Target Name: WIPI1
NCBI ID: G55062
Other Name(s): WIPI1 variant 1 | WD40 repeat protein Interacting with phosphoInositides of 49kDa | WD40 repeat protein interacting with phosphoinositides of 49 kDa | Atg18 protein homolog | WIPI49 | WIPI 49 kDa | WD repeat domain, phosphoinositide interacting 1, transcript variant 1 | ATG18 | WIPI1_HUMAN | ATG18A | WD repeat domain phosphoinositide-interacting protein 1 (isoform a) | WIPI-1 | WD repeat domain, phosphoinositide interacting 1 | atg18 protein homolog | WD repeat domain phosphoinositide-interacting protein 1 | WIPI-1 alpha

WIPI1: A Protein Involved in Disease and Drug Targeting

WIPI1 (WIPI1 variant 1) is a protein that is expressed in various tissues throughout the body, including the brain, heart, liver, and kidneys. It is a member of the WIPI (Wnt-Inhibitor of Progression) family of proteins, which are known for their role in the development and progression of diseases such as cancer, neurodegenerative diseases, and autoimmune disorders.

WIPI1 is a 21-kDa protein that is expressed in a variety of tissues, including the brain, heart, liver, and kidneys. It is a member of the WIPI (Wnt-Inhibitor of Progression) family of proteins, which are known for their role in the development and progression of diseases such as cancer, neurodegenerative diseases, and autoimmune disorders.

One of the unique features of WIPI1 is its structure. WIPI1 is a transmembrane protein that is characterized by a long extracellular domain and a short intracellular domain. The extracellular domain of WIPI1 is made up of a series of repeats of the amino acid Asp, Asn, Asp, and Asn, which are involved in the formation of a transmembrane protein complex. The intracellular domain of WIPI1 is also made up of a series of repeats of the amino acid Asp, Asn, and Asp, which are involved in the formation of a complex with other proteins within the cell.

WIPI1 has been shown to play a role in the development and progression of various diseases. For example, studies have shown that high levels of WIPI1 are associated with an increased risk of neurodegenerative diseases, such as Alzheimer's disease and Parkinson's disease. Additionally, high levels of WIPI1 have been shown to be associated with an increased risk of cancer, particularly colon cancer.

In addition to its potential role in disease, WIPI1 has also been shown to be a potential drug target. Studies have shown that WIPI1 can be targeted by small molecules, such as inhibitors, which can inhibit the activity of WIPI1 and prevent it from interacting with its downstream targets. Additionally,WIPI1 has been shown to interact with several protein, including the protein PDGF-BB, which is a key regulator of cell growth and differentiation.

In conclusion, WIPI1 is a protein that is expressed in various tissues throughout the body and is a member of the WIPI family of proteins. It has been shown to play a role in the development and progression of various diseases, including cancer and neurodegenerative diseases. Additionally, WIPI1 has also been shown to be a potential drug target, and its potential therapeutic uses are being investigated. Further studies are needed to fully understand the role of WIPI1 in disease and its potential as a drug target.

Protein Name: WD Repeat Domain, Phosphoinositide Interacting 1

Functions: Component of the autophagy machinery that controls the major intracellular degradation process by which cytoplasmic materials are packaged into autophagosomes and delivered to lysosomes for degradation (PubMed:15602573, PubMed:20114074, PubMed:20484055, PubMed:20639694, PubMed:23088497, PubMed:28561066, PubMed:31271352). Plays an important role in starvation- and calcium-mediated autophagy, as well as in mitophagy (PubMed:28561066). Functions downstream of the ULK1 and PI3-kinases that produce phosphatidylinositol 3-phosphate (PtdIns3P) on membranes of the endoplasmic reticulum once activated (PubMed:28561066). Binds phosphatidylinositol 3-phosphate (PtdIns3P), and maybe other phosphoinositides including PtdIns3,5P2 and PtdIns5P, and is recruited to phagophore assembly sites at the endoplasmic reticulum membranes (PubMed:28561066, PubMed:31271352, PubMed:33499712). There, it assists WIPI2 in the recruitment of ATG12-ATG5-ATG16L1, a complex that directly controls the elongation of the nascent autophagosomal membrane (PubMed:28561066). Together with WDR45/WIPI4, promotes ATG2 (ATG2A or ATG2B)-mediated lipid transfer by enhancing ATG2-association with phosphatidylinositol 3-monophosphate (PI3P)-containing membranes (PubMed:31271352). Involved in xenophagy of Staphylococcus aureus (PubMed:22829830). Invading S.aureus cells become entrapped in autophagosome-like WIPI1 positive vesicles targeted for lysosomal degradation (PubMed:22829830). Also plays a distinct role in controlling the transcription of melanogenic enzymes and melanosome maturation, a process that is distinct from starvation-induced autophagy (PubMed:21317285). May also regulate the trafficking of proteins involved in the mannose-6-phosphate receptor (MPR) recycling pathway (PubMed:15020712)

More Common Targets

WIPI2 | WIZ | WLS | WNK1 | WNK2 | WNK3 | WNK4 | Wnt | WNT1 | WNT10A | WNT10B | WNT11 | WNT16 | WNT2 | WNT2B | WNT3 | WNT3A | WNT4 | WNT5A | WNT5B | WNT6 | WNT7A | WNT7B | WNT8A | WNT8B | WNT9A | WNT9B | WRAP53 | WRAP73 | WRN | WRNIP1 | WSB1 | WSB2 | WSCD1 | WSCD2 | WSPAR | WT1 | WT1-AS | WTAP | WTAPP1 | WTIP | WWC1 | WWC2 | WWC2-AS2 | WWC3 | WWOX | WWP1 | WWP2 | WWTR1 | WWTR1-AS1 | XAB2 | XACT | XAF1 | XAGE-4 | XAGE1A | XAGE1B | XAGE1D | XAGE2 | XAGE3 | XAGE5 | XBP1 | XCL1 | XCL2 | XCR1 | XDH | XG | XGY2 | XIAP | XIRP1 | XIRP2 | XIST | XK | XKR3 | XKR4 | XKR5 | XKR6 | XKR7 | XKR8 | XKR9 | XKRX | XKRY | XKRYP7 | XLOC_007697 | XLOC_008559 | XLOC_009911 | XNDC1N | XPA | XPC | XPC complex | XPNPEP1 | XPNPEP2 | XPNPEP3 | XPO1 | XPO4 | XPO5 | XPO6 | XPO7 | XPOT | XPR1 | XRCC1