WIPI1_XENLA
ID WIPI1_XENLA Reviewed; 433 AA.
AC Q6DCN1;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=WD repeat domain phosphoinositide-interacting protein 1;
DE Short=WIPI-1;
GN Name=wipi1;
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 (JUL-2004) 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. 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 {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:0000250|UniProtKB:Q5MNZ9}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q5MNZ9}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q5MNZ9}.
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) (By similarity). {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}.
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DR EMBL; BC077974; AAH77974.1; -; mRNA.
DR RefSeq; NP_001087066.1; NM_001093597.1.
DR AlphaFoldDB; Q6DCN1; -.
DR SMR; Q6DCN1; -.
DR DNASU; 446901; -.
DR GeneID; 446901; -.
DR KEGG; xla:446901; -.
DR CTD; 446901; -.
DR Xenbase; XB-GENE-5920775; wipi1.S.
DR OMA; HIATTSE; -.
DR OrthoDB; 1216824at2759; -.
DR Proteomes; UP000186698; Chromosome 9_10S.
DR Bgee; 446901; Expressed in internal ear and 19 other tissues.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0000407; C:phagophore assembly site; ISS:UniProtKB.
DR GO; GO:0034045; C:phagophore assembly site membrane; IEA:UniProtKB-SubCell.
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:2000786; P:positive regulation of autophagosome assembly; 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; IPR032909; WIPI1.
DR PANTHER; PTHR11227:SF23; PTHR11227:SF23; 1.
DR SMART; SM00320; WD40; 3.
DR SUPFAM; SSF50978; SSF50978; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endosome;
KW Golgi apparatus; Lipid-binding; Membrane; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..433
FT /note="WD repeat domain phosphoinositide-interacting
FT protein 1"
FT /id="PRO_0000051439"
FT REPEAT 136..177
FT /note="WD 1"
FT REPEAT 180..220
FT /note="WD 2"
FT REPEAT 226..265
FT /note="WD 3"
FT REPEAT 296..346
FT /note="WD 4"
FT MOTIF 127..132
FT /note="Nuclear receptor interaction"
FT /evidence="ECO:0000250|UniProtKB:Q5MNZ9"
FT MOTIF 221..224
FT /note="L/FRRG motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y4P8"
SQ SEQUENCE 433 AA; 47385 MW; 2919FA1A6F5BC752 CRC64;
METGGGGDGT GDICCLSYNQ DCTSVAIGMR SGYKLYSLSN VERLDLVHES CEAKDVYIVE
RLFSSSLVVV VSHAKPRQMN VLHFKKGTEI CNYNYSDNIL SIRLNRQRLI VCLEESIYIH
NIKDMKLLKT LLDTPRNPHG LCTLSINHSN SYLAYPGSSS TGEVSLYDAN CLKCECTIPA
HDSPLAAIAF NSTGTKLASA SEKGTVIRVF SIPDGQKLYE FRRGMKRYVN ISSLVFSMDS
QFLCASSNTE TVHVFKLEQL PERSEENASW TGYMGKMFMA ASNYLPTQVS DMMNQDRAFA
TVRLNFSGQK NACTLVTIQK LPRLLVTSSS GHLYVYNLDP QDGGECVLIK KHSLLGSAKS
ETDGDSDAES PVPVSYAATV ARPSSAPALS TITGYSEDGG TLRGEVIPEH ELAVGPVCLD
DEKEFPPVSI KNP
