ID   PRIC3_HUMAN             Reviewed;         615 AA.
AC   O43900; B7Z8F2; O76007; Q53XR5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2002, sequence version 2.
DT   27-MAR-2024, entry version 193.
DE   RecName: Full=Prickle planar cell polarity protein 3 {ECO:0000312|HGNC:HGNC:6645};
DE   AltName: Full=LIM domain only protein 6;
DE            Short=LMO-6;
DE   AltName: Full=Prickle-like protein 3;
DE            Short=Pk3 {ECO:0000305};
DE   AltName: Full=Triple LIM domain protein 6;
GN   Name=PRICKLE3 {ECO:0000312|HGNC:HGNC:6645}; Synonyms=LMO6;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Heart;
RA   Strom T.M., Gutwillinger N., Nyakatura G., Hellebrand H., Drescher B.,
RA   Rosenthal A., Meindl A.;
RT   "Transcription map in Xp11.23.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Thymus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15772651; DOI=10.1038/nature03440;
RA   Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA   Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA   Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA   Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA   Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA   Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA   Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA   Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA   Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA   Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA   Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA   Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA   Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA   Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA   Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA   Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA   Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA   Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA   Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA   Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA   Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA   Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA   Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA   Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA   Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA   Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA   Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA   Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA   Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA   McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA   Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA   Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA   Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA   Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA   Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA   Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA   Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA   Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA   Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA   d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA   Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA   Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA   Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA   Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA   Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA   Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA   Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA   Rogers J., Bentley D.R.;
RT   "The DNA sequence of the human X chromosome.";
RL   Nature 434:325-337(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Colon, and Kidney;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-615.
RX   PubMed=9344658; DOI=10.1006/geno.1997.4941;
RA   Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., D'Urso M.,
RA   Craig I.W.;
RT   "Sequence-based exon prediction around the synaptophysin locus reveals a
RT   gene-rich area containing novel genes in human proximal Xp.";
RL   Genomics 45:340-347(1997).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-491, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] ASP-558.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
RN   [11]
RP   VARIANT LOAM TRP-53, INVOLVEMENT IN LOAM, CHARACTERIZATION OF VARIANT LOAM
RP   TRP-53, SUBCELLULAR LOCATION, INTERACTION WITH MT-ATP8, AND FUNCTION.
RX   PubMed=32516135; DOI=10.1172/jci134965;
RA   Yu J., Liang X., Ji Y., Ai C., Liu J., Zhu L., Nie Z., Jin X., Wang C.,
RA   Zhang J., Zhao F., Mei S., Zhao X., Zhou X., Zhang M., Wang M., Huang T.,
RA   Jiang P., Guan M.X.;
RT   "PRICKLE3 linked to ATPase biogenesis manifested Leber's hereditary optic
RT   neuropathy.";
RL   J. Clin. Invest. 130:4935-4946(2020).
CC   -!- FUNCTION: Involved in the planar cell polarity (PCP) pathway that is
CC       essential for the polarization of epithelial cells during morphogenetic
CC       processes, including gastrulation and neurulation (By similarity). PCP
CC       is maintained by two molecular modules, the global and the core
CC       modules, PRICKLE3 being part of the core module (By similarity).
CC       Distinct complexes of the core module segregate to opposite sides of
CC       the cell, where they interact with the opposite complex in the
CC       neighboring cell at or near the adherents junctions (By similarity).
CC       Involved in the organization of the basal body (By similarity).
CC       Involved in cilia growth and positioning (By similarity). Required for
CC       proper assembly, stability, and function of mitochondrial membrane ATP
CC       synthase (mitochondrial complex V) (PubMed:32516135).
CC       {ECO:0000250|UniProtKB:A8WH69, ECO:0000269|PubMed:32516135}.
CC   -!- SUBUNIT: Interacts with VANGL2 via its C-terminus (By similarity). The
CC       VANGL2-dependent membrane recruitment of PRICKLE3 is a prerequisite for
CC       its polarization (By similarity). Interacts with WTIP. WTIP is involved
CC       in the recruitment of PRICKLE3 to the basal body (By similarity).
CC       Interacts with MT-ATP8, a component of the mitochondrial complex V
CC       (PubMed:32516135). {ECO:0000250|UniProtKB:A8WH69,
CC       ECO:0000269|PubMed:32516135}.
CC   -!- INTERACTION:
CC       O43900; P00519: ABL1; NbExp=2; IntAct=EBI-1751761, EBI-375543;
CC       O43900; P06241: FYN; NbExp=2; IntAct=EBI-1751761, EBI-515315;
CC       O43900; O00204: SULT2B1; NbExp=3; IntAct=EBI-1751761, EBI-749441;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69,
CC       ECO:0000269|PubMed:32516135}. Cell membrane
CC       {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:A8WH69}. Mitochondrion
CC       {ECO:0000269|PubMed:32516135}. Note=Recruited by VANGL2 to anterior
CC       cell borders. This polarity is controlled by Wnt proteins (By
CC       similarity). WTIP is involved in the recruitment of PRICKLE3 to the
CC       basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=O43900-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O43900-2; Sequence=VSP_056568, VSP_056569;
CC   -!- TISSUE SPECIFICITY: Widely expressed.
CC   -!- DISEASE: Leber hereditary optic neuropathy, modifier (LOAM)
CC       [MIM:308905]: A form of Leber hereditary optic neuropathy, a
CC       mitochondrial disease resulting in bilateral painless loss of central
CC       vision due to selective degeneration of the retinal ganglion cells and
CC       their axons. The disorder shows incomplete penetrance and male
CC       predominance. Leber hereditary optic neuropathy is maternally inherited
CC       in most case and results from primary mitochondrial DNA mutations
CC       affecting the respiratory chain complexes. Mutations in modifier genes
CC       can influence disease expression. LOAM exhibits increased penetrance
CC       and earlier age of onset compared to Leber optic atrophy caused by
CC       MTND4 primary mutations, due to the action of mutations in PRICKLE3 as
CC       a modifier gene. {ECO:0000269|PubMed:32516135}. Note=The gene
CC       represented in this entry acts as a disease modifier.
CC   -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC       {ECO:0000305}.
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DR   EMBL; AJ011654; CAA09726.1; -; mRNA.
DR   EMBL; BT007423; AAP36091.1; -; mRNA.
DR   EMBL; AK303308; BAH13938.1; -; mRNA.
DR   EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471224; EAW50686.1; -; Genomic_DNA.
DR   EMBL; BC002468; AAH02468.1; -; mRNA.
DR   EMBL; BC016856; AAH16856.1; -; mRNA.
DR   EMBL; U93305; AAB92357.1; -; Genomic_DNA.
DR   CCDS; CCDS14320.1; -. [O43900-1]
DR   RefSeq; NP_006141.2; NM_006150.4. [O43900-1]
DR   AlphaFoldDB; O43900; -.
DR   SMR; O43900; -.
DR   BioGRID; 110192; 81.
DR   IntAct; O43900; 70.
DR   STRING; 9606.ENSP00000470248; -.
DR   iPTMnet; O43900; -.
DR   PhosphoSitePlus; O43900; -.
DR   BioMuta; PRICKLE3; -.
DR   EPD; O43900; -.
DR   jPOST; O43900; -.
DR   MassIVE; O43900; -.
DR   MaxQB; O43900; -.
DR   PaxDb; 9606-ENSP00000470248; -.
DR   PeptideAtlas; O43900; -.
DR   ProteomicsDB; 49223; -. [O43900-1]
DR   ProteomicsDB; 6945; -.
DR   Pumba; O43900; -.
DR   Antibodypedia; 404; 128 antibodies from 27 providers.
DR   DNASU; 4007; -.
DR   Ensembl; ENST00000599218.6; ENSP00000470248.1; ENSG00000012211.13. [O43900-1]
DR   GeneID; 4007; -.
DR   KEGG; hsa:4007; -.
DR   MANE-Select; ENST00000599218.6; ENSP00000470248.1; NM_006150.5; NP_006141.2.
DR   UCSC; uc004dmy.2; human. [O43900-1]
DR   AGR; HGNC:6645; -.
DR   CTD; 4007; -.
DR   DisGeNET; 4007; -.
DR   GeneCards; PRICKLE3; -.
DR   HGNC; HGNC:6645; PRICKLE3.
DR   HPA; ENSG00000012211; Low tissue specificity.
DR   MalaCards; PRICKLE3; -.
DR   MIM; 300111; gene.
DR   MIM; 308905; phenotype.
DR   neXtProt; NX_O43900; -.
DR   OpenTargets; ENSG00000012211; -.
DR   PharmGKB; PA162400060; -.
DR   VEuPathDB; HostDB:ENSG00000012211; -.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00940000153629; -.
DR   HOGENOM; CLU_008937_8_1_1; -.
DR   InParanoid; O43900; -.
DR   OMA; GRHRCDL; -.
DR   OrthoDB; 370973at2759; -.
DR   PhylomeDB; O43900; -.
DR   TreeFam; TF313265; -.
DR   PathwayCommons; O43900; -.
DR   SignaLink; O43900; -.
DR   BioGRID-ORCS; 4007; 12 hits in 783 CRISPR screens.
DR   ChiTaRS; PRICKLE3; human.
DR   GenomeRNAi; 4007; -.
DR   Pharos; O43900; Tbio.
DR   PRO; PR:O43900; -.
DR   Proteomes; UP000005640; Chromosome X.
DR   RNAct; O43900; Protein.
DR   Bgee; ENSG00000012211; Expressed in lower esophagus mucosa and 96 other cell types or tissues.
DR   ExpressionAtlas; O43900; baseline and differential.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR   CDD; cd09415; LIM1_Prickle; 1.
DR   CDD; cd09418; LIM2_Prickle; 1.
DR   CDD; cd09420; LIM3_Prickle; 1.
DR   CDD; cd09827; PET_Prickle; 1.
DR   Gene3D; 2.10.110.10; Cysteine Rich Protein; 3.
DR   InterPro; IPR033725; LIM1_prickle.
DR   InterPro; IPR033726; LIM2_prickle.
DR   InterPro; IPR033727; LIM3_prickle.
DR   InterPro; IPR010442; PET_domain.
DR   InterPro; IPR033723; PET_prickle.
DR   InterPro; IPR047120; Pk/Esn/Tes.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24211; LIM DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR24211:SF19; PRICKLE PLANAR CELL POLARITY PROTEIN 3; 1.
DR   Pfam; PF00412; LIM; 3.
DR   Pfam; PF06297; PET; 1.
DR   SMART; SM00132; LIM; 3.
DR   SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 2.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR   PROSITE; PS51303; PET; 1.
DR   Genevisible; O43900; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cilium biogenesis/degradation;
KW   Cytoplasm; Developmental protein; Disease variant;
KW   Leber hereditary optic neuropathy; LIM domain; Membrane; Metal-binding;
KW   Mitochondrion; Phosphoprotein; Primary mitochondrial disease;
KW   Reference proteome; Repeat; Zinc.
FT   CHAIN           1..615
FT                   /note="Prickle planar cell polarity protein 3"
FT                   /id="PRO_0000075822"
FT   DOMAIN          74..182
FT                   /note="PET"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT   DOMAIN          184..249
FT                   /note="LIM zinc-binding 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          250..309
FT                   /note="LIM zinc-binding 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   DOMAIN          310..373
FT                   /note="LIM zinc-binding 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          396..567
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          587..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..416
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..529
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        537..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         475
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         491
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         1..68
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056568"
FT   VAR_SEQ         106..142
FT                   /note="YQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSE -> TRGQPSTLAVQ
FT                   WVHTNAHTHTHTQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056569"
FT   VARIANT         53
FT                   /note="R -> W (in LOAM; acts as a modifier allele
FT                   increasing the penetrance and expressivity of
FT                   LHON-associated mtDNA mutations; reduced protein levels;
FT                   does not affect localization to mitochondria; results in
FT                   altered complex V stability and activity)"
FT                   /evidence="ECO:0000269|PubMed:32516135"
FT                   /id="VAR_084628"
FT   VARIANT         343
FT                   /note="R -> C (in dbSNP:rs7065449)"
FT                   /id="VAR_050169"
FT   VARIANT         558
FT                   /note="E -> D (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036188"
FT   CONFLICT        185
FT                   /note="I -> S (in Ref. 7; AAB92357)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        370..509
FT                   /note="Missing (in Ref. 7; AAB92357)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   615 AA;  68609 MW;  CD024365C072B052 CRC64;
     MFARGSRRRR SGRAPPEAED PDRGQPCNSC REQCPGFLLH GWRKICQHCK CPREEHAVHA
     VPVDLERIMC RLISDFQRHS ISDDDSGCAS EEYAWVPPGL KPEQVYQFFS CLPEDKVPYV
     NSPGEKYRIK QLLHQLPPHD SEAQYCTALE EEEKKELRAF SQQRKRENLG RGIVRIFPVT
     ITGAICEECG KQIGGGDIAV FASRAGLGAC WHPQCFVCTT CQELLVDLIY FYHVGKVYCG
     RHHAECLRPR CQACDEIIFS PECTEAEGRH WHMDHFCCFE CEASLGGQRY VMRQSRPHCC
     ACYEARHAEY CDGCGEHIGL DQGQMAYEGQ HWHASDRCFC CSRCGRALLG RPFLPRRGLI
     FCSRACSLGS EPTAPGPSRR SWSAGPVTAP LAASTASFSA VKGASETTTK GTSTELAPAT
     GPEEPSRFLR GAPHRHSMPE LGLRSVPEPP PESPGQPNLR PDDSAFGRQS TPRVSFRDPL
     VSEGGPRRTL SAPPAQRRRP RSPPPRAPSR RRHHHHNHHH HHNRHPSRRR HYQCDAGSGS
     DSESCSSSPS SSSSESSEDD GFFLGERIPL PPHLCRPMPA QDTAMETFNS PSLSLPRDSR
     AGMPRQARDK NCIVA
//