O43900 · PRIC3_HUMAN
- ProteinPrickle planar cell polarity protein 3
- GenePRICKLE3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids615 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in the planar cell polarity (PCP) pathway that is essential for the polarization of epithelial cells during morphogenetic processes, including gastrulation and neurulation (By similarity).
PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity).
Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity).
Involved in the organization of the basal body (By similarity).
Involved in cilia growth and positioning (By similarity).
Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (PubMed:32516135).
PCP is maintained by two molecular modules, the global and the core modules, PRICKLE3 being part of the core module (By similarity).
Distinct complexes of the core module segregate to opposite sides of the cell, where they interact with the opposite complex in the neighboring cell at or near the adherents junctions (By similarity).
Involved in the organization of the basal body (By similarity).
Involved in cilia growth and positioning (By similarity).
Required for proper assembly, stability, and function of mitochondrial membrane ATP synthase (mitochondrial complex V) (PubMed:32516135).
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 | mitochondrion | |
Cellular Component | plasma membrane | |
Molecular Function | zinc ion binding | |
Biological Process | cell projection organization |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePrickle planar cell polarity protein 3
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO43900
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Note: Recruited by VANGL2 to anterior cell borders. This polarity is controlled by Wnt proteins (By similarity).
WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity).
WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity).
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Leber hereditary optic neuropathy, modifier (LOAM)
- Note
- DescriptionA form of Leber hereditary optic neuropathy, a mitochondrial disease resulting in bilateral painless loss of central vision due to selective degeneration of the retinal ganglion cells and their axons. The disorder shows incomplete penetrance and male predominance. Leber hereditary optic neuropathy is maternally inherited in most case and results from primary mitochondrial DNA mutations affecting the respiratory chain complexes. Mutations in modifier genes can influence disease expression. LOAM exhibits increased penetrance and earlier age of onset compared to Leber optic atrophy caused by MTND4 primary mutations, due to the action of mutations in PRICKLE3 as a modifier gene.
- See alsoMIM:308905
Natural variants in LOAM
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_084628 | 53 | R>W | in LOAM; acts as a modifier allele increasing the penetrance and expressivity of LHON-associated mtDNA mutations; reduced protein levels; does not affect localization to mitochondria; results in altered complex V stability and activity; dbSNP:rs2065470015 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_084628 | 53 | in LOAM; acts as a modifier allele increasing the penetrance and expressivity of LHON-associated mtDNA mutations; reduced protein levels; does not affect localization to mitochondria; results in altered complex V stability and activity; dbSNP:rs2065470015 | |||
Sequence: R → W | ||||||
Natural variant | VAR_050169 | 343 | in dbSNP:rs7065449 | |||
Sequence: R → C | ||||||
Natural variant | VAR_036188 | 558 | in a breast cancer sample; somatic mutation | |||
Sequence: E → D |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 588 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 chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000075822 | 1-615 | UniProt | Prickle planar cell polarity protein 3 | |||
Sequence: MFARGSRRRRSGRAPPEAEDPDRGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVHAVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRGIVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHVGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMDHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCGRALLGRPFLPRRGLIFCSRACSLGSEPTAPGPSRRSWSAGPVTAPLAASTASFSAVKGASETTTKGTSTELAPATGPEEPSRFLRGAPHRHSMPELGLRSVPEPPPESPGQPNLRPDDSAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRAPSRRRHHHHNHHHHHNRHPSRRRHYQCDAGSGSDSESCSSSPSSSSSESSEDDGFFLGERIPLPPHLCRPMPAQDTAMETFNSPSLSLPRDSRAGMPRQARDKNCIVA | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 381 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 453 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 475 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 482 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 491 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 491 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 594 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with VANGL2 via its C-terminus (By similarity).
The VANGL2-dependent membrane recruitment of PRICKLE3 is a prerequisite for its polarization (By similarity).
Interacts with WTIP. WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity).
Interacts with MT-ATP8, a component of the mitochondrial complex V (PubMed:32516135).
The VANGL2-dependent membrane recruitment of PRICKLE3 is a prerequisite for its polarization (By similarity).
Interacts with WTIP. WTIP is involved in the recruitment of PRICKLE3 to the basal body (By similarity).
Interacts with MT-ATP8, a component of the mitochondrial complex V (PubMed:32516135).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O43900 | ABL1 P00519 | 2 | EBI-1751761, EBI-375543 | |
BINARY | O43900 | FYN P06241 | 2 | EBI-1751761, EBI-515315 | |
BINARY | O43900 | SULT2B1 O00204 | 3 | EBI-1751761, EBI-749441 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-26 | Disordered | ||||
Sequence: MFARGSRRRRSGRAPPEAEDPDRGQP | ||||||
Compositional bias | 10-26 | Basic and acidic residues | ||||
Sequence: RSGRAPPEAEDPDRGQP | ||||||
Domain | 74-182 | PET | ||||
Sequence: SDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRGIVRIFPVTIT | ||||||
Domain | 184-249 | LIM zinc-binding 1 | ||||
Sequence: AICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHVGKVYCGRHHAECLRP | ||||||
Domain | 250-309 | LIM zinc-binding 2 | ||||
Sequence: RCQACDEIIFSPECTEAEGRHWHMDHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAE | ||||||
Domain | 310-373 | LIM zinc-binding 3 | ||||
Sequence: YCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCGRALLGRPFLPRRGLIFCSRACSLGSEPT | ||||||
Compositional bias | 396-416 | Polar residues | ||||
Sequence: ASFSAVKGASETTTKGTSTEL | ||||||
Region | 396-567 | Disordered | ||||
Sequence: ASFSAVKGASETTTKGTSTELAPATGPEEPSRFLRGAPHRHSMPELGLRSVPEPPPESPGQPNLRPDDSAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRAPSRRRHHHHNHHHHHNRHPSRRRHYQCDAGSGSDSESCSSSPSSSSSESSEDDGFFLGER | ||||||
Compositional bias | 503-529 | Basic residues | ||||
Sequence: PPPRAPSRRRHHHHNHHHHHNRHPSRR | ||||||
Compositional bias | 537-559 | Polar residues | ||||
Sequence: GSGSDSESCSSSPSSSSSESSED | ||||||
Region | 587-615 | Disordered | ||||
Sequence: TFNSPSLSLPRDSRAGMPRQARDKNCIVA |
Sequence similarities
Belongs to the prickle / espinas / testin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
O43900-1
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
- Length615
- Mass (Da)68,609
- Last updated2002-08-02 v2
- ChecksumCD024365C072B052
O43900-2
- Name2
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
H0Y413 | H0Y413_HUMAN | PRICKLE3 | 547 | ||
A0A0A0MRT7 | A0A0A0MRT7_HUMAN | PRICKLE3 | 114 | ||
H7BZP7 | H7BZP7_HUMAN | PRICKLE3 | 251 | ||
F5H4N2 | F5H4N2_HUMAN | PRICKLE3 | 98 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_056568 | 1-68 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 10-26 | Basic and acidic residues | ||||
Sequence: RSGRAPPEAEDPDRGQP | ||||||
Alternative sequence | VSP_056569 | 106-142 | in isoform 2 | |||
Sequence: YQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSE → TRGQPSTLAVQWVHTNAHTHTHTQ | ||||||
Sequence conflict | 185 | in Ref. 7; AAB92357 | ||||
Sequence: I → S | ||||||
Sequence conflict | 370-509 | in Ref. 7; AAB92357 | ||||
Sequence: Missing | ||||||
Compositional bias | 396-416 | Polar residues | ||||
Sequence: ASFSAVKGASETTTKGTSTEL | ||||||
Compositional bias | 503-529 | Basic residues | ||||
Sequence: PPPRAPSRRRHHHHNHHHHHNRHPSRR | ||||||
Compositional bias | 537-559 | Polar residues | ||||
Sequence: GSGSDSESCSSSPSSSSSESSED |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ011654 EMBL· GenBank· DDBJ | CAA09726.1 EMBL· GenBank· DDBJ | mRNA | ||
BT007423 EMBL· GenBank· DDBJ | AAP36091.1 EMBL· GenBank· DDBJ | mRNA | ||
AK303308 EMBL· GenBank· DDBJ | BAH13938.1 EMBL· GenBank· DDBJ | mRNA | ||
AF196779 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471224 EMBL· GenBank· DDBJ | EAW50686.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC002468 EMBL· GenBank· DDBJ | AAH02468.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016856 EMBL· GenBank· DDBJ | AAH16856.1 EMBL· GenBank· DDBJ | mRNA | ||
U93305 EMBL· GenBank· DDBJ | AAB92357.1 EMBL· GenBank· DDBJ | Genomic DNA |