WIPI1_MOUSE
ID WIPI1_MOUSE Reviewed; 446 AA.
AC Q8R3E3; Q8BGE1; Q8R1A9; Q8R1C7;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 1;
DE Short=WIPI-1;
DE AltName: Full=WD40 repeat protein interacting with phosphoinositides of 49 kDa;
DE Short=WIPI 49 kDa;
GN Name=Wipi1; Synonyms=D11Ertd498e;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Osteoclast, Pancreas, and Testis;
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] (ISOFORMS 1; 2 AND 3).
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 PROTEIN SEQUENCE OF 316-325, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Heart;
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 [5]
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 [6]
RP FUNCTION.
RX PubMed=22275429; DOI=10.1242/jcs.094110;
RA Itakura E., Kishi-Itakura C., Koyama-Honda I., Mizushima N.;
RT "Structures containing Atg9A and the ULK1 complex independently target
RT depolarized mitochondria at initial stages of Parkin-mediated mitophagy.";
RL J. Cell Sci. 125:1488-1499(2012).
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:22275429). Plays an important role in starvation- and calcium-
CC mediated autophagy, as well as in mitophagy. Functions downstream of
CC the ULK1 and PI3-kinases that produce phosphatidylinositol 3-phosphate
CC (PtdIns3P) on membranes of the endoplasmic reticulum once activated.
CC Binds phosphatidylinositol 3-phosphate (PtdIns3P), and maybe other
CC phosphoinositides including PtdIns3,5P2 and PtdIns5P, and is recruited
CC to phagophore assembly sites at the endoplasmic reticulum membranes.
CC There, it assists WIPI2 in the recruitment of ATG12-ATG5-ATG16L1, a
CC complex that directly controls the elongation of the nascent
CC autophagosomal membrane. Together with WDR45/WIPI4, promotes ATG2
CC (ATG2A or ATG2B)-mediated lipid transfer by enhancing ATG2-association
CC with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes.
CC Involved in xenophagy of Staphylococcus aureus. Invading S.aureus cells
CC become entrapped in autophagosome-like WIPI1 positive vesicles targeted
CC for lysosomal degradation. Also plays a distinct role in controlling
CC the transcription of melanogenic enzymes and melanosome maturation, a
CC process that is distinct from starvation-induced autophagy. May also
CC regulate the trafficking of proteins involved in the mannose-6-
CC phosphate receptor (MPR) recycling pathway (By similarity).
CC {ECO:0000250|UniProtKB:Q5MNZ9, ECO:0000269|PubMed:22275429}.
CC -!- SUBUNIT: Interacts with androgen receptor (AR) and the estrogen
CC receptors ESR1 and ESR2. Interacts with WIPI2. Interacts with WDR45.
CC Interacts with ATG16L1. May interact with NUDC.
CC {ECO:0000250|UniProtKB:Q5MNZ9}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000250|UniProtKB:Q5MNZ9}. Endosome
CC {ECO:0000250|UniProtKB:Q5MNZ9}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000250|UniProtKB:Q5MNZ9}. Preautophagosomal structure
CC membrane {ECO:0000269|PubMed:21896713}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21896713}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5MNZ9}. Note=Trans elements of the Golgi and
CC peripheral endosomes. Dynamically cycles through these compartments and
CC is 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 {ECO:0000250|UniProtKB:Q5MNZ9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8R3E3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3E3-2; Sequence=VSP_016969;
CC Name=3;
CC IsoId=Q8R3E3-3; Sequence=VSP_016967, VSP_016968;
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:0000250|UniProtKB:Q5MNZ9}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAH24811.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH24883.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={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; AK031672; BAC27504.1; -; mRNA.
DR EMBL; AK034907; BAC28878.1; -; mRNA.
DR EMBL; AK050495; BAE20673.1; -; mRNA.
DR EMBL; AK159608; BAE35227.1; -; mRNA.
DR EMBL; AK170563; BAE41884.1; -; mRNA.
DR EMBL; BC024811; AAH24811.1; ALT_INIT; mRNA.
DR EMBL; BC024883; AAH24883.1; ALT_INIT; mRNA.
DR EMBL; BC025560; AAH25560.1; -; mRNA.
DR CCDS; CCDS25582.1; -. [Q8R3E3-1]
DR RefSeq; NP_666052.1; NM_145940.2. [Q8R3E3-1]
DR AlphaFoldDB; Q8R3E3; -.
DR SMR; Q8R3E3; -.
DR BioGRID; 206708; 3.
DR STRING; 10090.ENSMUSP00000099349; -.
DR iPTMnet; Q8R3E3; -.
DR PhosphoSitePlus; Q8R3E3; -.
DR MaxQB; Q8R3E3; -.
DR PaxDb; Q8R3E3; -.
DR PeptideAtlas; Q8R3E3; -.
DR PRIDE; Q8R3E3; -.
DR ProteomicsDB; 299787; -. [Q8R3E3-1]
DR ProteomicsDB; 299788; -. [Q8R3E3-2]
DR ProteomicsDB; 299789; -. [Q8R3E3-3]
DR Antibodypedia; 1968; 291 antibodies from 36 providers.
DR Ensembl; ENSMUST00000047186; ENSMUSP00000038635; ENSMUSG00000041895. [Q8R3E3-2]
DR Ensembl; ENSMUST00000103060; ENSMUSP00000099349; ENSMUSG00000041895. [Q8R3E3-1]
DR GeneID; 52639; -.
DR KEGG; mmu:52639; -.
DR UCSC; uc007mcq.1; mouse. [Q8R3E3-1]
DR UCSC; uc007mcr.1; mouse. [Q8R3E3-2]
DR CTD; 55062; -.
DR MGI; MGI:1261864; Wipi1.
DR VEuPathDB; HostDB:ENSMUSG00000041895; -.
DR eggNOG; KOG2110; Eukaryota.
DR GeneTree; ENSGT00940000156833; -.
DR HOGENOM; CLU_025895_1_0_1; -.
DR InParanoid; Q8R3E3; -.
DR OMA; TLGQIFP; -.
DR OrthoDB; 1216824at2759; -.
DR PhylomeDB; Q8R3E3; -.
DR TreeFam; TF314879; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 52639; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Wipi1; mouse.
DR PRO; PR:Q8R3E3; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8R3E3; protein.
DR Bgee; ENSMUSG00000041895; Expressed in seminal vesicle and 250 other tissues.
DR ExpressionAtlas; Q8R3E3; baseline and differential.
DR Genevisible; Q8R3E3; MM.
DR GO; GO:0000421; C:autophagosome membrane; ISO:MGI.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0000407; C:phagophore assembly site; IDA:MGI.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISO:MGI.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0050681; F:nuclear androgen receptor binding; ISO:MGI.
DR GO; GO:0030331; F:nuclear estrogen receptor binding; ISO:MGI.
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:0005102; F:signaling receptor 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: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 GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; ISO:MGI.
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; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasm; Cytoplasmic vesicle;
KW Cytoskeleton; Direct protein sequencing; Endosome; Golgi apparatus;
KW Lipid-binding; Membrane; Reference proteome; Repeat; WD repeat.
FT CHAIN 1..446
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 1"
FT /id="PRO_0000051438"
FT REPEAT 184..224
FT /note="WD 1"
FT REPEAT 230..269
FT /note="WD 2"
FT REPEAT 312..351
FT /note="WD 3"
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:0000250|UniProtKB:Q5MNZ9"
FT MOTIF 225..228
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
FT VAR_SEQ 267..270
FT /note="SRPE -> RCRT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016967"
FT VAR_SEQ 271..446
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_016968"
FT VAR_SEQ 432..446
FT /note="IILCRGSQKGKTKQS -> VSIRNP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_016969"
SQ SEQUENCE 446 AA; 48758 MW; 9F7FA1CB802E5344 CRC64;
MEAEAADAPP GRVEAALSCF SFNQDCTSLA IGTKAGYKLF SLSSVEQLDQ VHGSNEIPDV
YIVERLFSSS LVVVVSHTKP RQMNVYHFKK GTEICNYSYS SNILSIRLNR QRLLVCLEES
IYIHNIKDMK LLKTVLDIPS NPTGLCALSI NHSNSYLAYP GSQSTGEIVL YDGNSLKTVC
TIAAHEGTLA AITFNSSGSK LASASEKGTV IRVFSVPEGQ KLYEFRRGMK RYVTISSLVF
SMDSQFLCAS SNTETVHIFK MEHLTDSRPE EPSTWSGYMG KMFMAATNYL PAQVSDMMNQ
DRAFATGRLN FSGQKNICTL STIQKLPRLL VASSDGHLYI YNLDPQDGGE CVLIKTHSLL
SSGTTEENKE NDLRPSLPPS YAATVARPST SAASTVPGYS EDGGALRGEV IPEHEFATGP
VCLDDENEFP PIILCRGSQK GKTKQS
