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Protein

Norrin

Gene

NDP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Activates the canonical Wnt signaling pathway through FZD4 and LRP5 coreceptor. Plays a central role in retinal vascularization by acting as a ligand for FZD4 that signals via stabilizing beta-catenin (CTNNB1) and activating LEF/TCF-mediated transcriptional programs. Acts in concert with TSPAN12 to activate FZD4 independently of the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1). May be involved in a pathway that regulates neural cell differentiation and proliferation. Possible role in neuroectodermal cell-cell interaction.

GO - Molecular functioni

  • cytokine activity Source: GO_Central
  • frizzled binding Source: BHF-UCL
  • growth factor activity Source: ProtInc
  • protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  • canonical Wnt signaling pathway Source: BHF-UCL
  • cell-cell signaling Source: ProtInc
  • cell proliferation Source: ProtInc
  • extracellular matrix-cell signaling Source: Ensembl
  • nervous system development Source: ProtInc
  • placenta development Source: Ensembl
  • positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: BHF-UCL
  • retina vasculature morphogenesis in camera-type eye Source: Ensembl
  • sensory perception of sound Source: ProtInc
  • signal transduction Source: ProtInc
  • vacuole organization Source: ProtInc
  • visual perception Source: ProtInc
  • Wnt signaling pathway Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Vision, Wnt signaling pathway

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124479-MONOMER.
SIGNORiQ00604.

Names & Taxonomyi

Protein namesi
Recommended name:
Norrin
Alternative name(s):
Norrie disease protein
X-linked exudative vitreoretinopathy 2 protein
Gene namesi
Name:NDP
Synonyms:EVR2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:7678. NDP.

Subcellular locationi

  • Secreted 1 Publication

GO - Cellular componenti

  • cell surface Source: BHF-UCL
  • extracellular matrix Source: BHF-UCL
  • extracellular space Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Norrie disease (ND)27 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionRecessive disorder characterized by very early childhood blindness due to degenerative and proliferative changes of the neuroretina. Approximately 50% of patients show some form of progressive mental disorder, often with psychotic features, and about one-third of patients develop sensorineural deafness in the second decade. In addition, some patients have more complex phenotypes, including growth failure and seizure.
See also OMIM:310600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00547813L → R in ND. 1 PublicationCorresponds to variant rs104894879dbSNPEnsembl.1
Natural variantiVAR_01604816L → P in ND. 1 Publication1
Natural variantiVAR_06399938R → C in ND and EVR2. 2 Publications1
Natural variantiVAR_00547939C → R in ND. 2 Publications1
Natural variantiVAR_06400143H → Q in ND. 1 Publication1
Natural variantiVAR_06400243H → R in ND. 1 Publication1
Natural variantiVAR_00548244Y → C in ND. 2 PublicationsCorresponds to variant rs104894870dbSNPEnsembl.1
Natural variantiVAR_06400345V → E in ND. 1 PublicationCorresponds to variant rs137852221dbSNPEnsembl.1
Natural variantiVAR_06400445V → M in ND. 1 Publication1
Natural variantiVAR_06400655C → R in ND. 1 Publication1
Natural variantiVAR_00548358K → N in ND and EVR2. 2 Publications1
Natural variantiVAR_00548460V → E in ND; reduction of protein amount in the extracellular matrix. 2 PublicationsCorresponds to variant rs104894869dbSNPEnsembl.1
Natural variantiVAR_00548561L → F in ND. 2 PublicationsCorresponds to variant rs104894880dbSNPEnsembl.1
Natural variantiVAR_00548661L → P in ND. 1 Publication1
Natural variantiVAR_00548763A → D in ND. 1 Publication1
Natural variantiVAR_00549065C → W in ND. 1 Publication1
Natural variantiVAR_00548865C → Y in ND. 2 Publications1
Natural variantiVAR_06400867G → E in ND. 1 Publication1
Natural variantiVAR_06400967G → R in ND. 1 Publication1
Natural variantiVAR_00548969C → S in ND. 1 PublicationCorresponds to variant rs104894872dbSNPEnsembl.1
Natural variantiVAR_00549174R → C in ND. 3 PublicationsCorresponds to variant rs727504031dbSNPEnsembl.1
Natural variantiVAR_00549275S → C in ND. 1 PublicationCorresponds to variant rs104894868dbSNPEnsembl.1
Natural variantiVAR_01604975S → P in ND. 1 Publication1
Natural variantiVAR_06401089F → L in ND. 1 Publication1
Natural variantiVAR_06401190R → C in ND. 1 Publication1
Natural variantiVAR_00549490R → P in ND. 1 PublicationCorresponds to variant rs104894867dbSNPEnsembl.1
Natural variantiVAR_06401292S → P in ND. 1 Publication1
Natural variantiVAR_00549594 – 96HCC → QCGL in ND. 3
Natural variantiVAR_06401395C → F in ND. 1 Publication1
Natural variantiVAR_06401495C → R in ND. 1 Publication1
Natural variantiVAR_00927596C → W in ND. 1 PublicationCorresponds to variant rs104894877dbSNPEnsembl.1
Natural variantiVAR_00549696C → Y in ND. 3 PublicationsCorresponds to variant rs104894871dbSNPEnsembl.1
Natural variantiVAR_06401597R → P in ND. 1 Publication1
Natural variantiVAR_06401698P → L in ND. 1 Publication1
Natural variantiVAR_005497101S → F in ND. 1 PublicationCorresponds to variant rs104894883dbSNPEnsembl.1
Natural variantiVAR_064018104K → N in ND. 1 Publication1
Natural variantiVAR_005498104K → Q in ND. 1 Publication1
Natural variantiVAR_016050105A → T in ND. 1 PublicationCorresponds to variant rs104894875dbSNPEnsembl.1
Natural variantiVAR_016051110C → G in ND. 1 PublicationCorresponds to variant rs104894876dbSNPEnsembl.1
Natural variantiVAR_064020110C → R in ND. 1 Publication1
Natural variantiVAR_064021112G → E in ND. 1 Publication1
Natural variantiVAR_064023118A → D in ND. 1 Publication1
Natural variantiVAR_005503121 – 123Missing in ND. 1 Publication3
Natural variantiVAR_005501121R → Q in EVR2 and ND; reduced amount of protein in the extracellular matrix. 4 Publications1
Natural variantiVAR_005502121R → W in ND and EVR2. 2 PublicationsCorresponds to variant rs104894878dbSNPEnsembl.1
Natural variantiVAR_005504123I → N in ND. 1 Publication1
Natural variantiVAR_064025126C → S in ND. 1 Publication1
Natural variantiVAR_064026128C → R in ND. 1 Publication1
Vitreoretinopathy, exudative 2 (EVR2)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA disorder of the retinal vasculature characterized by an abrupt cessation of growth of peripheral capillaries, leading to an avascular peripheral retina. This may lead to compensatory retinal neovascularization, which is thought to be induced by hypoxia from the initial avascular insult. New vessels are prone to leakage and rupture causing exudates and bleeding, followed by scarring, retinal detachment and blindness. Clinical features can be highly variable, even within the same family. Patients with mild forms of the disease are asymptomatic, and their only disease related abnormality is an arc of avascular retina in the extreme temporal periphery.
See also OMIM:305390
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06399818I → K in EVR2; the patient presented significant phenotypic heterogeneity between the two eyes. 1 Publication1
Natural variantiVAR_06399938R → C in ND and EVR2. 2 Publications1
Natural variantiVAR_00548041R → K in EVR2. 1 Publication1
Natural variantiVAR_00548142H → R in EVR2. 2 PublicationsCorresponds to variant rs104894874dbSNPEnsembl.1
Natural variantiVAR_06400554K → N in EVR2. 1 Publication1
Natural variantiVAR_00548358K → N in ND and EVR2. 2 Publications1
Natural variantiVAR_06400761L → I in EVR2. 1 Publication1
Natural variantiVAR_064017103L → V in EVR2. 1 Publication1
Natural variantiVAR_064022115R → L in EVR2. 1 Publication1
Natural variantiVAR_005499120Y → C in EVR2. 1 Publication1
Natural variantiVAR_005500121R → G in EVR2. 1
Natural variantiVAR_064024121R → L in EVR2. 1 PublicationCorresponds to variant rs137852220dbSNPEnsembl.1
Natural variantiVAR_005501121R → Q in EVR2 and ND; reduced amount of protein in the extracellular matrix. 4 Publications1
Natural variantiVAR_005502121R → W in ND and EVR2. 2 PublicationsCorresponds to variant rs104894878dbSNPEnsembl.1
Natural variantiVAR_005505124L → F in EVR2. 1 PublicationCorresponds to variant rs28933684dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi95C → A: Impairs oligomerization. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

DisGeNETi4693.
MalaCardsiNDP.
MIMi305390. phenotype.
310600. phenotype.
OpenTargetsiENSG00000124479.
Orphaneti190. Coats disease.
891. Familial exudative vitreoretinopathy.
649. Norrie disease.
91495. Persistent hyperplastic primary vitreous.
90050. Retinopathy of prematurity.
PharmGKBiPA31481.

Polymorphism and mutation databases

BioMutaiNDP.
DMDMi548342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 24Sequence analysisAdd BLAST24
ChainiPRO_000002179425 – 133NorrinAdd BLAST109

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi39 ↔ 961 Publication
Disulfide bondi55 ↔ 1101 Publication
Disulfide bondi65 ↔ 1261 Publication
Disulfide bondi69 ↔ 1281 Publication
Disulfide bondi93Interchain (with C-95)1 Publication
Disulfide bondi95Interchain (with C-93)1 Publication
Disulfide bondi131Interchain1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ00604.
PeptideAtlasiQ00604.
PRIDEiQ00604.

PTM databases

iPTMnetiQ00604.
PhosphoSitePlusiQ00604.

Expressioni

Tissue specificityi

Expressed in the outer nuclear, inner nuclear and ganglion cell layers of the retina, and in fetal and adult brain.1 Publication

Gene expression databases

BgeeiENSG00000124479.
CleanExiHS_NDP.
GenevisibleiQ00604. HS.

Organism-specific databases

HPAiHPA003095.

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Component of a complex, at least composed of TSPAN12, FZD4, LRP5/6 and norrin (NDP). Binds FZD4 with high affinity. Interacts with LRP6 (via Beta-propellers 1 and 2).1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
FZD4Q9ULV14EBI-2466352,EBI-2466380

GO - Molecular functioni

  • cytokine activity Source: GO_Central
  • frizzled binding Source: BHF-UCL
  • growth factor activity Source: ProtInc
  • protein homodimerization activity Source: BHF-UCL

Protein-protein interaction databases

BioGridi110773. 6 interactors.
IntActiQ00604. 4 interactors.
STRINGi9606.ENSP00000367301.

Structurei

Secondary structure

1133
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi37 – 48Combined sources12
Beta strandi51 – 53Combined sources3
Beta strandi58 – 67Combined sources10
Beta strandi73 – 77Combined sources5
Beta strandi80 – 83Combined sources4
Beta strandi88 – 92Combined sources5
Beta strandi94 – 110Combined sources17
Turni111 – 113Combined sources3
Beta strandi115 – 133Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MY2X-ray2.40A30-133[»]
5BPUX-ray2.40A/B/C/D/E/F25-133[»]
5BQ8X-ray2.00A/B/C/D25-133[»]
5BQBX-ray2.30A/B/C/D25-133[»]
5BQCX-ray3.00A25-133[»]
5BQEX-ray2.30A/B25-133[»]
5CL1X-ray3.80A/B31-133[»]
ProteinModelPortaliQ00604.
SMRiQ00604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini39 – 132CTCKPROSITE-ProRule annotationAdd BLAST94

Sequence similaritiesi

Contains 1 CTCK (C-terminal cystine knot-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IR8E. Eukaryota.
ENOG4111RWI. LUCA.
GeneTreeiENSGT00390000004304.
HOGENOMiHOG000030892.
HOVERGENiHBG004945.
InParanoidiQ00604.
OMAiKQPFRST.
OrthoDBiEOG091G0TKF.
PhylomeDBiQ00604.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR003064. Norrie_dis.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
[Graphical view]
PRINTSiPR01304. NORRIEDSEASE.
SMARTiSM00041. CT. 1 hit.
[Graphical view]
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q00604-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRKHVLAASF SMLSLLVIMG DTDSKTDSSF IMDSDPRRCM RHHYVDSISH
60 70 80 90 100
PLYKCSSKMV LLARCEGHCS QASRSEPLVS FSTVLKQPFR SSCHCCRPQT
110 120 130
SKLKALRLRC SGGMRLTATY RYILSCHCEE CNS
Length:133
Mass (Da):15,044
Last modified:June 1, 1994 - v1
Checksum:iD219E8B7F957286A
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_00547813L → R in ND. 1 PublicationCorresponds to variant rs104894879dbSNPEnsembl.1
Natural variantiVAR_01604816L → P in ND. 1 Publication1
Natural variantiVAR_06399818I → K in EVR2; the patient presented significant phenotypic heterogeneity between the two eyes. 1 Publication1
Natural variantiVAR_03413723D → E.Corresponds to variant rs5952410dbSNPEnsembl.1
Natural variantiVAR_06399938R → C in ND and EVR2. 2 Publications1
Natural variantiVAR_00547939C → R in ND. 2 Publications1
Natural variantiVAR_00548041R → K in EVR2. 1 Publication1
Natural variantiVAR_06400041R → S in persistent fetal vasculature syndrome. 1 Publication1
Natural variantiVAR_00548142H → R in EVR2. 2 PublicationsCorresponds to variant rs104894874dbSNPEnsembl.1
Natural variantiVAR_06400143H → Q in ND. 1 Publication1
Natural variantiVAR_06400243H → R in ND. 1 Publication1
Natural variantiVAR_00548244Y → C in ND. 2 PublicationsCorresponds to variant rs104894870dbSNPEnsembl.1
Natural variantiVAR_06400345V → E in ND. 1 PublicationCorresponds to variant rs137852221dbSNPEnsembl.1
Natural variantiVAR_06400445V → M in ND. 1 Publication1
Natural variantiVAR_06400554K → N in EVR2. 1 Publication1
Natural variantiVAR_06400655C → R in ND. 1 Publication1
Natural variantiVAR_00548358K → N in ND and EVR2. 2 Publications1
Natural variantiVAR_00548460V → E in ND; reduction of protein amount in the extracellular matrix. 2 PublicationsCorresponds to variant rs104894869dbSNPEnsembl.1
Natural variantiVAR_00548561L → F in ND. 2 PublicationsCorresponds to variant rs104894880dbSNPEnsembl.1
Natural variantiVAR_06400761L → I in EVR2. 1 Publication1
Natural variantiVAR_00548661L → P in ND. 1 Publication1
Natural variantiVAR_00548763A → D in ND. 1 Publication1
Natural variantiVAR_00549065C → W in ND. 1 Publication1
Natural variantiVAR_00548865C → Y in ND. 2 Publications1
Natural variantiVAR_06400867G → E in ND. 1 Publication1
Natural variantiVAR_06400967G → R in ND. 1 Publication1
Natural variantiVAR_00548969C → S in ND. 1 PublicationCorresponds to variant rs104894872dbSNPEnsembl.1
Natural variantiVAR_00549174R → C in ND. 3 PublicationsCorresponds to variant rs727504031dbSNPEnsembl.1
Natural variantiVAR_00549275S → C in ND. 1 PublicationCorresponds to variant rs104894868dbSNPEnsembl.1
Natural variantiVAR_01604975S → P in ND. 1 Publication1
Natural variantiVAR_06401089F → L in ND. 1 Publication1
Natural variantiVAR_06401190R → C in ND. 1 Publication1
Natural variantiVAR_00549490R → P in ND. 1 PublicationCorresponds to variant rs104894867dbSNPEnsembl.1
Natural variantiVAR_06401292S → P in ND. 1 Publication1
Natural variantiVAR_00549594 – 96HCC → QCGL in ND. 3
Natural variantiVAR_06401395C → F in ND. 1 Publication1
Natural variantiVAR_06401495C → R in ND. 1 Publication1
Natural variantiVAR_00927596C → W in ND. 1 PublicationCorresponds to variant rs104894877dbSNPEnsembl.1
Natural variantiVAR_00549696C → Y in ND. 3 PublicationsCorresponds to variant rs104894871dbSNPEnsembl.1
Natural variantiVAR_06401597R → P in ND. 1 Publication1
Natural variantiVAR_06401698P → L in ND. 1 Publication1
Natural variantiVAR_005497101S → F in ND. 1 PublicationCorresponds to variant rs104894883dbSNPEnsembl.1
Natural variantiVAR_064017103L → V in EVR2. 1 Publication1
Natural variantiVAR_064018104K → N in ND. 1 Publication1
Natural variantiVAR_005498104K → Q in ND. 1 Publication1
Natural variantiVAR_016050105A → T in ND. 1 PublicationCorresponds to variant rs104894875dbSNPEnsembl.1
Natural variantiVAR_064019108L → P in retinopathy of prematurity. 1 Publication1
Natural variantiVAR_016051110C → G in ND. 1 PublicationCorresponds to variant rs104894876dbSNPEnsembl.1
Natural variantiVAR_064020110C → R in ND. 1 Publication1
Natural variantiVAR_064021112G → E in ND. 1 Publication1
Natural variantiVAR_064022115R → L in EVR2. 1 Publication1
Natural variantiVAR_064023118A → D in ND. 1 Publication1
Natural variantiVAR_005499120Y → C in EVR2. 1 Publication1
Natural variantiVAR_005503121 – 123Missing in ND. 1 Publication3
Natural variantiVAR_005500121R → G in EVR2. 1
Natural variantiVAR_064024121R → L in EVR2. 1 PublicationCorresponds to variant rs137852220dbSNPEnsembl.1
Natural variantiVAR_005501121R → Q in EVR2 and ND; reduced amount of protein in the extracellular matrix. 4 Publications1
Natural variantiVAR_005502121R → W in ND and EVR2. 2 PublicationsCorresponds to variant rs104894878dbSNPEnsembl.1
Natural variantiVAR_005504123I → N in ND. 1 Publication1
Natural variantiVAR_005505124L → F in EVR2. 1 PublicationCorresponds to variant rs28933684dbSNPEnsembl.1
Natural variantiVAR_064025126C → S in ND. 1 Publication1
Natural variantiVAR_064026128C → R in ND. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65724 mRNA. Translation: CAA46639.1.
X65882 mRNA. Translation: CAA46713.1.
AL034370 Genomic DNA. Translation: CAA22268.1.
AK313409 mRNA. Translation: BAG36203.1.
BC029901 mRNA. Translation: AAH29901.1.
CCDSiCCDS14262.1.
PIRiA57005.
RefSeqiNP_000257.1. NM_000266.3.
UniGeneiHs.522615.

Genome annotation databases

EnsembliENST00000378062; ENSP00000367301; ENSG00000124479.
GeneIDi4693.
KEGGihsa:4693.
UCSCiuc004dga.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the NDP gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X65724 mRNA. Translation: CAA46639.1.
X65882 mRNA. Translation: CAA46713.1.
AL034370 Genomic DNA. Translation: CAA22268.1.
AK313409 mRNA. Translation: BAG36203.1.
BC029901 mRNA. Translation: AAH29901.1.
CCDSiCCDS14262.1.
PIRiA57005.
RefSeqiNP_000257.1. NM_000266.3.
UniGeneiHs.522615.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4MY2X-ray2.40A30-133[»]
5BPUX-ray2.40A/B/C/D/E/F25-133[»]
5BQ8X-ray2.00A/B/C/D25-133[»]
5BQBX-ray2.30A/B/C/D25-133[»]
5BQCX-ray3.00A25-133[»]
5BQEX-ray2.30A/B25-133[»]
5CL1X-ray3.80A/B31-133[»]
ProteinModelPortaliQ00604.
SMRiQ00604.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110773. 6 interactors.
IntActiQ00604. 4 interactors.
STRINGi9606.ENSP00000367301.

PTM databases

iPTMnetiQ00604.
PhosphoSitePlusiQ00604.

Polymorphism and mutation databases

BioMutaiNDP.
DMDMi548342.

Proteomic databases

PaxDbiQ00604.
PeptideAtlasiQ00604.
PRIDEiQ00604.

Protocols and materials databases

DNASUi4693.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378062; ENSP00000367301; ENSG00000124479.
GeneIDi4693.
KEGGihsa:4693.
UCSCiuc004dga.5. human.

Organism-specific databases

CTDi4693.
DisGeNETi4693.
GeneCardsiNDP.
GeneReviewsiNDP.
HGNCiHGNC:7678. NDP.
HPAiHPA003095.
MalaCardsiNDP.
MIMi300658. gene.
305390. phenotype.
310600. phenotype.
neXtProtiNX_Q00604.
OpenTargetsiENSG00000124479.
Orphaneti190. Coats disease.
891. Familial exudative vitreoretinopathy.
649. Norrie disease.
91495. Persistent hyperplastic primary vitreous.
90050. Retinopathy of prematurity.
PharmGKBiPA31481.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IR8E. Eukaryota.
ENOG4111RWI. LUCA.
GeneTreeiENSGT00390000004304.
HOGENOMiHOG000030892.
HOVERGENiHBG004945.
InParanoidiQ00604.
OMAiKQPFRST.
OrthoDBiEOG091G0TKF.
PhylomeDBiQ00604.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000124479-MONOMER.
SIGNORiQ00604.

Miscellaneous databases

ChiTaRSiNDP. human.
GeneWikiiNorrin.
GenomeRNAii4693.
PROiQ00604.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000124479.
CleanExiHS_NDP.
GenevisibleiQ00604. HS.

Family and domain databases

InterProiIPR006207. Cys_knot_C.
IPR006208. Glyco_hormone_CN.
IPR003064. Norrie_dis.
[Graphical view]
PfamiPF00007. Cys_knot. 1 hit.
[Graphical view]
PRINTSiPR01304. NORRIEDSEASE.
SMARTiSM00041. CT. 1 hit.
[Graphical view]
PROSITEiPS01185. CTCK_1. 1 hit.
PS01225. CTCK_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNDP_HUMAN
AccessioniPrimary (citable) accession number: Q00604
Secondary accession number(s): B2R8K6, Q5JYH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: November 2, 2016
This is version 155 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.