O43900 · PRIC3_HUMAN

  • Protein
    Prickle planar cell polarity protein 3
  • Gene
    PRICKLE3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentmitochondrion
Cellular Componentplasma membrane
Molecular Functionzinc ion binding
Biological Processcell projection organization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Prickle planar cell polarity protein 3
  • Alternative names
    • LIM domain only protein 6 (LMO-6)
    • Prickle-like protein 3 (Pk3
      )
    • Triple LIM domain protein 6

Gene names

    • Name
      PRICKLE3
    • Synonyms
      LMO6

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O43900
  • Secondary accessions
    • B7Z8F2
    • O76007
    • Q53XR5

Proteomes

Organism-specific databases

Subcellular Location

Cytoplasm
Cell membrane
; Peripheral membrane protein
Mitochondrion
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).

Keywords

Disease & Variants

Involvement in disease

Leber hereditary optic neuropathy, modifier (LOAM)

  • Note
    • The gene represented in this entry acts as a disease modifier
  • Description
    A 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 also
    MIM:308905
Natural variants in LOAM
Variant IDPosition(s)ChangeDescription
VAR_08462853R>Win 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.

TypeIDPosition(s)Description
Natural variantVAR_08462853in 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
Natural variantVAR_050169343in dbSNP:rs7065449
Natural variantVAR_036188558in a breast cancer sample; somatic mutation

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.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00000758221-615UniProtPrickle planar cell polarity protein 3
Modified residue (large scale data)11PRIDEPhosphoserine
Modified residue (large scale data)122PRIDEPhosphoserine
Modified residue (large scale data)303PRIDEPhosphotyrosine
Modified residue (large scale data)381PRIDEPhosphoserine
Modified residue (large scale data)383PRIDEPhosphoserine
Modified residue (large scale data)437PRIDEPhosphoserine
Modified residue (large scale data)453PRIDEPhosphoserine
Modified residue475UniProtPhosphoserine
Modified residue (large scale data)475PRIDEPhosphoserine
Modified residue (large scale data)482PRIDEPhosphoserine
Modified residue491UniProtPhosphoserine
Modified residue (large scale data)491PRIDEPhosphoserine
Modified residue (large scale data)594PRIDEPhosphoserine

Keywords

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).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY O43900ABL1 P005192EBI-1751761, EBI-375543
BINARY O43900FYN P062412EBI-1751761, EBI-515315
BINARY O43900SULT2B1 O002043EBI-1751761, EBI-749441

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-26Disordered
Compositional bias10-26Basic and acidic residues
Domain74-182PET
Domain184-249LIM zinc-binding 1
Domain250-309LIM zinc-binding 2
Domain310-373LIM zinc-binding 3
Compositional bias396-416Polar residues
Region396-567Disordered
Compositional bias503-529Basic residues
Compositional bias537-559Polar residues
Region587-615Disordered

Sequence similarities

Belongs to the prickle / espinas / testin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

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.

  • Length
    615
  • Mass (Da)
    68,609
  • Last updated
    2002-08-02 v2
  • Checksum
    CD024365C072B052
MFARGSRRRRSGRAPPEAEDPDRGQPCNSCREQCPGFLLHGWRKICQHCKCPREEHAVHAVPVDLERIMCRLISDFQRHSISDDDSGCASEEYAWVPPGLKPEQVYQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSEAQYCTALEEEEKKELRAFSQQRKRENLGRGIVRIFPVTITGAICEECGKQIGGGDIAVFASRAGLGACWHPQCFVCTTCQELLVDLIYFYHVGKVYCGRHHAECLRPRCQACDEIIFSPECTEAEGRHWHMDHFCCFECEASLGGQRYVMRQSRPHCCACYEARHAEYCDGCGEHIGLDQGQMAYEGQHWHASDRCFCCSRCGRALLGRPFLPRRGLIFCSRACSLGSEPTAPGPSRRSWSAGPVTAPLAASTASFSAVKGASETTTKGTSTELAPATGPEEPSRFLRGAPHRHSMPELGLRSVPEPPPESPGQPNLRPDDSAFGRQSTPRVSFRDPLVSEGGPRRTLSAPPAQRRRPRSPPPRAPSRRRHHHHNHHHHHNRHPSRRRHYQCDAGSGSDSESCSSSPSSSSSESSEDDGFFLGERIPLPPHLCRPMPAQDTAMETFNSPSLSLPRDSRAGMPRQARDKNCIVA

O43900-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-68: Missing
    • 106-142: YQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSE → TRGQPSTLAVQWVHTNAHTHTHTQ

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
H0Y413H0Y413_HUMANPRICKLE3547
A0A0A0MRT7A0A0A0MRT7_HUMANPRICKLE3114
H7BZP7H7BZP7_HUMANPRICKLE3251
F5H4N2F5H4N2_HUMANPRICKLE398

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0565681-68in isoform 2
Compositional bias10-26Basic and acidic residues
Alternative sequenceVSP_056569106-142in isoform 2
Sequence conflict185in Ref. 7; AAB92357
Sequence conflict370-509in Ref. 7; AAB92357
Compositional bias396-416Polar residues
Compositional bias503-529Basic residues
Compositional bias537-559Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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