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WD repeat domain phosphoinositide-interacting protein 1 (WIPI-1) (Atg18 protein homolog) (WD40 repeat protein interacting with phosphoinositides of 49 kDa) (WIPI 49 kDa)

 WIPI1_HUMAN             Reviewed;         446 AA.
Q5MNZ9; Q8IXM5; Q9NWF8;
10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-2007, sequence version 3.
23-MAY-2018, entry version 135.
RecName: Full=WD repeat domain phosphoinositide-interacting protein 1;
Short=WIPI-1;
AltName: Full=Atg18 protein homolog;
AltName: Full=WD40 repeat protein interacting with phosphoinositides of 49 kDa;
Short=WIPI 49 kDa;
Name=WIPI1; Synonyms=WIPI49;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
INTERACTION WITH AR; ESR1 AND ESR2, SUBCELLULAR LOCATION, AND VARIANT
ILE-31.
TISSUE=Testis;
PubMed=15602573; DOI=10.1038/sj.onc.1208331;
Proikas-Cezanne T., Waddell S., Gaugel A., Frickey T., Lupas A.,
Nordheim A.;
"WIPI-1alpha (WIPI49), a member of the novel 7-bladed WIPI protein
family, is aberrantly expressed in human cancer and is linked to
starvation-induced autophagy.";
Oncogene 23:9314-9325(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Embryo;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ILE-31.
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION, FUNCTION, SUBCELLULAR LOCATION, BINDING TO
PHOSPHOINOSITIDES, AND MUTAGENESIS OF 226-ARG-ARG-227.
PubMed=15020712; DOI=10.1091/mbc.E03-10-0732;
Jeffries T.R., Dove S.K., Michell R.H., Parker P.J.;
"PtdIns-specific MPR pathway association of a novel WD40 repeat
protein, WIPI49.";
Mol. Biol. Cell 15:2652-2663(2004).
[6]
SUBCELLULAR LOCATION.
PubMed=17618624; DOI=10.1016/j.febslet.2007.06.040;
Proikas-Cezanne T., Ruckerbauer S., Stierhof Y.D., Berg C.,
Nordheim A.;
"Human WIPI-1 puncta-formation: a novel assay to assess mammalian
autophagy.";
FEBS Lett. 581:3396-3404(2007).
[7]
SUBCELLULAR LOCATION.
PubMed=19590496; DOI=10.1038/emboj.2009.159;
Vergne I., Roberts E., Elmaoued R.A., Tosch V., Delgado M.A.,
Proikas-Cezanne T., Laporte J., Deretic V.;
"Control of autophagy initiation by phosphoinositide 3-phosphatase
Jumpy.";
EMBO J. 28:2244-2258(2009).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20639694; DOI=10.4161/auto.6.6.12709;
Itakura E., Mizushima N.;
"Characterization of autophagosome formation site by a hierarchical
analysis of mammalian Atg proteins.";
Autophagy 6:764-776(2010).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20114074; DOI=10.1016/j.cellsig.2010.01.015;
Grotemeier A., Alers S., Pfisterer S.G., Paasch F., Daubrawa M.,
Dieterle A., Viollet B., Wesselborg S., Proikas-Cezanne T., Stork B.;
"AMPK-independent induction of autophagy by cytosolic Ca2+ increase.";
Cell. Signal. 22:914-925(2010).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MICROTUBULE-BINDING.
PubMed=20484055; DOI=10.1074/jbc.M109.091553;
Geeraert C., Ratier A., Pfisterer S.G., Perdiz D., Cantaloube I.,
Rouault A., Pattingre S., Proikas-Cezanne T., Codogno P., Pous C.;
"Starvation-induced hyperacetylation of tubulin is required for the
stimulation of autophagy by nutrient deprivation.";
J. Biol. Chem. 285:24184-24194(2010).
[11]
SUBCELLULAR LOCATION.
PubMed=20529838; DOI=10.1074/jbc.M110.118125;
Gao P., Bauvy C., Souquere S., Tonelli G., Liu L., Zhu Y., Qiao Z.,
Bakula D., Proikas-Cezanne T., Pierron G., Codogno P., Chen Q.,
Mehrpour M.;
"The Bcl-2 homology domain 3 mimetic gossypol induces both Beclin 1-
dependent and Beclin 1-independent cytoprotective autophagy in cancer
cells.";
J. Biol. Chem. 285:25570-25581(2010).
[12]
SUBCELLULAR LOCATION.
PubMed=20059746; DOI=10.1111/j.1600-0854.2010.01034.x;
Taguchi-Atarashi N., Hamasaki M., Matsunaga K., Omori H.,
Ktistakis N.T., Yoshimori T., Noda T.;
"Modulation of local PtdIns3P levels by the PI phosphatase MTMR3
regulates constitutive autophagy.";
Traffic 11:468-478(2010).
[13]
FUNCTION.
PubMed=21317285; DOI=10.1074/jbc.M110.200543;
Ho H., Kapadia R., Al-Tahan S., Ahmad S., Ganesan A.K.;
"WIPI1 coordinates melanogenic gene transcription and melanosome
formation via TORC1 inhibition.";
J. Biol. Chem. 286:12509-12523(2011).
[14]
SUBCELLULAR LOCATION.
PubMed=21564513; DOI=10.1111/j.1582-4934.2011.01339.x;
Proikas-Cezanne T., Robenek H.;
"Freeze-fracture replica immunolabelling reveals human WIPI-1 and
WIPI-2 as membrane proteins of autophagosomes.";
J. Cell. Mol. Med. 15:2007-2010(2011).
[15]
REGULATION BY CALCIUM-SIGNALING, AND SUBCELLULAR LOCATION.
PubMed=21896713; DOI=10.1124/mol.111.071761;
Pfisterer S.G., Mauthe M., Codogno P., Proikas-Cezanne T.;
"Ca2+/calmodulin-dependent kinase (CaMK) signaling via CaMKI and AMP-
activated protein kinase contributes to the regulation of WIPI-1 at
the onset of autophagy.";
Mol. Pharmacol. 80:1066-1075(2011).
[16]
FUNCTION.
PubMed=22829830; DOI=10.1155/2012/179207;
Mauthe M., Yu W., Krut O., Kronke M., Gotz F., Robenek H.,
Proikas-Cezanne T.;
"WIPI-1 positive autophagosome-like vesicles entrap pathogenic
Staphylococcus aureus for lysosomal degradation.";
Int. J. Cell Biol. 2012:179207-179207(2012).
[17]
FUNCTION, DOMAIN, PIP2-BINDING, AND MUTAGENESIS OF SER-203; SER-205;
GLY-208; THR-209; ARG-212; ARG-226; ARG-227; GLY-228; SER-251; THR-255
AND HIS-257.
PubMed=23088497; DOI=10.1186/1750-2187-7-16;
Gaugel A., Bakula D., Hoffmann A., Proikas-Cezanne T.;
"Defining regulatory and phosphoinositide-binding sites in the human
WIPI-1 beta-propeller responsible for autophagosomal membrane
localization downstream of mTORC1 inhibition.";
J. Mol. Signal. 7:16-16(2012).
-!- FUNCTION: Plays an important role in autophagy and in particular
starvation- and calcium-mediated autophagy, as well as in
mitophagy. Functions upstream of the ATG12-ATG5-ATG16L1 complex
and LC3, and downstream of the ULK1 and PI3-kinase complexes.
Involved in xenophagy of Staphylococcus aureus. Invading S.aureus
cells become entrapped in autophagosome-like WIPI1 positive
vesicles targeted for lysosomal degradation. Plays also a distinct
role in controlling the transcription of melanogenic enzymes and
melanosome maturation, a process that is distinct from starvation-
induced autophagy. May also regulate the trafficking of proteins
involved in the mannose-6-phosphate receptor (MPR) recycling
pathway. {ECO:0000269|PubMed:15020712,
ECO:0000269|PubMed:15602573, ECO:0000269|PubMed:20114074,
ECO:0000269|PubMed:20484055, ECO:0000269|PubMed:20639694,
ECO:0000269|PubMed:21317285, ECO:0000269|PubMed:22829830,
ECO:0000269|PubMed:23088497}.
-!- SUBUNIT: Interacts with androgen receptor (AR) and the estrogen
receptors ESR1 and ESR2. Binds PtdIns3P and to a lesser extent,
PtdIns3,5P2 and PtdIns5P in vitro. Interaction with PtdIns3P is
required for recruitment to membranes.
{ECO:0000269|PubMed:15602573}.
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network.
Endosome. Cytoplasmic vesicle, clathrin-coated vesicle.
Preautophagosomal structure membrane; Peripheral membrane protein.
Cytoplasm, cytoskeleton. Note=Trans elements of the Golgi and
peripheral endosomes. Dynamically cycles through these
compartments and is susceptible to conditions that modulate
membrane flux. Enriched in clathrin-coated vesicles. Upon
starvation-induced autophagy, accumulates at subcellular
structures in the cytoplasm: enlarged vesicular and lasso-like
structures, and large cup-shaped structures predominantly around
the nucleus. Recruitment to autophagic membranes is controlled by
MTMR14. Labile microtubules specifically recruit markers of
autophagosome formation like WIPI1, whereas mature autophagosomes
may bind to stable microtubules.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=WIPI-1 alpha;
IsoId=Q5MNZ9-1; Sequence=Displayed;
Name=2; Synonyms=WIPI-1 beta;
IsoId=Q5MNZ9-2; Sequence=VSP_016966;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
skeletal muscle, heart, testis, pancreas and placenta. Highly
expressed in G361, Sk-mel-28, Sk-mel-13, WM852 and WM451 cells.
Up-regulated in a variety of tumor tissues.
{ECO:0000269|PubMed:15602573}.
-!- DOMAIN: The N-terminus might form a beta-propeller domain involved
in specific binding to phosphatidylinositol 3,5-bisphosphate
(PIP2), leading to the association of the protein to the membrane.
Association to the membrane can also occur through binding to
phosphatidylinositol 3-monophosphate (PI3P).
{ECO:0000269|PubMed:23088497}.
-!- SIMILARITY: Belongs to the WD repeat SVP1 family. {ECO:0000305}.
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EMBL; AY691424; AAV80760.1; -; mRNA.
EMBL; AK000917; BAA91423.1; -; mRNA.
EMBL; AC007780; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039867; AAH39867.1; -; mRNA.
CCDS; CCDS11677.1; -. [Q5MNZ9-1]
RefSeq; NP_001307701.1; NM_001320772.1.
RefSeq; NP_060453.3; NM_017983.6. [Q5MNZ9-1]
UniGene; Hs.463964; -.
ProteinModelPortal; Q5MNZ9; -.
SMR; Q5MNZ9; -.
BioGrid; 120380; 12.
IntAct; Q5MNZ9; 7.
STRING; 9606.ENSP00000262139; -.
iPTMnet; Q5MNZ9; -.
PhosphoSitePlus; Q5MNZ9; -.
BioMuta; WIPI1; -.
DMDM; 146291100; -.
MaxQB; Q5MNZ9; -.
PaxDb; Q5MNZ9; -.
PeptideAtlas; Q5MNZ9; -.
PRIDE; Q5MNZ9; -.
DNASU; 55062; -.
Ensembl; ENST00000262139; ENSP00000262139; ENSG00000070540. [Q5MNZ9-1]
GeneID; 55062; -.
KEGG; hsa:55062; -.
UCSC; uc010dey.4; human. [Q5MNZ9-1]
CTD; 55062; -.
DisGeNET; 55062; -.
EuPathDB; HostDB:ENSG00000070540.12; -.
GeneCards; WIPI1; -.
H-InvDB; HIX0014115; -.
HGNC; HGNC:25471; WIPI1.
HPA; CAB037230; -.
HPA; HPA007493; -.
MIM; 609224; gene.
neXtProt; NX_Q5MNZ9; -.
OpenTargets; ENSG00000070540; -.
PharmGKB; PA142670575; -.
eggNOG; KOG2110; Eukaryota.
eggNOG; ENOG410XP6Y; LUCA.
GeneTree; ENSGT00730000110845; -.
HOGENOM; HOG000217544; -.
HOVERGEN; HBG056639; -.
InParanoid; Q5MNZ9; -.
KO; K17908; -.
OMA; STWTGYM; -.
OrthoDB; EOG091G08ZS; -.
PhylomeDB; Q5MNZ9; -.
TreeFam; TF314879; -.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-381038; XBP1(S) activates chaperone genes.
SignaLink; Q5MNZ9; -.
SIGNOR; Q5MNZ9; -.
ChiTaRS; WIPI1; human.
GeneWiki; WIPI1; -.
GenomeRNAi; 55062; -.
PRO; PR:Q5MNZ9; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000070540; -.
CleanEx; HS_WIPI1; -.
ExpressionAtlas; Q5MNZ9; baseline and differential.
Genevisible; Q5MNZ9; HS.
GO; GO:0000421; C:autophagosome membrane; IDA:UniProtKB.
GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0019898; C:extrinsic component of membrane; IBA:GO_Central.
GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
GO; GO:0000407; C:phagophore assembly site; IDA:MGI.
GO; GO:0034045; C:phagophore assembly site membrane; IDA:UniProtKB.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IDA:UniProtKB.
GO; GO:0030331; F:estrogen receptor binding; IDA:UniProtKB.
GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IDA:UniProtKB.
GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
GO; GO:0005102; F:signaling receptor binding; IDA:MGI.
GO; GO:0006914; P:autophagy; IEP:UniProtKB.
GO; GO:0000422; P:autophagy of mitochondrion; IBA:GO_Central.
GO; GO:0044804; P:autophagy of nucleus; IBA:GO_Central.
GO; GO:0036498; P:IRE1-mediated unfolded protein response; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0006497; P:protein lipidation; IBA:GO_Central.
GO; GO:0034497; P:protein localization to phagophore assembly site; IBA:GO_Central.
GO; GO:0048203; P:vesicle targeting, trans-Golgi to endosome; IDA:UniProtKB.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR036322; WD40_repeat_dom_sf.
InterPro; IPR032909; WIPI1.
PANTHER; PTHR11227:SF23; PTHR11227:SF23; 1.
SMART; SM00320; WD40; 2.
SUPFAM; SSF50978; SSF50978; 2.
1: Evidence at protein level;
Alternative splicing; Autophagy; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Cytoskeleton; Endosome; Golgi apparatus;
Membrane; Polymorphism; Reference proteome; Repeat; WD repeat.
CHAIN 1 446 WD repeat domain phosphoinositide-
interacting protein 1.
/FTId=PRO_0000051437.
REPEAT 3 42 WD 1.
REPEAT 47 88 WD 2.
REPEAT 92 126 WD 3.
REPEAT 131 173 WD 4.
REPEAT 177 216 WD 5.
REPEAT 222 261 WD 6.
REPEAT 304 343 WD 7.
MOTIF 131 136 Nuclear receptor interaction.
VAR_SEQ 1 6 MEAEAA -> M (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_016966.
VARIANT 31 31 T -> I (in dbSNP:rs883541).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15602573}.
/FTId=VAR_024848.
VARIANT 308 308 R -> H (in dbSNP:rs36084378).
/FTId=VAR_053439.
MUTAGEN 203 203 S->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 205 205 S->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 208 208 G->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 209 209 T->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 212 212 R->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 226 227 RR->AA: Loss of binding to
phosphoinositides, does not disrupt the
MPR pathway.
{ECO:0000269|PubMed:15020712}.
MUTAGEN 226 226 R->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 227 227 R->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 228 228 G->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 251 251 S->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 255 255 T->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
MUTAGEN 257 257 H->A: Loss of binding to
phosphoinositides and abolishes puncta
formation. {ECO:0000269|PubMed:23088497}.
CONFLICT 63 63 V -> A (in Ref. 1; AAV80760).
{ECO:0000305}.
CONFLICT 249 249 A -> AA (in Ref. 1; AAV80760).
{ECO:0000305}.
CONFLICT 358 358 S -> R (in Ref. 2; BAA91423).
{ECO:0000305}.
SEQUENCE 446 AA; 48673 MW; 35B5650990B62E31 CRC64;
MEAEAADAPP GGVESALSCF SFNQDCTSLA TGTKAGYKLF SLSSVEQLDQ VHGSNEIPDV
YIVERLFSSS LVVVVSHTKP RQMNVYHFKK GTEICNYSYS SNILSIRLNR QRLLVCLEES
IYIHNIKDMK LLKTLLDIPA NPTGLCALSI NHSNSYLAYP GSLTSGEIVL YDGNSLKTVC
TIAAHEGTLA AITFNASGSK LASASEKGTV IRVFSVPDGQ KLYEFRRGMK RYVTISSLVF
SMDSQFLCAS SNTETVHIFK LEQVTNSRPE EPSTWSGYMG KMFMAATNYL PTQVSDMMHQ
DRAFATARLN FSGQRNICTL STIQKLPRLL VASSSGHLYM YNLDPQDGGE CVLIKTHSLL
GSGTTEENKE NDLRPSLPQS YAATVARPSA SSASTVPGYS EDGGALRGEV IPEHEFATGP
VCLDDENEFP PIILCRGNQK GKTKQS


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EIAAB46366 Rat,Rattus norvegicus,WD repeat domain phosphoinositide-interacting protein 4,WD repeat-containing protein 45,Wdr45,Wipi4,WIPI-4
EIAAB46367 Homo sapiens,Human,JM5,WD repeat domain phosphoinositide-interacting protein 4,WD repeat-containing protein 45,WDR45,WDRX1,WDRXI4,WIPI4,WIPI-4
EIAAB46363 Chicken,Gallus gallus,RCJMB04_8d21,WD repeat domain phosphoinositide-interacting protein 3,WD repeat protein 45-like,WDR45L,WDR45-like protein,WIPI3,WIPI-3
EIAAB46359 Mouse,Mus musculus,WD repeat domain phosphoinositide-interacting protein 2,Wipi2,WIPI-2
EIAAB46361 Rat,Rattus norvegicus,WD repeat domain phosphoinositide-interacting protein 2,Wipi2,WIPI-2
EIAAB46362 CGI-50,Homo sapiens,Human,WD repeat domain phosphoinositide-interacting protein 2,WIPI2,WIPI-2,WIPI49-like protein 2
EIAAB46360 Chicken,Gallus gallus,RCJMB04_35d18,WD repeat domain phosphoinositide-interacting protein 2,WIPI2,WIPI-2
25-231 WDR45L is a member of the WIPI or SVP1 family of WD40 repeat-containing proteins. The protein contains seven WD40 repeats that are thought to fold into a beta-propeller structure that mediates protein 0.05 mg
E1142b Rat ELISA Kit FOR WD repeat domain phosphoinositide-interacting protein 2 96T
EIAAB41848 Bos taurus,Bovine,RAP1,RAP1 homolog,Repressor_activator protein 1 homolog,Telomeric repeat-binding factor 2-interacting protein 1,TERF2-interacting telomeric protein 1,TERF2IP,TRF2-interacting telomer
EIAAB31218 Homo sapiens,hPIP1,Human,p21-activated protein kinase-interacting protein 1,PAK_PLC-interacting protein 1,PAK1-interacting protein 1,PAK1IP1,PIP1,WD repeat-containing protein 84,WDR84
EIAAB41846 Rap1,RAP1 homolog,Rat,Rattus norvegicus,Repressor_activator protein 1 homolog,Telomeric repeat-binding factor 2-interacting protein 1,TERF2-interacting telomeric protein 1,Terf2ip,TRF2-interacting tel
I2604 WD repeat domain phosphoinositide-interacting protein 4 (WDR45), Rat, ELISA Kit 96T
CA074_HUMAN Mouse ELISA Kit FOR WD repeat domain phosphoinositide-interacting protein 4 96T
I2598 WD repeat domain phosphoinositide-interacting protein 2 (WIPI2), Rat, ELISA Kit 96T
E0312r Mouse ELISA Kit FOR WD repeat domain phosphoinositide-interacting protein 4 96T
CSB-EL026031RA Rat WD repeat domain phosphoinositide-interacting protein 4(WDR45) ELISA kit 96T
CSB-EL026118RA Rat WD repeat domain phosphoinositide-interacting protein 2(WIPI2) ELISA kit 96T
WIPI1_MOUSE Mouse ELISA Kit FOR WD repeat domain phosphoinositide-interacting protein 1 96T
DUS6_MOUSE Mouse ELISA Kit FOR WD repeat domain phosphoinositide-interacting protein 4 96T


 

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