Q5IJ48 · CRUM2_HUMAN
- ProteinProtein crumbs homolog 2
- GeneCRB2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1285 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein crumbs homolog 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5IJ48
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Apical cell membrane ; Single-pass type I membrane protein
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).
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).
Isoform 2
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 1225-1245 | Helical | ||||
Sequence: VAVPAACACLLLLLLGLLSGI |
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Focal segmental glomerulosclerosis 9 (FSGS9)
- Note
- DescriptionA 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.
- See alsoMIM:616220
Natural variants in FSGS9
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084122 | 149-1285 | missing | in FSGS9; when associated in cis with M-902 and S-1064; uncertain significance | |
VAR_084123 | 498 | W>C | in FSGS9; when associated in cis with A-1076; uncertain significance; dbSNP:rs144803819 | |
VAR_073266 | 620 | C>S | in FSGS9; loss of function mutation; dbSNP:rs879255250 | |
VAR_073267 | 628 | R>C | in FSGS9; dbSNP:rs202128397 | |
VAR_073268 | 629 | C>S | in FSGS9; moderate loss of function mutation; dbSNP:rs879255252 | |
VAR_084126 | 839 | G>W | in FSGS9; when associated in cis with C-628; uncertain significance | |
VAR_084127 | 902 | T>M | in FSGS9; when associated in cis with S-1064 and 149-E--I-1285 del; uncertain significance; dbSNP:rs1463148582 | |
VAR_084128 | 1064 | P>S | in FSGS9; when associated in cis with M-902 and 149-E--I-1285 del; uncertain significance; dbSNP:rs868484209 | |
VAR_084129 | 1076 | D>A | in FSGS9; when associated in cis with C-498; uncertain significance | |
VAR_084130 | 1098-1285 | missing | in FSGS9; when associated in cis with C-1115; uncertain significance | |
VAR_084131 | 1115 | R>C | in FSGS9; when associated in cis with 1098-C--I-1285 del; uncertain significance; dbSNP:rs1219047251 | |
VAR_084132 | 1129 | C>R | in FSGS9; uncertain significance | |
VAR_084133 | 1184 | N>T | in FSGS9; uncertain significance | |
VAR_073272 | 1249 | R>Q | in FSGS9; dbSNP:rs147412276 |
Retinitis pigmentosa (RP)
- Note
- DescriptionA 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.
- See alsoMIM:268000
Natural variants in RP
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084134 | 1249 | R>G | in RP; uncertain significance; reduces protein stability and expression |
Ventriculomegaly with cystic kidney disease (VMCKD)
- Note
- DescriptionA 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.
- See alsoMIM:219730
Natural variants in VMCKD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_073269 | 633 | R>W | in VMCKD; dbSNP:rs730880377 | |
VAR_073270 | 643 | E>A | in VMCKD; when associated in cis with K-800; uncertain significance. In FSGS9; when associated in cis with K-800; uncertain significance; dbSNP:rs730880300 | |
VAR_084125 | 760-1285 | missing | in VMCKD; when associated in cis with K-800; uncertain significance | |
VAR_073271 | 800 | N>K | in VMCKD. In VMCKD; when associated in cis with A-643; uncertain significance. In FSGS9; when associated in cis with K-643; uncertain significance; dbSNP:rs765676223 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_022984 | 46 | in dbSNP:rs73571404 | |||
Sequence: P → L | ||||||
Natural variant | VAR_048974 | 90 | in dbSNP:rs2808415 | |||
Sequence: T → N | ||||||
Natural variant | VAR_022985 | 97 | ||||
Sequence: V → L | ||||||
Natural variant | VAR_022986 | 116 | in dbSNP:rs542211566 | |||
Sequence: P → L | ||||||
Natural variant | VAR_022987 | 145 | in dbSNP:rs1105223 | |||
Sequence: M → T | ||||||
Natural variant | VAR_084122 | 149-1285 | in FSGS9; when associated in cis with M-902 and S-1064; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_022988 | 159 | in dbSNP:rs1105222 | |||
Sequence: G → A | ||||||
Natural variant | VAR_022989 | 187 | ||||
Sequence: E → D | ||||||
Natural variant | VAR_022990 | 351 | in dbSNP:rs199679542 | |||
Sequence: A → T | ||||||
Natural variant | VAR_084123 | 498 | in FSGS9; when associated in cis with A-1076; uncertain significance; dbSNP:rs144803819 | |||
Sequence: W → C | ||||||
Natural variant | VAR_022991 | 534 | in dbSNP:rs370059953 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_022992 | 610 | in dbSNP:rs145286619 | |||
Sequence: R → W | ||||||
Natural variant | VAR_073266 | 620 | in FSGS9; loss of function mutation; dbSNP:rs879255250 | |||
Sequence: C → S | ||||||
Natural variant | VAR_073267 | 628 | in FSGS9; dbSNP:rs202128397 | |||
Sequence: R → C | ||||||
Natural variant | VAR_073268 | 629 | in FSGS9; moderate loss of function mutation; dbSNP:rs879255252 | |||
Sequence: C → S | ||||||
Natural variant | VAR_073269 | 633 | in VMCKD; dbSNP:rs730880377 | |||
Sequence: R → W | ||||||
Natural variant | VAR_073270 | 643 | in VMCKD; when associated in cis with K-800; uncertain significance. In FSGS9; when associated in cis with K-800; uncertain significance; dbSNP:rs730880300 | |||
Sequence: E → A | ||||||
Natural variant | VAR_084124 | 654 | found in a fetus with ventriculomegaly with cystic kidney disease; uncertain significance; dbSNP:rs372093386 | |||
Sequence: A → P | ||||||
Natural variant | VAR_061153 | 709 | in dbSNP:rs2488602 | |||
Sequence: V → A | ||||||
Natural variant | VAR_022993 | 746 | in dbSNP:rs757353722 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_084125 | 760-1285 | in VMCKD; when associated in cis with K-800; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_073271 | 800 | in VMCKD. In VMCKD; when associated in cis with A-643; uncertain significance. In FSGS9; when associated in cis with K-643; uncertain significance; dbSNP:rs765676223 | |||
Sequence: N → K | ||||||
Natural variant | VAR_084126 | 839 | in FSGS9; when associated in cis with C-628; uncertain significance | |||
Sequence: G → W | ||||||
Natural variant | VAR_084127 | 902 | in FSGS9; when associated in cis with S-1064 and 149-E--I-1285 del; uncertain significance; dbSNP:rs1463148582 | |||
Sequence: T → M | ||||||
Natural variant | VAR_084128 | 1064 | in FSGS9; when associated in cis with M-902 and 149-E--I-1285 del; uncertain significance; dbSNP:rs868484209 | |||
Sequence: P → S | ||||||
Natural variant | VAR_084129 | 1076 | in FSGS9; when associated in cis with C-498; uncertain significance | |||
Sequence: D → A | ||||||
Natural variant | VAR_084130 | 1098-1285 | in FSGS9; when associated in cis with C-1115; uncertain significance | |||
Sequence: Missing | ||||||
Natural variant | VAR_022994 | 1110 | in dbSNP:rs73571431 | |||
Sequence: T → M | ||||||
Natural variant | VAR_084131 | 1115 | in FSGS9; when associated in cis with 1098-C--I-1285 del; uncertain significance; dbSNP:rs1219047251 | |||
Sequence: R → C | ||||||
Natural variant | VAR_084132 | 1129 | in FSGS9; uncertain significance | |||
Sequence: C → R | ||||||
Natural variant | VAR_084133 | 1184 | in FSGS9; uncertain significance | |||
Sequence: N → T | ||||||
Natural variant | VAR_084134 | 1249 | in RP; uncertain significance; reduces protein stability and expression | |||
Sequence: R → G | ||||||
Natural variant | VAR_073272 | 1249 | in FSGS9; dbSNP:rs147412276 | |||
Sequence: R → Q | ||||||
Mutagenesis | 1258 | No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with P-1260 and E-1264. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 1260 | No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and E-1264. | ||||
Sequence: P → A | ||||||
Mutagenesis | 1264 | No effect on secretion of APP amyloid-beta peptide 40 and amyloid-beta peptide 42; when associated with Y-1258 and P-1260. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,773 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Signal | 1-28 | UniProt | |||||
Sequence: MALARPGTPDPQALASVLLLLLWAPALS | |||||||
Chain | PRO_0000007502 | 29-1285 | UniProt | Protein crumbs homolog 2 | |||
Sequence: LLAGTVPSEPPSACASDPCAPGTECQATESGGYTCGPMEPRGCATQPCHHGALCVPQGPDPTGFRCYCVPGFQGPRCELDIDECASRPCHHGATCRNLADRYECHCPLGYAGVTCEMEVDECASAPCLHGGSCLDGVGSFRCVCAPGYGGTRCQLDLDECQSQPCAHGGTCHDLVNGFRCDCAGTGYEGTHCEREVLECASAPCEHNASCLEGLGSFRCLCWPGYSGELCEVDEDECASSPCQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLCHCPPGFEGADCGVEVDECASRPCLNGGHCQDLPNGFQCHCPDGYAGPTCEEDVDECLSDPCLHGGTCSDTVAGYICRCPETWGGRDCSVQLTGCQGHTCPLAATCIPIFESGVHSYVCHCPPGTHGPFCGQNTTFSVMAGSPIQASVPAGGPLGLALRFRTTLPAGTLATRNDTKESLELALVAATLQATLWSYSTTVLVLRLPDLALNDGHWHQVEVVLHLATLELRLWHEGCPARLCVASGPVALASTASATPLPAGISSAQLGDATFAGCLQDVRVDGHLLLPEDLGENVLLGCERREQCRPLPCVHGGSCVDLWTHFRCDCARPHRGPTCADEIPAATFGLGGAPSSASFLLQELPGPNLTVSFLLRTRESAGLLLQFANDSAAGLTVFLSEGRIRAEVPGSPAVVLPGRWDDGLRHLVMLSFGPDQLQDLGQHVHVGGRLLAADSQPWGGPFRGCLQDLRLDGCHLPFFPLPLDNSSQPSELGGRQSWNLTAGCVSEDMCSPDPCFNGGTCLVTWNDFHCTCPANFTGPTCAQQLWCPGQPCLPPATCEEVPDGFVCVAEATFREGPPAAFSGHNASSGRLLGGLSLAFRTRDSEAWLLRAAAGALEGVWLAVRNGSLAGGVRGGHGLPGAVLPIPGPRVADGAWHRVRLAMERPAATTSRWLLWLDGAATPVALRGLASDLGFLQGPGAVRILLAENFTGCLGRVALGGLPLPLARPRPGAAPGAREHFASWPGTPAPILGCRGAPVCAPSPCLHDGACRDLFDAFACACGPGWEGPRCEAHVDPCHSAPCARGRCHTHPDGRFECRCPPGFGGPRCRLPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLPCEANPCLNGGTCRAAGGVSECICNARFSGQFCEVAKGLPLPLPFPLLEVAVPAACACLLLLLLGLLSGILAARKRRQSEGTYSPSQQEVAGARLEMDSVLKVPPEERLI | |||||||
Disulfide bond | 71↔82 | UniProt | |||||
Sequence: CATQPCHHGALC | |||||||
Disulfide bond | 76↔94 | UniProt | |||||
Sequence: CHHGALCVPQGPDPTGFRC | |||||||
Disulfide bond | 96↔105 | UniProt | |||||
Sequence: CVPGFQGPRC | |||||||
Disulfide bond | 112↔123 | UniProt | |||||
Sequence: CASRPCHHGATC | |||||||
Disulfide bond | 117↔132 | UniProt | |||||
Sequence: CHHGATCRNLADRYEC | |||||||
Disulfide bond | 134↔143 | UniProt | |||||
Sequence: CPLGYAGVTC | |||||||
Disulfide bond | 150↔161 | UniProt | |||||
Sequence: CASAPCLHGGSC | |||||||
Disulfide bond | 155↔170 | UniProt | |||||
Sequence: CLHGGSCLDGVGSFRC | |||||||
Disulfide bond | 172↔181 | UniProt | |||||
Sequence: CAPGYGGTRC | |||||||
Disulfide bond | 188↔199 | UniProt | |||||
Sequence: CQSQPCAHGGTC | |||||||
Disulfide bond | 193↔208 | UniProt | |||||
Sequence: CAHGGTCHDLVNGFRC | |||||||
Disulfide bond | 210↔220 | UniProt | |||||
Sequence: CAGTGYEGTHC | |||||||
Disulfide bond | 227↔238 | UniProt | |||||
Sequence: CASAPCEHNASC | |||||||
Disulfide bond | 232↔247 | UniProt | |||||
Sequence: CEHNASCLEGLGSFRC | |||||||
Glycosylation | 235 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 249↔258 | UniProt | |||||
Sequence: CWPGYSGELC | |||||||
Disulfide bond | 265↔276 | UniProt | |||||
Sequence: CASSPCQHGGRC | |||||||
Glycosylation | 267 | UniProt | O-linked (Glc...) serine | ||||
Sequence: S | |||||||
Disulfide bond | 270↔306 | UniProt | |||||
Sequence: CQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLC | |||||||
Disulfide bond | 308↔317 | UniProt | |||||
Sequence: CPPGFEGADC | |||||||
Disulfide bond | 324↔335 | UniProt | |||||
Sequence: CASRPCLNGGHC | |||||||
Disulfide bond | 329↔344 | UniProt | |||||
Sequence: CLNGGHCQDLPNGFQC | |||||||
Disulfide bond | 346↔355 | UniProt | |||||
Sequence: CPDGYAGPTC | |||||||
Disulfide bond | 362↔373 | UniProt | |||||
Sequence: CLSDPCLHGGTC | |||||||
Disulfide bond | 367↔382 | UniProt | |||||
Sequence: CLHGGTCSDTVAGYIC | |||||||
Disulfide bond | 384↔393 | UniProt | |||||
Sequence: CPETWGGRDC | |||||||
Disulfide bond | 400↔411 | UniProt | |||||
Sequence: CQGHTCPLAATC | |||||||
Disulfide bond | 405↔424 | UniProt | |||||
Sequence: CPLAATCIPIFESGVHSYVC | |||||||
Disulfide bond | 426↔435 | UniProt | |||||
Sequence: CPPGTHGPFC | |||||||
Glycosylation | 438 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 478 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 579↔603 | UniProt | |||||
Sequence: CLQDVRVDGHLLLPEDLGENVLLGC | |||||||
Disulfide bond | 609↔620 | UniProt | |||||
Sequence: CRPLPCVHGGSC | |||||||
Disulfide bond | 614↔629 | UniProt | |||||
Sequence: CVHGGSCVDLWTHFRC | |||||||
Disulfide bond | 631↔640 | UniProt | |||||
Sequence: CARPHRGPTC | |||||||
Glycosylation | 669 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 690 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 766↔805 | UniProt | |||||
Sequence: CLQDLRLDGCHLPFFPLPLDNSSQPSELGGRQSWNLTAGC | |||||||
Glycosylation | 786 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 800 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 811↔822 | UniProt | |||||
Sequence: CSPDPCFNGGTC | |||||||
Disulfide bond | 816↔831 | UniProt | |||||
Sequence: CFNGGTCLVTWNDFHC | |||||||
Disulfide bond | 833↔842 | UniProt | |||||
Sequence: CPANFTGPTC | |||||||
Glycosylation | 836 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 886 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 926 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Glycosylation | 1009 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1013↔1054 | UniProt | |||||
Sequence: CLGRVALGGLPLPLARPRPGAAPGAREHFASWPGTPAPILGC | |||||||
Disulfide bond | 1060↔1071 | UniProt | |||||
Sequence: CAPSPCLHDGAC | |||||||
Disulfide bond | 1065↔1080 | UniProt | |||||
Sequence: CLHDGACRDLFDAFAC | |||||||
Disulfide bond | 1082↔1091 | UniProt | |||||
Sequence: CGPGWEGPRC | |||||||
Disulfide bond | 1098↔1108 | UniProt | |||||
Sequence: CHSAPCARGRC | |||||||
Disulfide bond | 1103↔1118 | UniProt | |||||
Sequence: CARGRCHTHPDGRFEC | |||||||
Disulfide bond | 1120↔1129 | UniProt | |||||
Sequence: CPPGFGGPRC | |||||||
Disulfide bond | 1138↔1150 | UniProt | |||||
Sequence: CSLNVTCLDGSPC | |||||||
Glycosylation | 1141 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1144↔1159 | UniProt | |||||
Sequence: CLDGSPCEGGSPAANC | |||||||
Glycosylation | 1158 | UniProt | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | |||||||
Disulfide bond | 1161↔1170 | UniProt | |||||
Sequence: CLEGLAGQRC | |||||||
Disulfide bond | 1177↔1188 | UniProt | |||||
Sequence: CEANPCLNGGTC | |||||||
Disulfide bond | 1182↔1197 | UniProt | |||||
Sequence: CLNGGTCRAAGGVSEC | |||||||
Disulfide bond | 1199↔1208 | UniProt | |||||
Sequence: CNARFSGQFC | |||||||
Modified residue (large scale data) | 1274 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in glomeruli, podocytes of the glomerular capillary loops, and parietal glomerular epithelial cells in the kidney (at protein level) (PubMed:27942854, PubMed:29473663).
Expressed in retina, fetal eye and brain (PubMed:15851977).
Also expressed in kidney, RPE/choroid, and at low levels in lung, placenta, and heart (PubMed:15851977).
Expressed in retina, fetal eye and brain (PubMed:15851977).
Also expressed in kidney, RPE/choroid, and at low levels in lung, placenta, and heart (PubMed:15851977).
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-350 | Required for maximum inhibition of APP amyloid-beta peptide secretion | ||||
Sequence: MALARPGTPDPQALASVLLLLLWAPALSLLAGTVPSEPPSACASDPCAPGTECQATESGGYTCGPMEPRGCATQPCHHGALCVPQGPDPTGFRCYCVPGFQGPRCELDIDECASRPCHHGATCRNLADRYECHCPLGYAGVTCEMEVDECASAPCLHGGSCLDGVGSFRCVCAPGYGGTRCQLDLDECQSQPCAHGGTCHDLVNGFRCDCAGTGYEGTHCEREVLECASAPCEHNASCLEGLGSFRCLCWPGYSGELCEVDEDECASSPCQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLCHCPPGFEGADCGVEVDECASRPCLNGGHCQDLPNGFQCHCPDGY | ||||||
Domain | 67-106 | EGF-like 1 | ||||
Sequence: EPRGCATQPCHHGALCVPQGPDPTGFRCYCVPGFQGPRCE | ||||||
Domain | 108-144 | EGF-like 2; calcium-binding | ||||
Sequence: DIDECASRPCHHGATCRNLADRYECHCPLGYAGVTCE | ||||||
Domain | 146-182 | EGF-like 3; calcium-binding | ||||
Sequence: EVDECASAPCLHGGSCLDGVGSFRCVCAPGYGGTRCQ | ||||||
Domain | 184-221 | EGF-like 4; calcium-binding | ||||
Sequence: DLDECQSQPCAHGGTCHDLVNGFRCDCAGTGYEGTHCE | ||||||
Domain | 223-259 | EGF-like 5 | ||||
Sequence: EVLECASAPCEHNASCLEGLGSFRCLCWPGYSGELCE | ||||||
Domain | 261-318 | EGF-like 6 | ||||
Sequence: DEDECASSPCQHGGRCLQRSDPALYGGVQAAFPGAFSFRHAAGFLCHCPPGFEGADCG | ||||||
Domain | 320-356 | EGF-like 7; calcium-binding | ||||
Sequence: EVDECASRPCLNGGHCQDLPNGFQCHCPDGYAGPTCE | ||||||
Domain | 358-394 | EGF-like 8; calcium-binding | ||||
Sequence: DVDECLSDPCLHGGTCSDTVAGYICRCPETWGGRDCS | ||||||
Domain | 396-436 | EGF-like 9 | ||||
Sequence: QLTGCQGHTCPLAATCIPIFESGVHSYVCHCPPGTHGPFCG | ||||||
Domain | 431-603 | Laminin G-like 1 | ||||
Sequence: HGPFCGQNTTFSVMAGSPIQASVPAGGPLGLALRFRTTLPAGTLATRNDTKESLELALVAATLQATLWSYSTTVLVLRLPDLALNDGHWHQVEVVLHLATLELRLWHEGCPARLCVASGPVALASTASATPLPAGISSAQLGDATFAGCLQDVRVDGHLLLPEDLGENVLLGC | ||||||
Domain | 605-641 | EGF-like 10 | ||||
Sequence: RREQCRPLPCVHGGSCVDLWTHFRCDCARPHRGPTCA | ||||||
Domain | 647-805 | Laminin G-like 2 | ||||
Sequence: ATFGLGGAPSSASFLLQELPGPNLTVSFLLRTRESAGLLLQFANDSAAGLTVFLSEGRIRAEVPGSPAVVLPGRWDDGLRHLVMLSFGPDQLQDLGQHVHVGGRLLAADSQPWGGPFRGCLQDLRLDGCHLPFFPLPLDNSSQPSELGGRQSWNLTAGC | ||||||
Domain | 807-843 | EGF-like 11 | ||||
Sequence: SEDMCSPDPCFNGGTCLVTWNDFHCTCPANFTGPTCA | ||||||
Domain | 871-1054 | Laminin G-like 3 | ||||
Sequence: EATFREGPPAAFSGHNASSGRLLGGLSLAFRTRDSEAWLLRAAAGALEGVWLAVRNGSLAGGVRGGHGLPGAVLPIPGPRVADGAWHRVRLAMERPAATTSRWLLWLDGAATPVALRGLASDLGFLQGPGAVRILLAENFTGCLGRVALGGLPLPLARPRPGAAPGAREHFASWPGTPAPILGC | ||||||
Domain | 1056-1092 | EGF-like 12 | ||||
Sequence: GAPVCAPSPCLHDGACRDLFDAFACACGPGWEGPRCE | ||||||
Domain | 1094-1130 | EGF-like 13 | ||||
Sequence: HVDPCHSAPCARGRCHTHPDGRFECRCPPGFGGPRCR | ||||||
Domain | 1134-1171 | EGF-like 14 | ||||
Sequence: PSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQ | ||||||
Domain | 1173-1209 | EGF-like 15 | ||||
Sequence: PTLPCEANPCLNGGTCRAAGGVSECICNARFSGQFCE | ||||||
Region | 1249-1285 | Interaction with EPB41L5 | ||||
Sequence: RKRRQSEGTYSPSQQEVAGARLEMDSVLKVPPEERLI |
Sequence similarities
Belongs to the Crumbs protein family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 3 isoforms produced by Alternative splicing.
Q5IJ48-1
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
- Length1,285
- Mass (Da)134,265
- Last updated2006-10-17 v2
- ChecksumC5B7E9D7A91CD703
Q5IJ48-2
- Name2
- Differences from canonical
- 1131-1176: LPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLP → WDGWAGGWAANAPWGYGGAEKSARSVDESLPFPGPHVLICDMRRTV
- 1177-1285: Missing
Q5IJ48-3
- Name3
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_014737 | 1-332 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014738 | 333-351 | in isoform 3 | |||
Sequence: GHCQDLPNGFQCHCPDGYA → MAMEPGALWTFLGHLWLLA | ||||||
Sequence conflict | 430 | in Ref. 2; BAC86684 | ||||
Sequence: T → A | ||||||
Sequence conflict | 969 | in Ref. 2; AK123000/BAC86684 | ||||
Sequence: T → A | ||||||
Alternative sequence | VSP_014739 | 1131-1176 | in isoform 2 | |||
Sequence: LPVPSKECSLNVTCLDGSPCEGGSPAANCSCLEGLAGQRCQVPTLP → WDGWAGGWAANAPWGYGGAEKSARSVDESLPFPGPHVLICDMRRTV | ||||||
Sequence conflict | 1153 | in Ref. 2; BAC86684 | ||||
Sequence: G → R | ||||||
Alternative sequence | VSP_014740 | 1177-1285 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 1239 | in Ref. 2; BAC86684 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY720432 EMBL· GenBank· DDBJ | AAU14134.1 EMBL· GenBank· DDBJ | mRNA | ||
AK123000 EMBL· GenBank· DDBJ | - | mRNA | No translation available. | |
AK126775 EMBL· GenBank· DDBJ | BAC86684.1 EMBL· GenBank· DDBJ | mRNA | ||
AL445489 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL365504 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
DQ426866 EMBL· GenBank· DDBJ | ABD90532.1 EMBL· GenBank· DDBJ | mRNA |