WIPI4_HUMAN
ID WIPI4_HUMAN Reviewed; 360 AA.
AC Q9Y484; A6NGH5; B7WPI2; Q5MNZ5; Q6IBS7; Q6NT94; Q96H03;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 170.
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=WDRX1, WDRXI4, WIPI4; ORFNames=JM5;
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), AND TISSUE SPECIFICITY.
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 1).
RA Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
RA Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 69-360 (ISOFORM 2).
RC TISSUE=Brain, and 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 [7]
RP SUBCELLULAR LOCATION.
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).
RN [8]
RP INVOLVEMENT IN NBIA5, AND FUNCTION.
RX PubMed=23435086; DOI=10.1038/ng.2562;
RA Saitsu H., Nishimura T., Muramatsu K., Kodera H., Kumada S., Sugai K.,
RA Kasai-Yoshida E., Sawaura N., Nishida H., Hoshino A., Ryujin F.,
RA Yoshioka S., Nishiyama K., Kondo Y., Tsurusaki Y., Nakashima M., Miyake N.,
RA Arakawa H., Kato M., Mizushima N., Matsumoto N.;
RT "De novo mutations in the autophagy gene WDR45 cause static encephalopathy
RT of childhood with neurodegeneration in adulthood.";
RL Nat. Genet. 45:445-449(2013).
RN [9]
RP INTERACTION WITH ATG2A AND ATG2B.
RX PubMed=28820312; DOI=10.1080/15548627.2017.1359381;
RA Zheng J.X., Li Y., Ding Y.H., Liu J.J., Zhang M.J., Dong M.Q., Wang H.W.,
RA Yu L.;
RT "Architecture of the ATG2B-WDR45 complex and an aromatic Y/HF motif crucial
RT for complex formation.";
RL Autophagy 13:1870-1883(2017).
RN [10]
RP FUNCTION, PHOSPHOINOSITIDES-BINDING, ACTIVITY REGULATION, INTERACTION WITH
RP AMPK; ATG2A; NUDC; ULK1; WIPI1 AND WIPI2, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASN-15; GLN-16; ASP-17; GLU-55; ARG-109; ARG-111; HIS-112;
RP ASP-113; LYS-114 AND 232-ARG-ARG-233.
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 [11]
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 [12]
RP INTERACTION WITH ATG2A.
RX PubMed=32483132; DOI=10.1038/s41467-020-16523-y;
RA Ren J., Liang R., Wang W., Zhang D., Yu L., Feng W.;
RT "Multi-site-mediated entwining of the linear WIR-motif around WIPI beta-
RT propellers for autophagy.";
RL Nat. Commun. 11:2702-2702(2020).
RN [13]
RP VARIANT NBIA5 7-ARG--PHE-360 DEL.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
RN [14]
RP VARIANT NBIA5 ASP-208.
RX PubMed=25592411; DOI=10.1016/j.jns.2014.12.036;
RA Tschentscher A., Dekomien G., Ross S., Cremer K., Kukuk G.M., Epplen J.T.,
RA Hoffjan S.;
RT "Analysis of the C19orf12 and WDR45 genes in patients with
RT neurodegeneration with brain iron accumulation.";
RL J. Neurol. Sci. 349:105-109(2015).
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:23435086, PubMed:28561066). Binds phosphatidylinositol 3-
CC phosphate (PtdIns3P) (PubMed:28561066). Activated by the STK11/AMPK
CC signaling pathway upon starvation, WDR45 is involved in autophagosome
CC assembly downstream of WIPI2, regulating the size of forming
CC autophagosomes (PubMed:28561066). 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 (PubMed:31271352). Probably recruited to membranes through its PtdIns3P
CC activity (PubMed:28561066). {ECO:0000269|PubMed:23435086,
CC ECO:0000269|PubMed:28561066, ECO:0000269|PubMed:31271352}.
CC -!- ACTIVITY REGULATION: Activated upon amino-acid starvation.
CC {ECO:0000269|PubMed:28561066}.
CC -!- SUBUNIT: Interacts with WIPI1 (PubMed:28561066). Interacts with WIPI2
CC (PubMed:28561066). Interacts with ATG2A and ATG2B (PubMed:28820312,
CC PubMed:28561066, PubMed:32483132). Interacts with ULK1
CC (PubMed:28561066). May interact with the PRKAA1, PRKAA2, PRKAB1 and
CC PRKAG1 subunits of the AMPK kinase (PubMed:28561066). May interact with
CC NUDC (PubMed:28561066). {ECO:0000269|PubMed:28561066,
CC ECO:0000269|PubMed:28820312, ECO:0000269|PubMed:32483132}.
CC -!- INTERACTION:
CC Q9Y484; Q2TAZ0: ATG2A; NbExp=5; IntAct=EBI-2682844, EBI-2514077;
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000269|PubMed:21802374, ECO:0000269|PubMed:28561066}. Cytoplasm
CC {ECO:0000269|PubMed:21802374}. Note=Diffusely localized in the
CC cytoplasm under nutrient-rich conditions. Localizes to autophagic
CC structures during starvation-induced autophagy.
CC {ECO:0000269|PubMed:21802374}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y484-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y484-2; Sequence=VSP_016976;
CC Name=3;
CC IsoId=Q9Y484-3; Sequence=VSP_016975;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with high expression in
CC skeletal muscle and heart. Weakly expressed in liver and placenta.
CC Expression is down-regulated in pancreatic and in kidney tumors.
CC {ECO:0000269|PubMed:15602573}.
CC -!- DOMAIN: The L/FRRG motif is required for recruitment to PtdIns3P.
CC {ECO:0000250|UniProtKB:Q9Y4P8}.
CC -!- DISEASE: Neurodegeneration with brain iron accumulation 5 (NBIA5)
CC [MIM:300894]: A neurodegenerative disorder associated with iron
CC accumulation in the brain, primarily in the basal ganglia. NBIA5 is
CC characterized by global developmental delay in early childhood that is
CC essentially static, with slow motor and cognitive gains until
CC adolescence or early adulthood. In young adulthood, affected
CC individuals develop progressive dystonia, parkinsonism, extrapyramidal
CC signs, and dementia resulting in severe disability.
CC {ECO:0000269|PubMed:23435086, ECO:0000269|PubMed:25356899,
CC ECO:0000269|PubMed:25592411}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; AY691428; AAV80764.1; -; mRNA.
DR EMBL; AJ005897; CAA06754.1; -; mRNA.
DR EMBL; CR456725; CAG33006.1; -; mRNA.
DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50697.1; -; Genomic_DNA.
DR EMBL; CH471224; EAW50702.1; -; Genomic_DNA.
DR EMBL; BC000464; AAH00464.1; -; mRNA.
DR EMBL; BC003037; AAH03037.1; -; mRNA.
DR EMBL; BC009027; AAH09027.1; -; mRNA.
DR EMBL; BC069206; AAH69206.1; -; mRNA.
DR CCDS; CCDS14318.1; -. [Q9Y484-3]
DR CCDS; CCDS35250.1; -. [Q9Y484-1]
DR RefSeq; NP_001025067.1; NM_001029896.1. [Q9Y484-1]
DR RefSeq; NP_009006.2; NM_007075.3. [Q9Y484-3]
DR AlphaFoldDB; Q9Y484; -.
DR SMR; Q9Y484; -.
DR BioGRID; 116323; 48.
DR IntAct; Q9Y484; 20.
DR STRING; 9606.ENSP00000348848; -.
DR iPTMnet; Q9Y484; -.
DR PhosphoSitePlus; Q9Y484; -.
DR SwissPalm; Q9Y484; -.
DR BioMuta; WDR45; -.
DR DMDM; 74762056; -.
DR EPD; Q9Y484; -.
DR jPOST; Q9Y484; -.
DR MassIVE; Q9Y484; -.
DR MaxQB; Q9Y484; -.
DR PaxDb; Q9Y484; -.
DR PeptideAtlas; Q9Y484; -.
DR PRIDE; Q9Y484; -.
DR ProteomicsDB; 86126; -. [Q9Y484-1]
DR ProteomicsDB; 86127; -. [Q9Y484-2]
DR ProteomicsDB; 86128; -. [Q9Y484-3]
DR ABCD; Q9Y484; 2 sequenced antibodies.
DR Antibodypedia; 34945; 186 antibodies from 20 providers.
DR DNASU; 11152; -.
DR Ensembl; ENST00000322995.13; ENSP00000365543.5; ENSG00000196998.19. [Q9Y484-2]
DR Ensembl; ENST00000356463.7; ENSP00000348848.3; ENSG00000196998.19. [Q9Y484-3]
DR Ensembl; ENST00000376368.7; ENSP00000365546.2; ENSG00000196998.19. [Q9Y484-3]
DR Ensembl; ENST00000376372.9; ENSP00000365551.3; ENSG00000196998.19. [Q9Y484-1]
DR Ensembl; ENST00000634944.1; ENSP00000488972.1; ENSG00000196998.19. [Q9Y484-1]
DR GeneID; 11152; -.
DR KEGG; hsa:11152; -.
DR MANE-Select; ENST00000376372.9; ENSP00000365551.3; NM_001029896.2; NP_001025067.1.
DR UCSC; uc004dmk.2; human. [Q9Y484-1]
DR CTD; 11152; -.
DR DisGeNET; 11152; -.
DR GeneCards; WDR45; -.
DR GeneReviews; WDR45; -.
DR HGNC; HGNC:28912; WDR45.
DR HPA; ENSG00000196998; Low tissue specificity.
DR MalaCards; WDR45; -.
DR MIM; 300526; gene.
DR MIM; 300894; phenotype.
DR neXtProt; NX_Q9Y484; -.
DR OpenTargets; ENSG00000196998; -.
DR Orphanet; 329284; Beta-propeller protein-associated neurodegeneration.
DR Orphanet; 3451; Infantile spasms syndrome.
DR PharmGKB; PA134927673; -.
DR VEuPathDB; HostDB:ENSG00000196998; -.
DR eggNOG; KOG2111; Eukaryota.
DR GeneTree; ENSGT00940000155657; -.
DR InParanoid; Q9Y484; -.
DR OMA; FLCAVSD; -.
DR OrthoDB; 966922at2759; -.
DR PhylomeDB; Q9Y484; -.
DR TreeFam; TF314859; -.
DR PathwayCommons; Q9Y484; -.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR SignaLink; Q9Y484; -.
DR SIGNOR; Q9Y484; -.
DR BioGRID-ORCS; 11152; 20 hits in 704 CRISPR screens.
DR ChiTaRS; WDR45; human.
DR GeneWiki; WDR45; -.
DR GenomeRNAi; 11152; -.
DR Pharos; Q9Y484; Tbio.
DR PRO; PR:Q9Y484; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9Y484; protein.
DR Bgee; ENSG00000196998; Expressed in apex of heart and 207 other tissues.
DR ExpressionAtlas; Q9Y484; baseline and differential.
DR Genevisible; Q9Y484; HS.
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; IDA:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IBA:GO_Central.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA:UniProtKB.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IBA:GO_Central.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0000045; P:autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0006914; P:autophagy; IMP: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 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; 4.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Disease variant; Lipid-binding;
KW Neurodegeneration; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..360
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 4"
FT /id="PRO_0000051452"
FT REPEAT 1..34
FT /note="WD 1"
FT REPEAT 40..84
FT /note="WD 2"
FT REPEAT 92..128
FT /note="WD 3"
FT REPEAT 133..174
FT /note="WD 4"
FT REPEAT 183..222
FT /note="WD 5"
FT REPEAT 227..266
FT /note="WD 6"
FT REPEAT 284..329
FT /note="WD 7"
FT MOTIF 231..234
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT VAR_SEQ 78
FT /note="S -> SA (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016975"
FT VAR_SEQ 145
FT /note="K -> KAAHPTPHLHTL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016976"
FT VARIANT 7..360
FT /note="Missing (in NBIA5)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078645"
FT VARIANT 208
FT /note="A -> D (in NBIA5; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25592411"
FT /id="VAR_080430"
FT MUTAGEN 15
FT /note="N->A: Decreased interaction with ATG2A. Loss of
FT interaction with ATG2A; when associated with A-17."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 16
FT /note="Q->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 17
FT /note="D->A: Decreased interaction with ATG2A. Loss of
FT interaction with ATG2A; when associated with A-15."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 55
FT /note="E->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 109
FT /note="R->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 111
FT /note="R->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 112
FT /note="H->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 113
FT /note="D->A: Loss of interaction with AMPK. No effect on
FT interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 114
FT /note="K->A: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT MUTAGEN 232..233
FT /note="RR->AA: No effect on interaction with ATG2A."
FT /evidence="ECO:0000269|PubMed:28561066"
FT CONFLICT 217
FT /note="I -> T (in Ref. 3; CAG33006)"
FT /evidence="ECO:0000305"
FT CONFLICT 300..302
FT /note="FTV -> YTA (in Ref. 1; AAV80764)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 360 AA; 39868 MW; E1A6746277182AF9 CRC64;
MTQQPLRGVT SLRFNQDQSC FCCAMETGVR IYNVEPLMEK GHLDHEQVGS MGLVEMLHRS
NLLALVGGGS SPKFSEISVL IWDDAREGKD SKEKLVLEFT FTKPVLSVRM RHDKIVIVLK
NRIYVYSFPD NPRKLFEFDT RDNPKGLCDL CPSLEKQLLV FPGHKCGSLQ LVDLASTKPG
TSSAPFTINA HQSDIACVSL NQPGTVVASA SQKGTLIRLF DTQSKEKLVE LRRGTDPATL
YCINFSHDSS FLCASSDKGT VHIFALKDTR LNRRSALARV GKVGPMIGQY VDSQWSLASF
TVPAESACIC AFGRNTSKNV NSVIAICVDG TFHKYVFTPD GNCNREAFDV YLDICDDDDF
