WIPI1_HUMAN
ID WIPI1_HUMAN Reviewed; 446 AA.
AC Q5MNZ9; Q8IXM5; Q9NWF8;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 3.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 1;
DE Short=WIPI-1;
DE AltName: Full=Atg18 protein homolog;
DE AltName: Full=WD40 repeat protein interacting with phosphoinositides of 49 kDa;
DE Short=WIPI 49 kDa;
GN Name=WIPI1; Synonyms=WIPI49;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INTERACTION WITH AR; ESR1 AND ESR2, SUBCELLULAR LOCATION, AND VARIANT
RP ILE-31.
RC TISSUE=Testis;
RX PubMed=15602573; DOI=10.1038/sj.onc.1208331;
RA Proikas-Cezanne T., Waddell S., Gaugel A., Frickey T., Lupas A.,
RA Nordheim A.;
RT "WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein family,
RT is aberrantly expressed in human cancer and is linked to starvation-induced
RT autophagy.";
RL Oncogene 23:9314-9325(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ILE-31.
RC TISSUE=Skin;
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, FUNCTION, SUBCELLULAR LOCATION, BINDING TO
RP PHOSPHOINOSITIDES, AND MUTAGENESIS OF 226-ARG-ARG-227.
RX PubMed=15020712; DOI=10.1091/mbc.e03-10-0732;
RA Jeffries T.R., Dove S.K., Michell R.H., Parker P.J.;
RT "PtdIns-specific MPR pathway association of a novel WD40 repeat protein,
RT WIPI49.";
RL Mol. Biol. Cell 15:2652-2663(2004).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=17618624; DOI=10.1016/j.febslet.2007.06.040;
RA Proikas-Cezanne T., Ruckerbauer S., Stierhof Y.D., Berg C., Nordheim A.;
RT "Human WIPI-1 puncta-formation: a novel assay to assess mammalian
RT autophagy.";
RL FEBS Lett. 581:3396-3404(2007).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19590496; DOI=10.1038/emboj.2009.159;
RA Vergne I., Roberts E., Elmaoued R.A., Tosch V., Delgado M.A.,
RA Proikas-Cezanne T., Laporte J., Deretic V.;
RT "Control of autophagy initiation by phosphoinositide 3-phosphatase Jumpy.";
RL EMBO J. 28:2244-2258(2009).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20639694; DOI=10.4161/auto.6.6.12709;
RA Itakura E., Mizushima N.;
RT "Characterization of autophagosome formation site by a hierarchical
RT analysis of mammalian Atg proteins.";
RL Autophagy 6:764-776(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20114074; DOI=10.1016/j.cellsig.2010.01.015;
RA Grotemeier A., Alers S., Pfisterer S.G., Paasch F., Daubrawa M.,
RA Dieterle A., Viollet B., Wesselborg S., Proikas-Cezanne T., Stork B.;
RT "AMPK-independent induction of autophagy by cytosolic Ca2+ increase.";
RL Cell. Signal. 22:914-925(2010).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, AND MICROTUBULE-BINDING.
RX PubMed=20484055; DOI=10.1074/jbc.m109.091553;
RA Geeraert C., Ratier A., Pfisterer S.G., Perdiz D., Cantaloube I.,
RA Rouault A., Pattingre S., Proikas-Cezanne T., Codogno P., Pous C.;
RT "Starvation-induced hyperacetylation of tubulin is required for the
RT stimulation of autophagy by nutrient deprivation.";
RL J. Biol. Chem. 285:24184-24194(2010).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=20529838; DOI=10.1074/jbc.m110.118125;
RA Gao P., Bauvy C., Souquere S., Tonelli G., Liu L., Zhu Y., Qiao Z.,
RA Bakula D., Proikas-Cezanne T., Pierron G., Codogno P., Chen Q.,
RA Mehrpour M.;
RT "The Bcl-2 homology domain 3 mimetic gossypol induces both Beclin 1-
RT dependent and Beclin 1-independent cytoprotective autophagy in cancer
RT cells.";
RL J. Biol. Chem. 285:25570-25581(2010).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=20059746; DOI=10.1111/j.1600-0854.2010.01034.x;
RA Taguchi-Atarashi N., Hamasaki M., Matsunaga K., Omori H., Ktistakis N.T.,
RA Yoshimori T., Noda T.;
RT "Modulation of local PtdIns3P levels by the PI phosphatase MTMR3 regulates
RT constitutive autophagy.";
RL Traffic 11:468-478(2010).
RN [13]
RP FUNCTION.
RX PubMed=21317285; DOI=10.1074/jbc.m110.200543;
RA Ho H., Kapadia R., Al-Tahan S., Ahmad S., Ganesan A.K.;
RT "WIPI1 coordinates melanogenic gene transcription and melanosome formation
RT via TORC1 inhibition.";
RL J. Biol. Chem. 286:12509-12523(2011).
RN [14]
RP SUBCELLULAR LOCATION.
RX PubMed=21564513; DOI=10.1111/j.1582-4934.2011.01339.x;
RA Proikas-Cezanne T., Robenek H.;
RT "Freeze-fracture replica immunolabelling reveals human WIPI-1 and WIPI-2 as
RT membrane proteins of autophagosomes.";
RL J. Cell. Mol. Med. 15:2007-2010(2011).
RN [15]
RP REGULATION BY CALCIUM-SIGNALING, AND SUBCELLULAR LOCATION.
RX PubMed=21896713; DOI=10.1124/mol.111.071761;
RA Pfisterer S.G., Mauthe M., Codogno P., Proikas-Cezanne T.;
RT "Ca2+/calmodulin-dependent kinase (CaMK) signaling via CaMKI and AMP-
RT activated protein kinase contributes to the regulation of WIPI-1 at the
RT onset of autophagy.";
RL Mol. Pharmacol. 80:1066-1075(2011).
RN [16]
RP FUNCTION.
RX PubMed=22829830; DOI=10.1155/2012/179207;
RA Mauthe M., Yu W., Krut O., Kronke M., Gotz F., Robenek H.,
RA Proikas-Cezanne T.;
RT "WIPI-1 positive autophagosome-like vesicles entrap pathogenic
RT Staphylococcus aureus for lysosomal degradation.";
RL Int. J. Cell Biol. 2012:179207-179207(2012).
RN [17]
RP FUNCTION, DOMAIN, PIP2-BINDING, AND MUTAGENESIS OF SER-203; SER-205;
RP GLY-208; THR-209; ARG-212; ARG-226; ARG-227; GLY-228; SER-251; THR-255 AND
RP HIS-257.
RX PubMed=23088497; DOI=10.1186/1750-2187-7-16;
RA Gaugel A., Bakula D., Hoffmann A., Proikas-Cezanne T.;
RT "Defining regulatory and phosphoinositide-binding sites in the human WIPI-1
RT beta-propeller responsible for autophagosomal membrane localization
RT downstream of mTORC1 inhibition.";
RL J. Mol. Signal. 7:16-16(2012).
RN [18]
RP FUNCTION, PHOSPHOINOSITIDES-BINDING, INTERACTION WITH ATG16L1; NUDC; WIPI2
RP AND WDR45, AND SUBCELLULAR LOCATION.
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).
RN [19]
RP FUNCTION.
RX PubMed=31271352; DOI=10.7554/elife.45777;
RA Maeda S., Otomo C., Otomo T.;
RT "The autophagic membrane tether ATG2A transfers lipids between membranes.";
RL Elife 8:0-0(2019).
RN [20]
RP SUBCELLULAR LOCATION, AND PHOSPHOINOSITIDES-BINDING.
RX PubMed=33499712; DOI=10.1080/15548627.2021.1874133;
RA Kojima W., Yamano K., Kosako H., Imai K., Kikuchi R., Tanaka K.,
RA Matsuda N.;
RT "Mammalian BCAS3 and C16orf70 associate with the phagophore assembly site
RT in response to selective and non-selective autophagy.";
RL Autophagy 1:1-26(2021).
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:15602573, PubMed:20114074, PubMed:20484055, PubMed:20639694,
CC PubMed:23088497, PubMed:28561066, PubMed:31271352). Plays an important
CC role in starvation- and calcium-mediated autophagy, as well as in
CC mitophagy (PubMed:28561066). Functions downstream of the ULK1 and PI3-
CC kinases that produce phosphatidylinositol 3-phosphate (PtdIns3P) on
CC membranes of the endoplasmic reticulum once activated
CC (PubMed:28561066). Binds phosphatidylinositol 3-phosphate (PtdIns3P),
CC and maybe other phosphoinositides including PtdIns3,5P2 and PtdIns5P,
CC and is recruited to phagophore assembly sites at the endoplasmic
CC reticulum membranes (PubMed:28561066, PubMed:31271352,
CC PubMed:33499712). There, it assists WIPI2 in the recruitment of ATG12-
CC ATG5-ATG16L1, a complex that directly controls the elongation of the
CC nascent autophagosomal membrane (PubMed:28561066). Together with
CC WDR45/WIPI4, promotes ATG2 (ATG2A or ATG2B)-mediated lipid transfer by
CC enhancing ATG2-association with phosphatidylinositol 3-monophosphate
CC (PI3P)-containing membranes (PubMed:31271352). Involved in xenophagy of
CC Staphylococcus aureus (PubMed:22829830). Invading S.aureus cells become
CC entrapped in autophagosome-like WIPI1 positive vesicles targeted for
CC lysosomal degradation (PubMed:22829830). Also plays a distinct role in
CC controlling the transcription of melanogenic enzymes and melanosome
CC maturation, a process that is distinct from starvation-induced
CC autophagy (PubMed:21317285). May also regulate the trafficking of
CC proteins involved in the mannose-6-phosphate receptor (MPR) recycling
CC pathway (PubMed:15020712). {ECO:0000269|PubMed:15020712,
CC ECO:0000269|PubMed:15602573, ECO:0000269|PubMed:20114074,
CC ECO:0000269|PubMed:20484055, ECO:0000269|PubMed:20639694,
CC ECO:0000269|PubMed:21317285, ECO:0000269|PubMed:22829830,
CC ECO:0000269|PubMed:23088497, ECO:0000269|PubMed:28561066,
CC ECO:0000269|PubMed:31271352, ECO:0000269|PubMed:33499712}.
CC -!- SUBUNIT: Interacts with androgen receptor (AR) and the estrogen
CC receptors ESR1 and ESR2 (PubMed:15602573). Interacts with WIPI2
CC (PubMed:28561066). Interacts with WDR45 (PubMed:28561066). Interacts
CC with ATG16L1 (PubMed:28561066). May interact with NUDC
CC (PubMed:28561066). {ECO:0000269|PubMed:15602573,
CC ECO:0000269|PubMed:28561066}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Endosome.
CC Cytoplasmic vesicle, clathrin-coated vesicle. Preautophagosomal
CC structure membrane {ECO:0000269|PubMed:28561066,
CC ECO:0000269|PubMed:33499712}; Peripheral membrane protein. Cytoplasm,
CC cytoskeleton. Note=Trans elements of the Golgi and peripheral
CC endosomes. Dynamically cycles through these compartments and is
CC susceptible to conditions that modulate membrane flux. Enriched in
CC clathrin-coated vesicles. Upon starvation-induced autophagy,
CC accumulates at subcellular structures in the cytoplasm: enlarged
CC vesicular and lasso-like structures, and large cup-shaped structures
CC predominantly around the nucleus. Recruitment to autophagic membranes
CC is controlled by MTMR14. Labile microtubules specifically recruit
CC markers of autophagosome formation like WIPI1, whereas mature
CC autophagosomes may bind to stable microtubules.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=WIPI-1 alpha;
CC IsoId=Q5MNZ9-1; Sequence=Displayed;
CC Name=2; Synonyms=WIPI-1 beta;
CC IsoId=Q5MNZ9-2; Sequence=VSP_016966;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC skeletal muscle, heart, testis, pancreas and placenta. Highly expressed
CC in G361, Sk-mel-28, Sk-mel-13, WM852 and WM451 cells. Up-regulated in a
CC variety of tumor tissues. {ECO:0000269|PubMed:15602573}.
CC -!- DOMAIN: The N-terminus might form a beta-propeller domain involved in
CC specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2),
CC leading to the association of the protein to the membrane. Association
CC to the membrane can also occur through binding to phosphatidylinositol
CC 3-monophosphate (PI3P). {ECO:0000269|PubMed:23088497}.
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; AY691424; AAV80760.1; -; mRNA.
DR EMBL; AK000917; BAA91423.1; -; mRNA.
DR EMBL; AC007780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC039867; AAH39867.1; -; mRNA.
DR CCDS; CCDS11677.1; -. [Q5MNZ9-1]
DR RefSeq; NP_001307701.1; NM_001320772.1.
DR RefSeq; NP_060453.3; NM_017983.6. [Q5MNZ9-1]
DR AlphaFoldDB; Q5MNZ9; -.
DR SMR; Q5MNZ9; -.
DR BioGRID; 120380; 52.
DR IntAct; Q5MNZ9; 11.
DR STRING; 9606.ENSP00000262139; -.
DR GlyGen; Q5MNZ9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q5MNZ9; -.
DR PhosphoSitePlus; Q5MNZ9; -.
DR BioMuta; WIPI1; -.
DR DMDM; 146291100; -.
DR EPD; Q5MNZ9; -.
DR jPOST; Q5MNZ9; -.
DR MassIVE; Q5MNZ9; -.
DR MaxQB; Q5MNZ9; -.
DR PaxDb; Q5MNZ9; -.
DR PeptideAtlas; Q5MNZ9; -.
DR PRIDE; Q5MNZ9; -.
DR ProteomicsDB; 63590; -. [Q5MNZ9-1]
DR ProteomicsDB; 63591; -. [Q5MNZ9-2]
DR Antibodypedia; 1968; 291 antibodies from 36 providers.
DR DNASU; 55062; -.
DR Ensembl; ENST00000262139.10; ENSP00000262139.4; ENSG00000070540.13. [Q5MNZ9-1]
DR GeneID; 55062; -.
DR KEGG; hsa:55062; -.
DR MANE-Select; ENST00000262139.10; ENSP00000262139.4; NM_017983.7; NP_060453.3.
DR UCSC; uc010dey.4; human. [Q5MNZ9-1]
DR CTD; 55062; -.
DR DisGeNET; 55062; -.
DR GeneCards; WIPI1; -.
DR HGNC; HGNC:25471; WIPI1.
DR HPA; ENSG00000070540; Tissue enhanced (skeletal).
DR MIM; 609224; gene.
DR neXtProt; NX_Q5MNZ9; -.
DR OpenTargets; ENSG00000070540; -.
DR PharmGKB; PA142670575; -.
DR VEuPathDB; HostDB:ENSG00000070540; -.
DR eggNOG; KOG2110; Eukaryota.
DR GeneTree; ENSGT00940000156833; -.
DR InParanoid; Q5MNZ9; -.
DR OMA; TLGQIFP; -.
DR OrthoDB; 1216824at2759; -.
DR PhylomeDB; Q5MNZ9; -.
DR TreeFam; TF314879; -.
DR PathwayCommons; Q5MNZ9; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
DR SignaLink; Q5MNZ9; -.
DR SIGNOR; Q5MNZ9; -.
DR BioGRID-ORCS; 55062; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; WIPI1; human.
DR GeneWiki; WIPI1; -.
DR GenomeRNAi; 55062; -.
DR Pharos; Q5MNZ9; Tbio.
DR PRO; PR:Q5MNZ9; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q5MNZ9; protein.
DR Bgee; ENSG00000070540; Expressed in stromal cell of endometrium and 195 other tissues.
DR ExpressionAtlas; Q5MNZ9; baseline and differential.
DR Genevisible; Q5MNZ9; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0000407; C:phagophore assembly site; IDA:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IDA:UniProtKB.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IEP: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; IDA:UniProtKB.
DR GO; GO:2000786; P:positive regulation of autophagosome assembly; IDA: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 GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IDA:UniProtKB.
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; IPR032909; WIPI1.
DR PANTHER; PTHR11227:SF23; PTHR11227:SF23; 1.
DR SMART; SM00320; WD40; 2.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Endosome; Golgi apparatus; Lipid-binding; Membrane;
KW Reference proteome; Repeat; WD repeat.
FT CHAIN 1..446
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 1"
FT /id="PRO_0000051437"
FT REPEAT 3..42
FT /note="WD 1"
FT REPEAT 47..88
FT /note="WD 2"
FT REPEAT 92..126
FT /note="WD 3"
FT REPEAT 131..173
FT /note="WD 4"
FT REPEAT 177..216
FT /note="WD 5"
FT REPEAT 222..261
FT /note="WD 6"
FT REPEAT 304..343
FT /note="WD 7"
FT REGION 386..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 131..136
FT /note="Nuclear receptor interaction"
FT /evidence="ECO:0000269|PubMed:15602573"
FT MOTIF 225..228
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT VAR_SEQ 1..6
FT /note="MEAEAA -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_016966"
FT VARIANT 31
FT /note="T -> I (in dbSNP:rs883541)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:15602573"
FT /id="VAR_024848"
FT VARIANT 308
FT /note="R -> H (in dbSNP:rs36084378)"
FT /id="VAR_053439"
FT MUTAGEN 203
FT /note="S->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 205
FT /note="S->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 208
FT /note="G->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 209
FT /note="T->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 212
FT /note="R->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 226..227
FT /note="RR->AA: Loss of binding to phosphoinositides, does
FT not disrupt the MPR pathway."
FT /evidence="ECO:0000269|PubMed:15020712"
FT MUTAGEN 226
FT /note="R->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 227
FT /note="R->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 228
FT /note="G->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 251
FT /note="S->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 255
FT /note="T->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT MUTAGEN 257
FT /note="H->A: Loss of binding to phosphoinositides and
FT abolishes puncta formation."
FT /evidence="ECO:0000269|PubMed:23088497"
FT CONFLICT 63
FT /note="V -> A (in Ref. 1; AAV80760)"
FT /evidence="ECO:0000305"
FT CONFLICT 249
FT /note="A -> AA (in Ref. 1; AAV80760)"
FT /evidence="ECO:0000305"
FT CONFLICT 358
FT /note="S -> R (in Ref. 2; BAA91423)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 446 AA; 48673 MW; 35B5650990B62E31 CRC64;
MEAEAADAPP GGVESALSCF SFNQDCTSLA TGTKAGYKLF SLSSVEQLDQ VHGSNEIPDV
YIVERLFSSS LVVVVSHTKP RQMNVYHFKK GTEICNYSYS SNILSIRLNR QRLLVCLEES
IYIHNIKDMK LLKTLLDIPA NPTGLCALSI NHSNSYLAYP GSLTSGEIVL YDGNSLKTVC
TIAAHEGTLA AITFNASGSK LASASEKGTV IRVFSVPDGQ KLYEFRRGMK RYVTISSLVF
SMDSQFLCAS SNTETVHIFK LEQVTNSRPE EPSTWSGYMG KMFMAATNYL PTQVSDMMHQ
DRAFATARLN FSGQRNICTL STIQKLPRLL VASSSGHLYM YNLDPQDGGE CVLIKTHSLL
GSGTTEENKE NDLRPSLPQS YAATVARPSA SSASTVPGYS EDGGALRGEV IPEHEFATGP
VCLDDENEFP PIILCRGNQK GKTKQS
