FRITZ_XENLA
ID FRITZ_XENLA Reviewed; 708 AA.
AC Q32NR9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 65.
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; Synonyms=fritz;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP SEPT2-A.
RX PubMed=20671153; DOI=10.1126/science.1191184;
RA Kim S.K., Shindo A., Park T.J., Oh E.C., Ghosh S., Gray R.S., Lewis R.A.,
RA Johnson C.A., Attie-Bittach T., Katsanis N., Wallingford J.B.;
RT "Planar cell polarity acts through septins to control collective cell
RT movement and ciliogenesis.";
RL Science 329:1337-1340(2010).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 including covergent extension during
CC gastrulation. Controls cell shape but not polarization during
CC convergent extension (PubMed:20671153). Proposed to function as core
CC component of the CPLANE (ciliogenesis and planar polarity effectors)
CC complex involved in the recruitment of peripheral IFT-A proteins to
CC basal bodies. {ECO:0000269|PubMed:20671153,
CC ECO:0000269|PubMed:27158779}.
CC -!- SUBUNIT: Interacts with sept2-a (PubMed:20671153). Interacts with intu
CC and fuz; fuz, intu and wdpcp probably form the core CPLANE
CC (ciliogenesis and planar polarity effectors) complex (By similarity).
CC {ECO:0000250|UniProtKB:Q8C456, ECO:0000269|PubMed:20671153}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20671153}.
CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:20671153}.
CC Cytoplasm, cytoskeleton, cilium basal body
CC {ECO:0000305|PubMed:27158779}. Note=Also found adjacent to the cilium
CC basal body.
CC -!- DEVELOPMENTAL STAGE: Expressed in the dorsal mesoderm of gastrulating
CC embryos. Expressed in the midline and in a punctate pattern in the
CC ciliates epidermis of stage 18 embryos. Expressed in otic vesicle,
CC nephrostome and ventral neural tube of stage 34 embryos.
CC {ECO:0000269|PubMed:20671153}.
CC -!- SIMILARITY: Belongs to the WD repeat fritz family. {ECO:0000305}.
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DR EMBL; BC108509; AAI08510.1; -; mRNA.
DR RefSeq; NP_001089828.1; NM_001096359.1.
DR RefSeq; XP_018117623.1; XM_018262134.1.
DR AlphaFoldDB; Q32NR9; -.
DR BioGRID; 592675; 1.
DR IntAct; Q32NR9; 1.
DR GeneID; 734894; -.
DR KEGG; xla:734894; -.
DR CTD; 734894; -.
DR Xenbase; XB-GENE-5820884; wdpcp.L.
DR OMA; LCFIQFA; -.
DR OrthoDB; 692945at2759; -.
DR Proteomes; UP000186698; Chromosome 5L.
DR Bgee; 734894; Expressed in testis and 18 other tissues.
DR GO; GO:0005930; C:axoneme; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR GO; GO:0060031; P:mediolateral intercalation; IMP:UniProtKB.
DR GO; GO:0016476; P:regulation of embryonic cell shape; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0032185; P:septin cytoskeleton organization; IMP:UniProtKB.
DR InterPro; IPR024511; Frtz.
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 Cell membrane; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Cytoplasm; Cytoskeleton; Membrane; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..708
FT /note="WD repeat-containing and planar cell polarity
FT effector protein fritz homolog"
FT /id="PRO_0000406197"
FT REPEAT 303..342
FT /note="WD 1"
FT REPEAT 343..382
FT /note="WD 2"
SQ SEQUENCE 708 AA; 80249 MW; 6F041C5CC8EE4B44 CRC64;
MSFCLTELYL WSLKNNLHIG DEDVGVHQYH EKKEAALHPD YGFLEEKQQW MESRGFPWIL
KNKRPEKLRD NLTELEELMQ SSECVLSKWK NKYVCQLLFG SGVLVSISLS GPQLEKVVID
RSLVGKLISN PISDAIFTDS FIILSFLKEN KLCLIQFTKK INSPDINRQL DKLSLLDLKI
SYTDIPGPKG RHLVRHLAIN SMQDLALCWW PVPVDDVKPW SPVSSEKDRA NLVLLSNSSC
KLEVLSYIRT EGDLLNACFS INQPYQICTV EHSLNSNKEP MADRFIYECV RNKIQCVSVT
RVPLRSRVIS CAVNTSEDKL VLGCEDSSLI LYESDCKVTL LAQADLLPDL IRWHPNGTIF
VVASSQGELQ IFDMALSPIR AQILAEEIEP NSTIQVCKQF NVSSTLVEMH WAAPHTLLQN
MDMTDIYNLL YLRFDGGPIG VLQLKLGAIC RGQLGAMEII SQYIRHDEVD EAVGLLSSMN
WNTMGHQCFT SMTAIVNHLL RQRLTPDREA QLEASLGTFY SPTRPLLDTI VLQYRDPISR
YARRFFHHLL RYQRFEKAFL LAVDIGARDL FMDIHYLALD KGELALAKVA RKKAEEIDAE
SINSGVEPLL PTDTLADVNE AFVDLSLIPQ VEDRILGSFP STDLGAHNSI QRNANRQLVH
IENEIGIEVY AESLDKSLPW NQECFEEDFA EENPEGIGSL KVVHFGLV
