AH receptor-interacting protein

Protein found in humans From Wikipedia, the free encyclopedia

AH receptor-interacting protein (AIP) also known as aryl hydrocarbon receptor-interacting protein, immunophilin homolog ARA9, or HBV X-associated protein 2 (XAP-2) is a protein that in humans is encoded by the AIP gene.[5][6][7] The protein is a member of the FKBP family.

AliasesAIP, ARA9, FKBP16, FKBP37, SMTPHN, XAP-2, XAP2, aryl hydrocarbon receptor interacting protein, PITA1
PDBOrtholog search: PDBe RCSB
Quick facts AIP, Identifiers ...
AIP
Identifiers
AliasesAIP, ARA9, FKBP16, FKBP37, SMTPHN, XAP-2, XAP2, aryl hydrocarbon receptor interacting protein, PITA1
External IDsOMIM: 605555; MGI: 109622; HomoloGene: 2959; GeneCards: AIP; OMA:AIP - orthologs
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_003977
NM_001302959
NM_001302960

NM_001276284
NM_016666

RefSeq (protein)

NP_001289888
NP_001289889
NP_003968

NP_001263213
NP_057875

Location (UCSC)Chr 11: 67.47 – 67.49 MbChr 19: 4.16 – 4.18 Mb
PubMed search[3][4]
Wikidata
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Function

AIP may play a positive role in aryl hydrocarbon receptor-mediated signalling possibly by influencing its receptivity for ligand and/or its nuclear targeting. AIP is the cellular negative regulator of the hepatitis B virus (HBV) X protein.[5] Further, it's been known to suppress antiviral signaling and the induction of type I interferon by targeting IRF7, a key player in the antiviral signal pathways.[8] AIP consists of an N-terminal FKBP52 like domain and a C-terminal TPR domain.[9]

Mutations and role in disease

AIP mutations may be the cause of a familial form of acromegaly, familial isolated pituitary adenoma (FIPA). Somatotropinomas (i.e. GH-producing pituitary adenomas), sometimes associated with prolactinomas, are present in most AIP mutated patients.[10]

Interactions

AIP has been shown to interact with the aryl hydrocarbon receptor,[7][11][12] peroxisome proliferator-activated receptor alpha[13] and the aryl hydrocarbon receptor nuclear translocator.[7][14] Further, it has shown that AIP can interact with IRF7 to exert its novel function of negatively regulating antiviral signal pathways.[8]

References

Further reading

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