WIPI2_RAT
ID WIPI2_RAT Reviewed; 445 AA.
AC Q6AY57;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 2 {ECO:0000305};
DE Short=WIPI-2;
GN Name=Wipi2 {ECO:0000312|RGD:1359154};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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
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. Mediates ER-isolation membranes contacts by interacting with
CC the ULK1:RB1CC1 complex and PtdIns3P. 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}.
CC -!- SUBUNIT: Interacts with TECPR1. Interacts with ATG16L1. Interacts with
CC ATG5. Interacts with WIPI1. Interacts with WDR45. May interact with
CC NUDC. Interacts with ULK1 and RB1CC1. {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}. 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:0000250|UniProtKB:Q9Y4P8}.
CC -!- SIMILARITY: Belongs to the WD repeat PROPPIN family. {ECO:0000305}.
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DR EMBL; BC079184; AAH79184.1; -; mRNA.
DR RefSeq; NP_001007616.1; NM_001007615.1.
DR AlphaFoldDB; Q6AY57; -.
DR SMR; Q6AY57; -.
DR STRING; 10116.ENSRNOP00000001476; -.
DR iPTMnet; Q6AY57; -.
DR PhosphoSitePlus; Q6AY57; -.
DR jPOST; Q6AY57; -.
DR PaxDb; Q6AY57; -.
DR PRIDE; Q6AY57; -.
DR Ensembl; ENSRNOT00000001476; ENSRNOP00000001476; ENSRNOG00000001114.
DR GeneID; 288498; -.
DR KEGG; rno:288498; -.
DR UCSC; RGD:1359154; rat.
DR CTD; 26100; -.
DR RGD; 1359154; Wipi2.
DR eggNOG; KOG2110; Eukaryota.
DR GeneTree; ENSGT00940000155537; -.
DR HOGENOM; CLU_025895_1_1_1; -.
DR InParanoid; Q6AY57; -.
DR OMA; PSRDFAW; -.
DR OrthoDB; 1216824at2759; -.
DR PhylomeDB; Q6AY57; -.
DR TreeFam; TF314879; -.
DR Reactome; R-RNO-1632852; Macroautophagy.
DR PRO; PR:Q6AY57; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001114; Expressed in testis and 19 other tissues.
DR Genevisible; Q6AY57; RN.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0000407; C:phagophore assembly site; ISO:RGD.
DR GO; GO:0034045; C:phagophore assembly site membrane; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
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:0010314; F:phosphatidylinositol-5-phosphate binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0034497; P:protein localization to phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0098792; P:xenophagy; ISO:RGD.
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_0000051442"
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:0000250|UniProtKB:Q9Y4P8"
FT MOD_RES 395
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 445 AA; 48519 MW; 884A8489F2AC399F CRC64;
MNLASQSGEA GAGQLLFANF NQDNTSLAVG SKSGYKFFSL SSVDKLEQIY ECTDTEDVCI
VERLFSSSLV AIVSLKAPRK LKVCHFKKGT EICNYSYSNT ILAVKLNRQR LIVCLEESLY
IHNIRDMKVL HTIRETPPNP AGLCALSINN DNCYLAYPGS ATIGEVQVFD TINLRAANMI
PAHDSPLAAL AFDASGTKLA TASEKGTVIR VFSIPEGQKL FEFRRGVKRC VSICSLAFSM
DGMFLSASSN TETVHIFKLE AVREKPPEEP TTWTGYFGKV LMASTSYLPS QVTEMFNQGR
AFATVRLPFC GHKNICSLTT IQKIPRLLVG ASDGYLYMYN LDPQEGGECA LMRQHRLDGS
METTSEIVDS ASHDCPLVTQ TYGTAAAKGA YVPSSPTRLG KGQDANLEAY TDDLGAVGGA
CLEDEASALR LDEDSEHPPM ILRTD
