CRB2
entrez
286204
canonical
uniprot
Q5IJ48
canonical
ensembl
ENSG00000148204
resolver
ensp
ENSP00000362734
resolver
ensp
ENSP00000435279
resolver
ensp
ENSP00000566274
resolver
genesymbol
CRB2
resolver
hgnc
HGNC:18688
resolver
uniprot
A2A3N4
resolver
uniprot
Q0QD46
resolver
uniprot
Q5JS41
resolver
uniprot
Q5JS43
resolver
uniprot
Q6ZTA9
resolver
uniprot
Q6ZWI6
resolver
uniprot_entry
CRUM2_HUMAN
resolver
uniprot_sec
A2A3N4
resolver
uniprot_sec
Q0QD46
resolver
uniprot_sec
Q5JS41
resolver
uniprot_sec
Q5JS43
resolver
uniprot_sec
Q6ZTA9
resolver
uniprot_sec
Q6ZWI6
resolver
amino_acid_sequence
MALARPGTPDPQALASVLLLLLWAPALSLLAGTVPSEPPSACASDPCAPGTECQATESGGYTCGPMEPRGCATQPCHHGALCVPQGPDPTGFRCYCVPGFQGPRCELDIDECASRPCHHGATCRNLADRYECHCPLGYAGVTCEMEVDECASAPCLHGGSCLDGVGSFRCVCAPGYGGTRCQLDLDECQSQPCAHGGTCHDLVNGFRCDCAGTGYEGTHCEREVLECASAPCEHNASCLEGLGSFRCLCWPGYSGELCEVDEDECASSPCQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLCHCPPGFEGADCGVEVDECASRPCLNGGHCQDLPNGFQCHCPDGYAGPTCEEDVDECLSDPCLHGGTCSDTVAGYICRCPETWGGRDCSVQLTGCQGHTCPLAATCIPIFESGVHSYVCHCPPGTHGPFCGQNTTFSVMAGSPIQASVPAGGPLGLALRFRTTLPAGTLATRNDTKESLELALVAATLQATLWSYSTTVLVLRLPDLALNDGHWHQVEVVLHLATLELRLWHEGCPARLCVASGPVALASTASATPLPAGISSAQLGDATFAGCLQDVRVDGHLLLPEDLGENVLLGCERREQCRPLPCVHGGSCVDLWTHFRCDCARPHRGPTCADEIPAATFGLGGAPSSASFLLQELPGPNLTVSFLLRTRESAGLLLQFANDSAAGLTVFLSEGRIRAEVPGSPAVVLPGRWDDGLRHLVMLSFGPDQLQDLGQHVHVGGRLLAADSQPWGGPFRGCLQDLRLDGCHLPFFPLPLDNSSQPSELGGRQSWNLTAGCVSEDMCSPDPCFNGGTCLVTWNDFHCTCPANFTGPTCAQQLWCPGQPCLPPATCEEVPDGFVCVAEATFREGPPAAFSGHNASSGRLLGGLSLAFRTRDSEAWLLRAAAGALEGVWLAVRNGSLAGGVRGGHGLPGAVLPIPGPRVADGAWHRVRLAMERPAATTSRWLLWLDGAATPVALRGLASDLGFLQGPGAVRILLAENFTGCLGRVALGGLPLPLARPRPGAAPGAREHFASWPGTPAPILGCRGAPVCAPSPCLHDGACRDLFDAFACACGPGWEGPRCEAHVDPCHSAPCARGRCHTHPDGRFECRCPPGFGGPRCRLPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLPCEANPCLNGGTCRAAGGVSECICNARFSGQFCEVAKGLPLPLPFPLLEVAVPAACACLLLLLLGLLSGILAARKRRQSEGTYSPSQQEVAGARLEMDSVLKVPPEERLI
uniprot
proteins
disease_involvement
DISEASE: Focal segmental glomerulosclerosis 9 (FSGS9) [MIM:616220]: A renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation. {ECO:0000269|PubMed:25557779, ECO:0000269|PubMed:27004616, ECO:0000269|PubMed:27942854, ECO:0000269|PubMed:29473663, ECO:0000269|PubMed:30212996}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Retinitis pigmentosa (RP) [MIM:268000]: A retinal dystrophy belonging to the group of pigmentary retinopathies. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Retinitis pigmentosa can be inherited as an autosomal dominant, autosomal recessive or X-linked condition. {ECO:0000269|PubMed:30593785}. Note=Disease susceptibility may be associated with variants affecting the gene represented in this entry.; DISEASE: Ventriculomegaly with cystic kidney disease (VMCKD) [MIM:219730]: A severe autosomal recessive developmental disorder manifesting in utero. It is characterized by cerebral ventriculomegaly, echogenic kidneys, microscopic renal tubular cysts and findings of congenital nephrosis. {ECO:0000269|PubMed:25557780, ECO:0000269|PubMed:26925547, ECO:0000269|PubMed:32051522}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Apical polarity protein that plays a central role during the epithelial-to-mesenchymal transition (EMT) at gastrulation, when newly specified mesodermal cells move inside the embryo (By similarity). Acts by promoting cell ingression, the process by which cells leave the epithelial epiblast and move inside the embryo to form a new tissue layer (By similarity). The anisotropic distribution of CRB2 and MYH10/myosin-IIB at cell edges define which cells will ingress: cells with high apical CRB2 are probably extruded from the epiblast by neighboring cells with high levels of apical MYH10/myosin-IIB (By similarity). Plays a role in the maintenance of retinal neuroepithelium organization, structural integrity, adhesion, photoreceptor polarity and retinal photoreceptor layer thickness (By similarity). May play a role in determining the length of cone photoreceptor outer segments and proliferation of late-born progenitor cells (By similarity). Also required for maintenance of the apical polarity complex during development of the cortex (By similarity). Inhibits gamma-secretase-dependent cleavage of APP and secretion of amyloid-beta peptide 40 and amyloid-beta peptide 42, and thereby inhibits gamma-secretase-dependent Notch transcription (PubMed:20299451). {ECO:0000250|UniProtKB:Q80YA8, ECO:0000269|PubMed:20299451}.
uniprot
proteins
mass_dalton
134265
uniprot
proteins
mutagenesis
MUTAGEN 1258; /note="Y->A: No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with P-1260 and E-1264."; /evidence="ECO:0000269|PubMed:20299451"; MUTAGEN 1260; /note="P->A: No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and E-1264."; /evidence="ECO:0000269|PubMed:20299451"; MUTAGEN 1264; /note="E->A: No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and P-1260."; /evidence="ECO:0000269|PubMed:20299451
uniprot
proteins
post_translational_modification
PTM: O-glucosylated by POGLUT1 at Ser-267; consists of an O-glucose trisaccharide, in which the O-glucose is elongated by the addition of two xylose residues. O-glucosylation is required for localization at the plasma membrane. {ECO:0000250|UniProtKB:Q80YA8}.; PTM: N-glycosylated. {ECO:0000269|PubMed:20299451}.
uniprot
proteins
protein_family
Crumbs protein family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15851977
uniprot
proteins
pubmed
17920587
uniprot
proteins
pubmed
20299451
uniprot
proteins
pubmed
25557779
uniprot
proteins
pubmed
25557780
uniprot
proteins
pubmed
26925547
uniprot
proteins
pubmed
27004616
uniprot
proteins
pubmed
27942854
uniprot
proteins
pubmed
29473663
uniprot
proteins
pubmed
30212996
uniprot
proteins
pubmed
30593785
uniprot
proteins
pubmed
32051522
uniprot
proteins
sequence_length
1285
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Apical cell membrane {ECO:0000250|UniProtKB:Q80YA8}; Single-pass type I membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q80YA8}. Cell junction {ECO:0000250|UniProtKB:Q80YA8}. Note=O-glucosylation is required for localization at the apical plasma membrane (By similarity). Distributed in a complex anisotropic pattern on apical cell edges: the level of CRB2 on a cell edge is inversely correlated with the level of MYH10/myosin-IIB (By similarity). {ECO:0000250|UniProtKB:Q80YA8}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 1225..1245; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins