WIPI4_RAT
ID WIPI4_RAT Reviewed; 309 AA.
AC Q5U2Y0;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 4;
DE Short=WIPI-4;
DE AltName: Full=WD repeat-containing protein 45;
GN Name=Wdr45; Synonyms=Wipi4;
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).
RN [2]
RP FUNCTION.
RX PubMed=21802374; DOI=10.1016/j.devcel.2011.06.024;
RA Lu Q., Yang P., Huang X., Hu W., Guo B., Wu F., Lin L., Kovacs A.L., Yu L.,
RA Zhang H.;
RT "The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of
RT omegasomes to autophagosomes.";
RL Dev. Cell 21:343-357(2011).
CC -!- FUNCTION: Component of the autophagy machinery that controls the major
CC intracellular degradation process by which cytoplasmic materials are
CC packaged into autophagosomes and delivered to lysosomes for degradation
CC (PubMed:21802374). Binds phosphatidylinositol 3-phosphate (PtdIns3P).
CC Activated by the STK11/AMPK signaling pathway upon starvation, WDR45 is
CC involved in autophagosome assembly downstream of WIPI2, regulating the
CC size of forming autophagosomes. Together with WIPI1, promotes ATG2
CC (ATG2A or ATG2B)-mediated lipid transfer by enhancing ATG2-association
CC with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes.
CC Probably recruited to membranes through its PtdIns3P activity (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y484,
CC ECO:0000269|PubMed:21802374}.
CC -!- SUBUNIT: Interacts with WIPI1. Interacts with WIPI2. Interacts with
CC ATG2A and ATG2B. Interacts with ULK1. May interact with the PRKAA1,
CC PRKAA2, PRKAB1 and PRKAG1 subunits of the AMPK kinase. May interact
CC with NUDC. {ECO:0000250|UniProtKB:Q9Y484}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000250|UniProtKB:Q9Y484}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q9Y484}. Note=Diffusely localized in the
CC cytoplasm under nutrient-rich conditions. Localizes to autophagic
CC structures during starvation-induced autophagy.
CC {ECO:0000250|UniProtKB:Q9Y484}.
CC -!- DOMAIN: The L/FRRG motif is required for recruitment to PtdIns3P.
CC {ECO:0000250|UniProtKB:Q9Y4P8}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; BC085816; AAH85816.1; -; mRNA.
DR RefSeq; NP_001013980.1; NM_001013958.1.
DR AlphaFoldDB; Q5U2Y0; -.
DR SMR; Q5U2Y0; -.
DR PaxDb; Q5U2Y0; -.
DR Ensembl; ENSRNOT00000099569; ENSRNOP00000089374; ENSRNOG00000009749.
DR GeneID; 302559; -.
DR KEGG; rno:302559; -.
DR UCSC; RGD:1359718; rat.
DR CTD; 11152; -.
DR RGD; 1359718; Wdr45.
DR eggNOG; KOG2111; Eukaryota.
DR GeneTree; ENSGT00940000155657; -.
DR HOGENOM; CLU_025895_2_2_1; -.
DR InParanoid; Q5U2Y0; -.
DR OrthoDB; 966922at2759; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR PRO; PR:Q5U2Y0; -.
DR Proteomes; UP000002494; Chromosome X.
DR Genevisible; Q5U2Y0; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; ISS:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
DR GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
DR GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR032910; WIPI4.
DR PANTHER; PTHR11227:SF44; PTHR11227:SF44; 2.
DR Pfam; PF00400; WD40; 1.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Lipid-binding; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..309
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 4"
FT /id="PRO_0000051454"
FT REPEAT 4..42
FT /note="WD 1"
FT REPEAT 184..223
FT /note="WD 2"
FT MOTIF 180..183
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
SQ SEQUENCE 309 AA; 34587 MW; 66D78153280C5ACE CRC64;
MTQQPLRGVT SLHFNQDQSC FCCAMETGVR IYNVEPLMEK GHLDHEQVGS VGLVEMLHRS
NLLALVGGGS SPKFSEISVL IWDDAREGKD SKDKLVLEFT FTKPVLAVRM RHDKIVIVLR
NRIYVYSFPD NPRKLFEFDT RDNPKGLCDL CPSLEKQLLV FPGHKCGSLQ LVSKEKLVEL
RRGTDPATLY CINFSHDSSF LCASSDKGTV HIFALKDTRL NRRSALARVG KVGPMIGQYV
DSQWSLASFT VPAESACICA FGRNTSKNVN SVIAICVDGT FHKYVFTPDG NCNREAFDVY
LDICDDDDF
