WDFY1_MOUSE
ID WDFY1_MOUSE Reviewed; 410 AA.
AC E9Q4P1; Q5DTX9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=WD repeat and FYVE domain-containing protein 1;
DE AltName: Full=WD40- and FYVE domain-containing protein 1;
GN Name=Wdfy1; Synonyms=Kiaa1435;
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 TISSUE=Brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA Gene. The
RT Complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-408, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
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 FUNCTION, AND INTERACTION WITH TLR3; TLR4 AND TICAM1.
RX PubMed=25736436; DOI=10.15252/embr.201439637;
RA Hu Y.H., Zhang Y., Jiang L.Q., Wang S., Lei C.Q., Sun M.S., Shu H.B.,
RA Liu Y.;
RT "WDFY1 mediates TLR3/4 signaling by recruiting TRIF.";
RL EMBO Rep. 16:447-455(2015).
CC -!- FUNCTION: Positively regulates TLR3- and TLR4-mediated signaling
CC pathways by bridging the interaction between TLR3 or TLR4 and TICAM1.
CC Promotes TLR3/4 ligand-induced activation of transcription factors IRF3
CC and NF-kappa-B, as well as the production of IFN-beta and inflammatory
CC cytokines (PubMed:25736436). {ECO:0000269|PubMed:25736436}.
CC -!- SUBUNIT: Binds PtdIns3P in vitro with high specificity over other
CC phosphoinositides (By similarity). Interacts (via WD repeat 2) with
CC tyrosine-phosphorylated TLR3 (via TIR domain) in response to poly(I:C)
CC (PubMed:25736436). Interacts with TLR4 in response to LPS
CC (PubMed:25736436). Interacts with TICAM1 in response to poly(I:C)
CC (PubMed:25736436). {ECO:0000250|UniProtKB:Q8IWB7,
CC ECO:0000269|PubMed:25736436}.
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000250|UniProtKB:Q8IWB7}.
CC -!- DOMAIN: The FYVE-type zinc finger domain mediates interactions with
CC phosphatidylinositol 3-phosphate in membranes of early endosomes and
CC penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched
CC membranes is substantially increased in acidic conditions. The FYVE
CC domain is required for its function in regulating TLR3 signaling.
CC {ECO:0000250|UniProtKB:Q8IWB7}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD90445.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK220391; BAD90445.1; ALT_INIT; mRNA.
DR EMBL; AC083910; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC170750; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS48296.1; -.
DR RefSeq; NP_001104749.1; NM_001111279.1.
DR AlphaFoldDB; E9Q4P1; -.
DR SMR; E9Q4P1; -.
DR STRING; 10090.ENSMUSP00000109140; -.
DR iPTMnet; E9Q4P1; -.
DR PhosphoSitePlus; E9Q4P1; -.
DR SwissPalm; E9Q4P1; -.
DR EPD; E9Q4P1; -.
DR jPOST; E9Q4P1; -.
DR MaxQB; E9Q4P1; -.
DR PaxDb; E9Q4P1; -.
DR PeptideAtlas; E9Q4P1; -.
DR PRIDE; E9Q4P1; -.
DR ProteomicsDB; 297891; -.
DR DNASU; 69368; -.
DR Ensembl; ENSMUST00000113512; ENSMUSP00000109140; ENSMUSG00000073643.
DR Ensembl; ENSMUST00000113513; ENSMUSP00000109141; ENSMUSG00000073643.
DR Ensembl; ENSMUST00000113514; ENSMUSP00000109142; ENSMUSG00000073643.
DR Ensembl; ENSMUST00000113515; ENSMUSP00000109143; ENSMUSG00000073643.
DR GeneID; 69368; -.
DR KEGG; mmu:69368; -.
DR UCSC; uc007bqu.2; mouse.
DR CTD; 57590; -.
DR MGI; MGI:1916618; Wdfy1.
DR VEuPathDB; HostDB:ENSMUSG00000073643; -.
DR eggNOG; KOG1409; Eukaryota.
DR GeneTree; ENSGT00940000157731; -.
DR HOGENOM; CLU_046919_0_0_1; -.
DR InParanoid; E9Q4P1; -.
DR OMA; RCCDPCY; -.
DR OrthoDB; 555190at2759; -.
DR PhylomeDB; E9Q4P1; -.
DR TreeFam; TF314470; -.
DR BioGRID-ORCS; 69368; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Wdfy1; mouse.
DR PRO; PR:E9Q4P1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; E9Q4P1; protein.
DR Bgee; ENSMUSG00000073643; Expressed in spermatid and 231 other tissues.
DR ExpressionAtlas; E9Q4P1; baseline and differential.
DR Genevisible; E9Q4P1; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; ISO:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034141; P:positive regulation of toll-like receptor 3 signaling pathway; IMP:UniProtKB.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; IMP:UniProtKB.
DR CDD; cd15756; FYVE_WDFY1; 1.
DR Gene3D; 2.130.10.10; -; 2.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR042234; WDFY1/WDFY2.
DR InterPro; IPR042733; WDFY1_FYVE.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46189; PTHR46189; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF00400; WD40; 4.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00320; WD40; 7.
DR SUPFAM; SSF50978; SSF50978; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
PE 1: Evidence at protein level;
KW Endosome; Metal-binding; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat; Zinc; Zinc-finger.
FT CHAIN 1..410
FT /note="WD repeat and FYVE domain-containing protein 1"
FT /id="PRO_0000434594"
FT REPEAT 22..61
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 66..105
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 112..150
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 153..192
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 197..236
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 240..279
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 364..403
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT ZN_FING 281..352
FT /note="FYVE-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 290
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 314
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 317
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 322
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 325
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 344
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT BINDING 347
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00091"
FT MOD_RES 408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:21183079"
FT CONFLICT 125
FT /note="A -> S (in Ref. 1; BAD90445)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 410 AA; 46218 MW; 17222AC356E9B074 CRC64;
MAAEIHSRPQ SSRPVLLSKI EGHQDAVTAA LLIPKEDGVI TASEDRTIRV WLKRDSGQYW
PSIYHTMASP CSAMAYHHDS RRIFVGQDNG AVMEFHVSED FNKMNFIKTY PAHQNRVSAI
IFSLAAEWVI STGHDKCVSW MCTRSGNMLG RHFFSSWASC LQYDLDTQHA FVGDYSGQIT
LLKLEQNTCS VITTLKGHEG SIACLWWDPI QRLLFSGASD NSVIMWDIGG RKGRTLLLQG
HHDRVQSLCY LQLTRQLVSC SADGGIAVWN MDVSREEAPQ WLESDSCQKC EQPFFWNIKQ
MWDTKTLGLR QHHCRKCGQA VCGKCSSKRS SYPVMGFEFQ VRVCDSCYDS IKDEDRTSLA
TFHEGKHNIS HMSMDIARGL MVTCGTDRVV KIWDMTPVVG CSLATGFSPH
