WDFY1_BOVIN
ID WDFY1_BOVIN Reviewed; 410 AA.
AC Q2KIY3;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=WD repeat and FYVE domain-containing protein 1;
DE AltName: Full=WD40- and FYVE domain-containing protein 1;
GN Name=WDFY1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Testis;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q8IWB7}.
CC -!- SUBUNIT: Binds PtdIns3P in vitro with high specificity over other
CC phosphoinositides. Interacts (via WD repeat 2) with tyrosine-
CC phosphorylated TLR3 (via TIR domain) in response to poly(I:C).
CC Interacts with TLR4 in response to LPS. Interacts with TICAM1 in
CC response to poly(I:C). {ECO:0000250|UniProtKB:Q8IWB7}.
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}.
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DR EMBL; BC112463; AAI12464.1; -; mRNA.
DR RefSeq; NP_001040007.1; NM_001046542.2.
DR AlphaFoldDB; Q2KIY3; -.
DR SMR; Q2KIY3; -.
DR STRING; 9913.ENSBTAP00000022552; -.
DR PaxDb; Q2KIY3; -.
DR PRIDE; Q2KIY3; -.
DR Ensembl; ENSBTAT00000022552; ENSBTAP00000022552; ENSBTAG00000016951.
DR GeneID; 614729; -.
DR KEGG; bta:614729; -.
DR CTD; 57590; -.
DR VEuPathDB; HostDB:ENSBTAG00000016951; -.
DR VGNC; VGNC:36876; WDFY1.
DR eggNOG; KOG1409; Eukaryota.
DR GeneTree; ENSGT00940000157731; -.
DR HOGENOM; CLU_046919_0_0_1; -.
DR InParanoid; Q2KIY3; -.
DR OMA; RCCDPCY; -.
DR OrthoDB; 555190at2759; -.
DR TreeFam; TF314470; -.
DR Proteomes; UP000009136; Chromosome 2.
DR Bgee; ENSBTAG00000016951; Expressed in granulosa cell and 107 other tissues.
DR GO; GO:0030054; C:cell junction; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR GO; GO:0005545; F:1-phosphatidylinositol binding; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0034145; P:positive regulation of toll-like receptor 4 signaling pathway; ISS: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 2: Evidence at transcript 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_0000244455"
FT REPEAT 22..61
FT /note="WD 1"
FT REPEAT 66..105
FT /note="WD 2"
FT REPEAT 112..150
FT /note="WD 3"
FT REPEAT 153..192
FT /note="WD 4"
FT REPEAT 197..236
FT /note="WD 5"
FT REPEAT 240..279
FT /note="WD 6"
FT REPEAT 364..403
FT /note="WD 7"
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:0000250|UniProtKB:Q8IWB7"
SQ SEQUENCE 410 AA; 46281 MW; 7B1C420C559DED90 CRC64;
MAAEIHSRPQ SSRPVLLSKI EGHQDAVTAA LLIPKEDGVI TASEDRTIRV WLKRDSGQYW
PSIYHTMASP CSAMAYHHDS RRIFVGQDNG AVMEFHVSED FNKMNFIKTY PAHQNRVTAI
IFSLATEWVI STGHDKCVSW MCTRSGNMLG RHFFSSWASC LQYDFDTQYA FVGDYSGQIT
LLKLEQSTCS VITTLKGHEG SIACLWWDPI QRLLFSGASD NSVIMWDIGG RKGRTLLLQG
HHDRVQALCY LQLTRQLVSC SSDGGIAVWN MDVSREEAPQ WLESDSCQKC EQPFFWNIKQ
MWDTKTLGLR QHHCRKCGQA VCGKCSSKRS SYPVMGFEFQ VRVCDSCYDS IKDEDRTSLA
TFHEGKHNIS HMSMDVARGL MVTCGTDRVV KIWDMTPVVG CSLATGFSPH
