WIPI2_MOUSE
ID WIPI2_MOUSE Reviewed; 445 AA.
AC Q80W47;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 2 {ECO:0000305};
DE Short=WIPI-2;
GN Name=Wipi2 {ECO:0000312|MGI:MGI:1923831};
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=Amnion, and Spleen;
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=Kidney;
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=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Spleen, and Testis;
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 FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23051912; DOI=10.4161/auto.22379;
RA Liao C.C., Ho M.Y., Liang S.M., Liang C.M.;
RT "Recombinant protein rVP1 upregulates BECN1-independent autophagy, MAPK1/3
RT phosphorylation and MMP9 activity via WIPI1/WIPI2 to promote macrophage
RT migration.";
RL Autophagy 9:5-19(2013).
RN [6]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=23291478; DOI=10.4161/auto.23066;
RA McAlpine F., Williamson L.E., Tooze S.A., Chan E.Y.;
RT "Regulation of nutrient-sensitive autophagy by uncoordinated 51-like
RT kinases 1 and 2.";
RL Autophagy 9:361-373(2013).
RN [7]
RP FUNCTION, INTERACTION WITH ATG16L1, AND SUBCELLULAR LOCATION.
RX PubMed=24954904; DOI=10.1016/j.molcel.2014.05.021;
RA Dooley H.C., Razi M., Polson H.E., Girardin S.E., Wilson M.I., Tooze S.A.;
RT "WIPI2 links LC3 conjugation with PI3P, autophagosome formation, and
RT pathogen clearance by recruiting Atg12-5-16L1.";
RL Mol. Cell 55:238-252(2014).
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. Involved in an early step of the formation of
CC preautophagosomal structures. Binds and is activated by
CC phosphatidylinositol 3-phosphate (PtdIns3P) forming on membranes of the
CC endoplasmic reticulum upon activation of the upstream ULK1 and PI3
CC kinases (PubMed:23051912, PubMed:23291478, PubMed:24954904). Mediates
CC ER-isolation membranes contacts by interacting with the ULK1:RB1CC1
CC complex and PtdIns3P (By similarity). Once activated, WIPI2 recruits at
CC phagophore assembly sites the ATG12-ATG5-ATG16L1 complex that directly
CC controls the elongation of the nascent autophagosomal membrane.
CC {ECO:0000250|UniProtKB:Q9Y4P8, ECO:0000269|PubMed:23051912,
CC ECO:0000269|PubMed:23291478, ECO:0000269|PubMed:24954904}.
CC -!- SUBUNIT: Interacts with TECPR1 (By similarity). Interacts with ATG16L1
CC (PubMed:24954904). Interacts with ATG5 (By similarity). Interacts with
CC WIPI1 (By similarity). Interacts with WDR45 (By similarity). May
CC interact with NUDC (By similarity). Interacts with ULK1 and RB1CC1 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Y4P8,
CC ECO:0000269|PubMed:24954904}.
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC {ECO:0000269|PubMed:23051912, ECO:0000269|PubMed:23291478,
CC ECO:0000269|PubMed:24954904}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q9Y4P8}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q9Y4P8}. Note=Localizes to omegasomes membranes
CC which are endoplasmic reticulum connected structures at the origin of
CC preautophagosomal structures. Enriched at preautophagosomal structure
CC membranes in response to PtdIns3P. {ECO:0000250|UniProtKB:Q9Y4P8}.
CC -!- DOMAIN: The L/FRRG motif is required for recruitment to PtdIns3P.
CC {ECO:0000269|PubMed:24954904}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; AK155113; BAE33057.1; -; mRNA.
DR EMBL; AK169051; BAE40839.1; -; mRNA.
DR EMBL; AK172030; BAE42786.1; -; mRNA.
DR EMBL; BC044894; AAH44894.1; -; mRNA.
DR CCDS; CCDS19828.1; -.
DR RefSeq; NP_848485.1; NM_178398.4.
DR AlphaFoldDB; Q80W47; -.
DR SMR; Q80W47; -.
DR BioGRID; 217015; 26.
DR IntAct; Q80W47; 10.
DR STRING; 10090.ENSMUSP00000045201; -.
DR iPTMnet; Q80W47; -.
DR PhosphoSitePlus; Q80W47; -.
DR EPD; Q80W47; -.
DR jPOST; Q80W47; -.
DR MaxQB; Q80W47; -.
DR PaxDb; Q80W47; -.
DR PeptideAtlas; Q80W47; -.
DR PRIDE; Q80W47; -.
DR ProteomicsDB; 297560; -.
DR Antibodypedia; 11278; 347 antibodies from 33 providers.
DR DNASU; 74781; -.
DR Ensembl; ENSMUST00000036872; ENSMUSP00000045201; ENSMUSG00000029578.
DR GeneID; 74781; -.
DR KEGG; mmu:74781; -.
DR UCSC; uc009aiy.1; mouse.
DR CTD; 26100; -.
DR MGI; MGI:1923831; Wipi2.
DR VEuPathDB; HostDB:ENSMUSG00000029578; -.
DR eggNOG; KOG2110; Eukaryota.
DR GeneTree; ENSGT00940000155537; -.
DR InParanoid; Q80W47; -.
DR OrthoDB; 1216824at2759; -.
DR PhylomeDB; Q80W47; -.
DR TreeFam; TF314879; -.
DR Reactome; R-MMU-1632852; Macroautophagy.
DR BioGRID-ORCS; 74781; 16 hits in 60 CRISPR screens.
DR ChiTaRS; Wipi2; mouse.
DR PRO; PR:Q80W47; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80W47; protein.
DR Bgee; ENSMUSG00000029578; Expressed in spermatocyte and 269 other tissues.
DR ExpressionAtlas; Q80W47; baseline and differential.
DR Genevisible; Q80W47; MM.
DR GO; GO:0005776; C:autophagosome; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000407; C:phagophore assembly site; IDA:MGI.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:MGI.
DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate 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:0061739; P:protein lipidation involved in autophagosome assembly; IDA:MGI.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; IPI:MGI.
DR GO; GO:0098792; P:xenophagy; IPI: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; IPR032911; WIPI2.
DR PANTHER; PTHR11227:SF27; PTHR11227:SF27; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 1: Evidence at protein level;
KW Autophagy; Lipid-binding; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; WD repeat.
FT CHAIN 1..445
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 2"
FT /id="PRO_0000051441"
FT REPEAT 182..222
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 228..267
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 311..349
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT MOTIF 223..226
FT /note="L/FRRG motif"
FT /evidence="ECO:0000303|PubMed:24954904"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
SQ SEQUENCE 445 AA; 48477 MW; A4D4FF973B104D93 CRC64;
MNLASQSGEA GAGQLLFANF NQDNTSLAVG SKSGYKFFSL SSVDKLEQIY ECTDTEDVCI
VERLFSSSLV AIVSLKAPRK LKVCHFKKGT EICNYSYSNT ILAVKLNRQR LIVCLEESLY
IHNIRDMKVL HTIRETPPNP AGLCALSINN DNCYLAYPGS ASIGEVQVFD TINLRAANMI
PAHDSPLAAL AFDASGTKLA TASEKGTVIR VFSIPEGQKL FEFRRGVKRC VSICSLAFSM
DGMFLSASSN TETVHIFKLE AVREKPPEEP TTWTGYFGKV LMASTSYLPS QVTEMFNQGR
AFATVRLPFC GHKNICSLTT IQKIPRLLVG ASDGYLYMYN LDPQEGGECA LMRQHRLDGS
METTSEIVDS ASHDCPLATQ TYGTAAAKGA YVPSSPTRLG KGQDANLEAY TDDLGAVGGA
CLEDEASALR LDEDSEHPPM ILRTD
