evidence="ECO:0000269|PubMed:26324709
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. {ECO:0000269|PubMed:26324709}.; PTM: Phosphorylated at Ser-548 or Ser-549; due to site ambiguity, the exact position of the serine phosphorylation could not be determined. Phosphorylation at residues Tyr-631 and/or Tyr-632. FYN mediates tyrosine phosphorylation in pancreatic beta-cells. {ECO:0000269|PubMed:26324709}.; PTM: The extracellular domain is cleaved leading to the generation of a soluble fragment and a membrane-bound C-terminal fragment, which is further cleaved by gamma-secretase. {ECO:0000269|PubMed:26324709}.
uniprot
proteins
protein_family
Immunoglobulin superfamily
uniprot
proteins
pubmed
12424224
uniprot
proteins
pubmed
12837264
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19887377
uniprot
proteins
pubmed
26324709
uniprot
proteins
sequence_length
700
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26324709}; Single-pass type I membrane protein {ECO:0000305}. Note=Localized along the sites of the cell contacts (PubMed:26324709). Colocalizes with E-Cadherin and beta-catenin (PubMed:26324709). {ECO:0000269|PubMed:26324709}.
uniprot
proteins
transmembrane_region
TRANSMEM 508..528; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins