WIPI3_MOUSE
ID WIPI3_MOUSE Reviewed; 344 AA.
AC Q9CR39; Q3U924;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 3;
DE Short=WIPI-3;
DE AltName: Full=WD repeat-containing protein 45-like;
DE Short=WDR45-like protein;
DE AltName: Full=WD repeat-containing protein 45B;
GN Name=Wdr45b; Synonyms=Wdr45l, Wipi3;
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 STRAIN=C57BL/6J, and NOD; TISSUE=Bone marrow, Embryo, Kidney, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, and Spleen;
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 [4]
RP INTERACTION WITH RB1CC1.
RX PubMed=28561066; DOI=10.1038/ncomms15637;
RA Bakula D., Mueller A.J., Zuleger T., Takacs Z., Franz-Wachtel M.,
RA Thost A.K., Brigger D., Tschan M.P., Frickey T., Robenek H., Macek B.,
RA Proikas-Cezanne T.;
RT "WIPI3 and WIPI4 beta-propellers are scaffolds for LKB1-AMPK-TSC signalling
RT circuits in the control of autophagy.";
RL Nat. Commun. 8:15637-15637(2017).
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), and
CC other phosphoinositides including PtdIns(3,5)P2, forming on membranes
CC of the endoplasmic reticulum upon activation of the upstream ULK1 and
CC PI3 kinases and is recruited at phagophore assembly sites where it
CC regulates the elongation of nascent phagophores downstream of WIPI2. In
CC the cellular response to starvation, may also function together with
CC the TSC1-TSC2 complex and RB1CC1 in the inhibition of the mTORC1
CC signaling pathway. {ECO:0000250|UniProtKB:Q5MNZ6}.
CC -!- SUBUNIT: Interacts with the TSC1-TSC2 complex; stimulated upon
CC starvation (By similarity). Interacts with RB1CC1 (PubMed:28561066).
CC Interacts with ATG2A (By similarity). {ECO:0000250|UniProtKB:Q5MNZ6,
CC ECO:0000269|PubMed:28561066}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000250|UniProtKB:Q5MNZ6}. Lysosome
CC {ECO:0000250|UniProtKB:Q5MNZ6}.
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}.
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; AK002352; BAB22031.2; -; mRNA.
DR EMBL; AK013170; BAB28689.2; -; mRNA.
DR EMBL; AK146101; BAE26902.1; -; mRNA.
DR EMBL; AK151975; BAE30843.1; -; mRNA.
DR EMBL; AK168603; BAE40470.1; -; mRNA.
DR EMBL; AK170602; BAE41906.1; -; mRNA.
DR EMBL; BC004595; AAH04595.2; -; mRNA.
DR CCDS; CCDS25773.1; -.
DR RefSeq; NP_080069.2; NM_025793.3.
DR AlphaFoldDB; Q9CR39; -.
DR SMR; Q9CR39; -.
DR BioGRID; 211756; 2.
DR STRING; 10090.ENSMUSP00000026173; -.
DR iPTMnet; Q9CR39; -.
DR PhosphoSitePlus; Q9CR39; -.
DR EPD; Q9CR39; -.
DR MaxQB; Q9CR39; -.
DR PaxDb; Q9CR39; -.
DR PeptideAtlas; Q9CR39; -.
DR PRIDE; Q9CR39; -.
DR ProteomicsDB; 299981; -.
DR Antibodypedia; 19917; 114 antibodies from 17 providers.
DR DNASU; 66840; -.
DR Ensembl; ENSMUST00000026173; ENSMUSP00000026173; ENSMUSG00000025173.
DR GeneID; 66840; -.
DR KEGG; mmu:66840; -.
DR UCSC; uc007mvt.2; mouse.
DR CTD; 56270; -.
DR MGI; MGI:1914090; Wdr45b.
DR VEuPathDB; HostDB:ENSMUSG00000025173; -.
DR eggNOG; KOG2111; Eukaryota.
DR GeneTree; ENSGT00940000157510; -.
DR InParanoid; Q9CR39; -.
DR OMA; WSFCKFQ; -.
DR OrthoDB; 966922at2759; -.
DR PhylomeDB; Q9CR39; -.
DR TreeFam; TF314859; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 66840; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Wdr45b; mouse.
DR PRO; PR:Q9CR39; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CR39; protein.
DR Bgee; ENSMUSG00000025173; Expressed in embryonic facial prominence and 66 other tissues.
DR ExpressionAtlas; Q9CR39; baseline and differential.
DR Genevisible; Q9CR39; 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:0005764; C:lysosome; ISS:UniProtKB.
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:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0062078; F:TSC1-TSC2 complex binding; ISO:MGI.
DR GO; GO:0000045; P:autophagosome assembly; 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: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 SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Autophagy; Lipid-binding; Lysosome; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..344
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 3"
FT /id="PRO_0000051446"
FT REPEAT 183..223
FT /note="WD 1"
FT REPEAT 228..267
FT /note="WD 2"
FT MOTIF 224..227
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT CONFLICT 199
FT /note="R -> S (in Ref. 1; BAE30843)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 344 AA; 38021 MW; 20B05342EF3DBC24 CRC64;
MNLLPCNPHG NGLLYAGFNQ DHGCFACGME NGFRVYNTDP LKEKEKQEFL EGGVGHVEML
FRCNYLALVG GGKKPKYPPN KVMIWDDLKK KTVIEIEFST EVKAVKLRRD RIVVVLDSMI
KVFTFTHNPH QLHVFETCYN PKGLCVLCPN SNNSLLAFPG THTGHVQLVD LASTEKPPVD
IPAHEGVLSC IALNLQGTRI ATASEKGTLI RIFDTSSGHL IQELRRGSQA ANIYCINFNQ
DASLICVSSD HGTVHIFAAE DPKRNKQSSL ASASFLPKYF SSKWSFSKFQ VPSGSPCICA
FGTEPNAVIA ICADGSYYKF LFSPKGECVR DVCAQFLEMT DDKL
