WIPI4_MOUSE
ID WIPI4_MOUSE Reviewed; 360 AA.
AC Q91VM3; A2AEV3; A2AEV4; Q9CVF7; Q9JIG9;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 4;
DE Short=WIPI-4;
DE AltName: Full=WD repeat domain X-linked 1;
DE AltName: Full=WD repeat-containing protein 45;
GN Name=Wdr45; Synonyms=DXImx38e, Wdrx1, Wipi4;
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 [MRNA] (ISOFORM 2).
RX PubMed=10857745; DOI=10.1006/geno.2000.6173;
RA Means G.D., Toy D.Y., Baum P.R., Derry J.M.J.;
RT "A transcript map of a 2-Mb BAC contig in the proximal portion of the mouse
RT X chromosome and regional mapping of the scurfy mutation.";
RL Genomics 65:213-223(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Blastocyst, and Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary tumor;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
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
CC degradation. 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.
CC {ECO:0000250|UniProtKB:Q9Y484}.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q91VM3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q91VM3-2; Sequence=VSP_016977;
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; AF229635; AAF66949.1; -; mRNA.
DR EMBL; AK008427; BAB25662.1; -; mRNA.
DR EMBL; AK145616; BAE26542.1; -; mRNA.
DR EMBL; AL671995; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011479; AAH11479.1; -; mRNA.
DR CCDS; CCDS29970.1; -. [Q91VM3-1]
DR CCDS; CCDS72331.1; -. [Q91VM3-2]
DR RefSeq; NP_001277721.1; NM_001290792.1. [Q91VM3-1]
DR RefSeq; NP_001277723.1; NM_001290794.1. [Q91VM3-1]
DR RefSeq; NP_001277724.1; NM_001290795.1. [Q91VM3-2]
DR RefSeq; NP_758960.1; NM_172372.2. [Q91VM3-1]
DR RefSeq; XP_006527719.1; XM_006527656.1. [Q91VM3-1]
DR RefSeq; XP_017174050.1; XM_017318561.1. [Q91VM3-2]
DR AlphaFoldDB; Q91VM3; -.
DR SMR; Q91VM3; -.
DR BioGRID; 207699; 7.
DR IntAct; Q91VM3; 2.
DR STRING; 10090.ENSMUSP00000111353; -.
DR iPTMnet; Q91VM3; -.
DR PhosphoSitePlus; Q91VM3; -.
DR SwissPalm; Q91VM3; -.
DR EPD; Q91VM3; -.
DR MaxQB; Q91VM3; -.
DR PaxDb; Q91VM3; -.
DR PeptideAtlas; Q91VM3; -.
DR PRIDE; Q91VM3; -.
DR ProteomicsDB; 299770; -. [Q91VM3-1]
DR ProteomicsDB; 299771; -. [Q91VM3-2]
DR Antibodypedia; 34945; 186 antibodies from 20 providers.
DR DNASU; 54636; -.
DR Ensembl; ENSMUST00000043045; ENSMUSP00000041456; ENSMUSG00000039382. [Q91VM3-1]
DR Ensembl; ENSMUST00000115687; ENSMUSP00000111351; ENSMUSG00000039382. [Q91VM3-1]
DR Ensembl; ENSMUST00000115688; ENSMUSP00000111352; ENSMUSG00000039382. [Q91VM3-2]
DR Ensembl; ENSMUST00000115689; ENSMUSP00000111353; ENSMUSG00000039382. [Q91VM3-1]
DR GeneID; 54636; -.
DR KEGG; mmu:54636; -.
DR UCSC; uc009smb.2; mouse. [Q91VM3-1]
DR UCSC; uc009smc.2; mouse. [Q91VM3-2]
DR CTD; 11152; -.
DR MGI; MGI:1859606; Wdr45.
DR VEuPathDB; HostDB:ENSMUSG00000039382; -.
DR eggNOG; KOG2111; Eukaryota.
DR GeneTree; ENSGT00940000155657; -.
DR HOGENOM; CLU_025895_2_2_1; -.
DR InParanoid; Q91VM3; -.
DR OMA; MGTTNYL; -.
DR OrthoDB; 966922at2759; -.
DR PhylomeDB; Q91VM3; -.
DR TreeFam; TF314859; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 54636; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Wdr45; mouse.
DR PRO; PR:Q91VM3; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q91VM3; protein.
DR Bgee; ENSMUSG00000039382; Expressed in morula and 269 other tissues.
DR ExpressionAtlas; Q91VM3; baseline and differential.
DR Genevisible; Q91VM3; MM.
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:MGI.
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; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Lipid-binding;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..360
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 4"
FT /id="PRO_0000051453"
FT REPEAT 4..42
FT /note="WD 1"
FT REPEAT 190..230
FT /note="WD 2"
FT REPEAT 235..274
FT /note="WD 3"
FT MOTIF 231..234
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT VAR_SEQ 243..256
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10857745"
FT /id="VSP_016977"
SQ SEQUENCE 360 AA; 39787 MW; B17FFF96E21EDF72 CRC64;
MTQQPLRGVT SLHFNQDQSC FCCAMETGVR IYNVEPLMEK GHLDHEQVGS VGLVEMLHRS
NLLALVGGGS SPKFSEISVL IWDDAREGKD SKDKLVLEFT FTKPVLAVRM RHDKIVIVLR
NRIYVYSFPD SPRKLFEFDT RDNPKGLCDL CPSLEKQLLV FPGHKCGSLQ LVDLASTKPG
TSSAPFTINA HQSDVACVSL NQPGTVVASA SQKGTLIRLF DTQSKEKLVE LRRGTDPATL
YCINFSHDSS FLCASSDKGT VHIFALKDTR LNRRSALARV GKVGPMIGQY VDSQWSLASF
TVPAESACIC AFGRNTSKNV NSVIAICVDG TFHKYVFTPD GNCNREAFDV YLDICDDEDF
