FRITZ_MOUSE
ID FRITZ_MOUSE Reviewed; 722 AA.
AC Q8C456; Q8BRR5; Q91ZJ2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=WD repeat-containing and planar cell polarity effector protein fritz homolog;
DE Short=mFrtz;
DE AltName: Full=Homolog-13;
DE AltName: Full=WD repeat-containing and planar cell polarity effector protein;
GN Name=Wdpcp;
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 [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RX PubMed=12174196; DOI=10.1186/1471-2156-3-14;
RA Fuchs S., Resch K., Thiel C., Ulbrich M., Platzer M., Jockusch H.,
RA Schmitt-John T.;
RT "Comparative transcription map of the wobbler critical region on mouse
RT chromosome 11 and the homologous region on human chromosome 2p13-14.";
RL BMC Genet. 3:14-14(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, and Embryonic spinal cord;
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 [3]
RP INTERACTION WITH CPLANE1; INTU AND WDPCP, DISRUPTION PHENOTYPE, AND
RP FUNCTION.
RX PubMed=27158779; DOI=10.1038/ng.3558;
RA Toriyama M., Lee C., Taylor S.P., Duran I., Cohn D.H., Bruel A.L.,
RA Tabler J.M., Drew K., Kelly M.R., Kim S., Park T.J., Braun D.A.,
RA Pierquin G., Biver A., Wagner K., Malfroot A., Panigrahi I., Franco B.,
RA Al-Lami H.A., Yeung Y., Choi Y.J., Duffourd Y., Faivre L., Riviere J.B.,
RA Chen J., Liu K.J., Marcotte E.M., Hildebrandt F., Thauvin-Robinet C.,
RA Krakow D., Jackson P.K., Wallingford J.B.;
RT "The ciliopathy-associated CPLANE proteins direct basal body recruitment of
RT intraflagellar transport machinery.";
RL Nat. Genet. 48:648-656(2016).
CC -!- FUNCTION: Probable effector of the planar cell polarity signaling
CC pathway which regulates the septin cytoskeleton in both ciliogenesis
CC and collective cell movements. Together with FUZ and WDPCP proposed to
CC function as core component of the CPLANE (ciliogenesis and planar
CC polarity effectors) complex involved in the recruitment of peripheral
CC IFT-A proteins to basal bodies (PubMed:27158779).
CC {ECO:0000250|UniProtKB:Q32NR9, ECO:0000305|PubMed:27158779}.
CC -!- SUBUNIT: Interacts with CPLANE1. Interacts with INTU and FUZ; FUZ, INTU
CC and WDPCP probably form the core CPLANE (ciliogenesis and planar
CC polarity effectors) complex. {ECO:0000269|PubMed:27158779}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q32NR9}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q32NR9}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000250|UniProtKB:Q32NR9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8C456-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8C456-2; Sequence=VSP_032411;
CC -!- DISRUPTION PHENOTYPE: Y-shaped metacarpals and defects in palate and
CC tongue morphology characteristic for a PFD syndrome phenotype.
CC {ECO:0000269|PubMed:27158779}.
CC -!- SIMILARITY: Belongs to the WD repeat fritz family. {ECO:0000305}.
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DR EMBL; AF424701; AAL24810.1; -; mRNA.
DR EMBL; AK043672; BAC31614.1; -; mRNA.
DR EMBL; AK083042; BAC38742.1; -; mRNA.
DR CCDS; CCDS24467.1; -. [Q8C456-1]
DR RefSeq; NP_663400.2; NM_145425.3. [Q8C456-1]
DR PDB; 7Q3E; EM; 3.35 A; A=1-722.
DR PDBsum; 7Q3E; -.
DR AlphaFoldDB; Q8C456; -.
DR ComplexPortal; CPX-5026; CPLANE complex.
DR CORUM; Q8C456; -.
DR DIP; DIP-60612N; -.
DR IntAct; Q8C456; 2.
DR STRING; 10090.ENSMUSP00000020568; -.
DR iPTMnet; Q8C456; -.
DR PhosphoSitePlus; Q8C456; -.
DR PaxDb; Q8C456; -.
DR PRIDE; Q8C456; -.
DR ProteomicsDB; 267410; -. [Q8C456-1]
DR ProteomicsDB; 267411; -. [Q8C456-2]
DR Antibodypedia; 47438; 113 antibodies from 20 providers.
DR DNASU; 216560; -.
DR Ensembl; ENSMUST00000020568; ENSMUSP00000020568; ENSMUSG00000020319. [Q8C456-1]
DR GeneID; 216560; -.
DR KEGG; mmu:216560; -.
DR UCSC; uc007idx.1; mouse. [Q8C456-1]
DR CTD; 51057; -.
DR MGI; MGI:2144467; Wdpcp.
DR VEuPathDB; HostDB:ENSMUSG00000020319; -.
DR eggNOG; ENOG502QR8Y; Eukaryota.
DR GeneTree; ENSGT00390000016551; -.
DR HOGENOM; CLU_004917_1_0_1; -.
DR InParanoid; Q8C456; -.
DR OMA; LCFIQFA; -.
DR OrthoDB; 692945at2759; -.
DR PhylomeDB; Q8C456; -.
DR TreeFam; TF323483; -.
DR BioGRID-ORCS; 216560; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Wdpcp; mouse.
DR PRO; PR:Q8C456; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C456; protein.
DR Bgee; ENSMUSG00000020319; Expressed in fourth ventricle and 193 other tissues.
DR ExpressionAtlas; Q8C456; baseline and differential.
DR Genevisible; Q8C456; MM.
DR GO; GO:0097541; C:axonemal basal plate; IDA:MGI.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002093; P:auditory receptor cell morphogenesis; IMP:MGI.
DR GO; GO:0043010; P:camera-type eye development; IMP:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0044782; P:cilium organization; IMP:MGI.
DR GO; GO:0072359; P:circulatory system development; IMP:MGI.
DR GO; GO:0055123; P:digestive system development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0048568; P:embryonic organ development; IGI:MGI.
DR GO; GO:0001736; P:establishment of planar polarity; IC:ComplexPortal.
DR GO; GO:0045184; P:establishment of protein localization; IMP:MGI.
DR GO; GO:0042073; P:intraciliary transport; IC:ComplexPortal.
DR GO; GO:0001822; P:kidney development; IMP:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0021915; P:neural tube development; IC:ComplexPortal.
DR GO; GO:0090521; P:podocyte cell migration; IMP:MGI.
DR GO; GO:1902017; P:regulation of cilium assembly; IC:ComplexPortal.
DR GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:MGI.
DR GO; GO:0010762; P:regulation of fibroblast migration; IMP:MGI.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IMP:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:1900027; P:regulation of ruffle assembly; IMP:MGI.
DR GO; GO:0060541; P:respiratory system development; IMP:MGI.
DR GO; GO:0060021; P:roof of mouth development; IMP:MGI.
DR GO; GO:0032185; P:septin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IMP:MGI.
DR GO; GO:0043587; P:tongue morphogenesis; IMP:MGI.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024511; Frtz.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13667; PTHR13667; 1.
DR Pfam; PF11768; Frtz; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; Cilium;
KW Cilium biogenesis/degradation; Cytoplasm; Cytoskeleton; Membrane;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..722
FT /note="WD repeat-containing and planar cell polarity
FT effector protein fritz homolog"
FT /id="PRO_0000325803"
FT REPEAT 305..343
FT /note="WD 1"
FT REPEAT 344..383
FT /note="WD 2"
FT REGION 655..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12174196,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_032411"
FT CONFLICT 417
FT /note="V -> L (in Ref. 1; AAL24810)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 722 AA; 81731 MW; 19D0973861891D23 CRC64;
MSFCLTELHL WSLKSTLHIA DRDIGVYQYY DKKDPSVSAT EHGNLEEKQR LAESRDYPWT
LKNRRPEKLR DSLKELEELM QSSPCVLSKW KSKYICQLLF GSGVLVSLSL SGPQLEKVVI
DRSLVGKLIS DTISDALLTD SFIILSFLAQ NKLCFIQFTK KMDSLDGNKR LEKLSALDLK
ISYYDIPGPA NRTIDRHLAV NSTQDLVVCW WPLVSDDVWP WTPVSSEKDR ANMLLLGFTQ
GGLEVLSFVR TEWSPLDVHF GTKQPYQVFT VECSVSVDKE PMADSCIYES VRNKLHCVSV
TRIPLRSKAI SCCRNSTEDK LIVGCEDSSV ILYEAHRGVT LLAQAELRPS LISCHPSGAI
LLVGSNQGEL QIFDIALSPI NIQLLAEDYS PKETLQFKKF FDVSSSLVQM QWMAPPVVFQ
KPKRGEICDL LFLRFNKGPL GVLLFKLGIL TRGQLGLVDL ILQYIHYSEV YEAISILRSM
DWDTLGQQCL IGMGTIVNHL LRQRLTPERE AQLEASLGTF YAPTRPLLDT TILEYREPVS
KYARRLFHHL LRYKRFEKAF LLAVDIGARD LFMDIHYLAL DMGELALAEV ARRRAHDIDV
ESVSSGVELL GPLDRRDMLN EGFASSALMP EGENKFPGLL PSIGSTHMQT LQQKIPNGPS
SRWAIERRTE EEEEEEEEEE EELCTDSSGA TTWNAEGELK EDQRKQDIGD VGSLRMVHFG
LV
