PRIC3_MOUSE
ID PRIC3_MOUSE Reviewed; 624 AA.
AC Q80VL3; B1AVA9; Q8CAY9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Prickle planar cell polarity protein 3 {ECO:0000250|UniProtKB:O43900};
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|MGI:MGI:1859635}; Synonyms=Lmo6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Skin;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, AND
RP 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 (By
CC similarity). {ECO:0000250|UniProtKB:A8WH69,
CC ECO:0000250|UniProtKB:O43900}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69}. Cell
CC membrane {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 -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:32516135}.
CC -!- DISRUPTION PHENOTYPE: Prickle3 knockdown results in reduced respiratory
CC complex V activity, altered complex V assembly, and abnormal
CC mitochondrial morphology observed in the retina. Mutant mice exhibit
CC degeneration of retinal ganglion cells, fewer retinal neurofilaments
CC than wild-type mice, abnormalities of the retinal vasculature, and
CC significantly reduced retinal function. {ECO:0000269|PubMed:32516135}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AK037217; BAC29758.1; -; mRNA.
DR EMBL; AL672231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC049258; AAH49258.1; -; mRNA.
DR CCDS; CCDS72329.1; -.
DR RefSeq; NP_001277553.1; NM_001290624.1.
DR AlphaFoldDB; Q80VL3; -.
DR SMR; Q80VL3; -.
DR STRING; 10090.ENSMUSP00000127892; -.
DR iPTMnet; Q80VL3; -.
DR PhosphoSitePlus; Q80VL3; -.
DR PaxDb; Q80VL3; -.
DR PRIDE; Q80VL3; -.
DR ProteomicsDB; 291561; -.
DR Antibodypedia; 404; 117 antibodies from 27 providers.
DR DNASU; 54630; -.
DR Ensembl; ENSMUST00000033485; ENSMUSP00000033485; ENSMUSG00000031145.
DR GeneID; 54630; -.
DR KEGG; mmu:54630; -.
DR UCSC; uc009slu.2; mouse.
DR CTD; 4007; -.
DR MGI; MGI:1859635; Prickle3.
DR VEuPathDB; HostDB:ENSMUSG00000031145; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000153629; -.
DR HOGENOM; CLU_008937_8_1_1; -.
DR InParanoid; Q80VL3; -.
DR OMA; LPGRAMF; -.
DR OrthoDB; 997264at2759; -.
DR PhylomeDB; Q80VL3; -.
DR BioGRID-ORCS; 54630; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Prickle3; mouse.
DR PRO; PR:Q80VL3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q80VL3; protein.
DR Bgee; ENSMUSG00000031145; Expressed in ascending aorta and 219 other tissues.
DR ExpressionAtlas; Q80VL3; 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 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; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cilium biogenesis/degradation; Cytoplasm;
KW Developmental protein; LIM domain; Membrane; Metal-binding; Mitochondrion;
KW Phosphoprotein; Reference proteome; Repeat; Zinc.
FT CHAIN 1..624
FT /note="Prickle planar cell polarity protein 3"
FT /id="PRO_0000075823"
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 371..617
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..540
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 548..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 586..605
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43900"
FT CONFLICT 318
FT /note="I -> V (in Ref. 1; BAC29758)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="Q -> R (in Ref. 1; BAC29758)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 624 AA; 69727 MW; 2B4DCE249778B640 CRC64;
MFARGSRRRR SGRAPPEAED PARGQPCNSC REQCPGFLLH GWRKICQHCK CPREEHAVRT
VPVDLERIMC RLISDFQRHS ISDDDSGCAS EEYAWVPPGL KPEQVYQFFS CLPEDKVPYV
NSPGEKYRIK QLLHQLPPHD SEAQYCTALE EEEKKELRAF SQQRKRENLG RATVRIFPVT
ITGAICEECG KQIGGGDIAV FASRAGLGAC WHPQCFVCTT CQELLVDLIY FYHAGKVYCG
RHHAECLRPR CQACDEIIFS PECTEAEGRH WHMGHFCCFE CEASLGGQRY VMRQSRPHCC
ACYEARHAEY CDGCGEHIGL DQGQMAYEGQ HWHASDRCFC CSRCSRPLLG RPFLPRRGLI
FCSRACSLGS ETTAPGPGRR SWSAGTVTTP LTTSTASFSA TEGTSETASK GTCTKAEPAA
GPEEPSHFLR GAPHRHSMPE LGLRSAPEPP TESPGHPAPH PDDNAFGRQS TPRVSFRDPL
VSEGGPRRTL SAPPAQRRRP RSPPPRTPSC HHHHHHRRRR QRHRRRGSHH HHHHPGRHGH
HRCDLGSGSD SGSCSSSPSS PSSESSEDDG FFLGERIPLP PHLCRPRTTQ DTSTETFNSP
AQPLVQESHP VMPRQTRDKN CIVA
