FRITZ_RAT
ID FRITZ_RAT Reviewed; 726 AA.
AC B1WC10;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=WD repeat-containing and planar cell polarity effector protein fritz homolog;
DE AltName: Full=WD repeat-containing and planar cell polarity effector protein;
GN Name=Wdpcp;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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).
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q32NR9, ECO:0000250|UniProtKB:Q8C456}.
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:0000250|UniProtKB:Q8C456}.
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 -!- SIMILARITY: Belongs to the WD repeat fritz family. {ECO:0000305}.
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DR EMBL; BC161962; AAI61962.1; -; mRNA.
DR RefSeq; NP_001121009.1; NM_001127537.1.
DR AlphaFoldDB; B1WC10; -.
DR STRING; 10116.ENSRNOP00000011567; -.
DR PaxDb; B1WC10; -.
DR GeneID; 305552; -.
DR KEGG; rno:305552; -.
DR UCSC; RGD:1309501; rat.
DR CTD; 51057; -.
DR RGD; 1309501; Wdpcp.
DR eggNOG; ENOG502QR8Y; Eukaryota.
DR InParanoid; B1WC10; -.
DR OrthoDB; 692945at2759; -.
DR PhylomeDB; B1WC10; -.
DR PRO; PR:B1WC10; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0097541; C:axonemal basal plate; ISO:RGD.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002093; P:auditory receptor cell morphogenesis; ISO:RGD.
DR GO; GO:0043010; P:camera-type eye development; ISO:RGD.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0044782; P:cilium organization; ISO:RGD.
DR GO; GO:0072359; P:circulatory system development; ISO:RGD.
DR GO; GO:0055123; P:digestive system development; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0048568; P:embryonic organ development; ISO:RGD.
DR GO; GO:0045184; P:establishment of protein localization; ISO:RGD.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0090521; P:podocyte cell migration; ISO:RGD.
DR GO; GO:0016476; P:regulation of embryonic cell shape; ISS:UniProtKB.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; ISO:RGD.
DR GO; GO:0010762; P:regulation of fibroblast migration; ISO:RGD.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISO:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:1900027; P:regulation of ruffle assembly; ISO:RGD.
DR GO; GO:0060541; P:respiratory system development; ISO:RGD.
DR GO; GO:0060021; P:roof of mouth development; ISO:RGD.
DR GO; GO:0032185; P:septin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; ISO:RGD.
DR GO; GO:0043587; P:tongue morphogenesis; ISO:RGD.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR024511; Frtz.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR13667; PTHR13667; 1.
DR Pfam; PF11768; Frtz; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..726
FT /note="WD repeat-containing and planar cell polarity
FT effector protein fritz homolog"
FT /id="PRO_0000406196"
FT REPEAT 305..343
FT /note="WD 1"
FT REPEAT 344..383
FT /note="WD 2"
FT REGION 642..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 672..687
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 699..716
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 726 AA; 81910 MW; 4ADAD9735B02E641 CRC64;
MSFCLTELHL WSLKSTLHIA DRDIGVYQYY DKKDLPVSAA EHGNLEEKQR LAESRDYPWT
LKNRRPEKLR DSLKELEELM QNSQCVLCQW KSKHICQLLF GSGVLVSLSL SGPQLEKVVI
DRSLVGKLIS DTISDALLTD SFIILSFLAQ NKLCFIQFAK KMDSLDVNKR LEKLSALDYK
ISYHDIPGPA TRTVDRHLAI NSTQDLAVCW WPLLSDDAWP WTPIASEKDR ANMLLLGFTQ
GGLEVLSSVR TEWNPLDVHF GTRQPYQVFT VECSFSVDQE PMADSCIYES VRNKLHCVSV
TRIPLRSKAI SCCKNSTEDK LIVGCEDSSV ILYEAHRGVT LLAQAELMPS LISCHPSGAI
LLVGSNQGEL QVFDIALSPI NIQLLAEDCL PKETLQFNKF FDFSSSLVHM QWIAPPIVFQ
KPKRGEICDL LFLRFNRGPL GVLLFKLGVL RRGQLGLVDL IFQYIHCDEV YEAVSVLSSM
NWDTLGQQCF ISMSTIVNHL LRQRLTPERE AQLEASLGTF YAPARPLLDT TVLAYRDPVG
TYARRLFHHL LRYQRFEKAF LLAVDIGARD LFMDIHYLAL DMGELALAEV ARRRADDIDV
ESVCSGVELL GPLDRRDMLN EGFAGSALTP EGGNPFPDLL PSSGSTPKHT IQQKIPNGPS
NRRAIERKNE VMEETEEEEE EEEEAAACTD SSVATTWDAE GELREDHRRQ DTEDVGSLRM
VHFGLV
