ID   WIPI2_XENLA             Reviewed;         435 AA.
AC   Q7ZWU5;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=WD repeat domain phosphoinositide-interacting protein 2;
DE            Short=WIPI-2;
GN   Name=wipi2;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000250|UniProtKB:Q9Y4P8}.
CC   -!- SUBCELLULAR LOCATION: Preautophagosomal structure membrane
CC       {ECO:0000250|UniProtKB:Q9Y4P8}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9Y4P8}; Cytoplasmic side
CC       {ECO:0000250|UniProtKB:Q9Y4P8}.
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; BC046705; AAH46705.1; -; mRNA.
DR   RefSeq; NP_001080319.1; NM_001086850.1.
DR   AlphaFoldDB; Q7ZWU5; -.
DR   SMR; Q7ZWU5; -.
DR   DNASU; 380011; -.
DR   GeneID; 380011; -.
DR   KEGG; xla:380011; -.
DR   CTD; 380011; -.
DR   Xenbase; XB-GENE-6084336; wipi2.L.
DR   OrthoDB; 1216824at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 380011; Expressed in brain and 19 other tissues.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
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:0000045; P:autophagosome assembly; ISS:UniProtKB.
DR   GO; GO:0009267; P:cellular response to starvation; ISS:UniProtKB.
DR   GO; GO:0034497; P:protein localization to phagophore assembly site; ISS: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; IPR032911; WIPI2.
DR   PANTHER; PTHR11227:SF27; PTHR11227:SF27; 1.
DR   SMART; SM00320; WD40; 3.
DR   SUPFAM; SSF50978; SSF50978; 1.
PE   2: Evidence at transcript level;
KW   Autophagy; Lipid-binding; Membrane; Reference proteome; Repeat; WD repeat.
FT   CHAIN           1..435
FT                   /note="WD repeat domain phosphoinositide-interacting
FT                   protein 2"
FT                   /id="PRO_0000051444"
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   REGION          386..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           223..226
FT                   /note="L/FRRG motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
SQ   SEQUENCE   435 AA;  47693 MW;  7827088AA7D91121 CRC64;
     MNLASQSVDA GAGQLLFANF NQDNTSLAVG SKSGYKFFSL SSVDKLEQIY ECTDTEDVCI
     VERLFSSSLV AIVSLKAPRK LKVCHFKKGT EICNYSYSNT TLAVKLNRQR LIVCLEESLY
     IHNIRDMKVL HTIRETPPNP SGLCSLSING ENCYLAYPGS ASIGEVQVFD TVNLRAANMI
     PAHDSPLAAL AFDASGTKLA TASEKGTVIR VFSIPEGQKL FEFRRGVKRC VSICSLAFSM
     DSIFLSASSN TETVHIFKLE TIKEKPPEEP TSWTGYFGRV IMASTSYLPS QVTEMFNQGR
     AFATVRLPFC GHKNICALAT IQKISRLLVG AADGYLYIYN FDPQEGGECT LMKQHKLDGS
     MEPSSEILES SSHDRQVGAQ TYSATVTKTY PPPSPTRHAY ADDLGAVGGA SEEDEMGNLR
     LDEDNENPPM ILQTE