ID   AIP_CHLAE               Reviewed;         330 AA.
AC   O97628;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=AH receptor-interacting protein;
DE            Short=AIP;
DE   AltName: Full=Aryl-hydrocarbon receptor-interacting protein;
DE   AltName: Full=HBV X-associated protein 2;
DE            Short=XAP-2;
DE   AltName: Full=p38;
GN   Name=AIP; Synonyms=XAP2;
OS   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9447995; DOI=10.1128/mcb.18.2.978;
RA   Meyer B.K., Pray-Grant M.G., Vanden Heuvel J.P., Perdew G.H.;
RT   "Hepatitis B virus X-associated protein 2 is a subunit of the unliganded
RT   aryl hydrocarbon receptor core complex and exhibits transcriptional
RT   enhancer activity.";
RL   Mol. Cell. Biol. 18:978-988(1998).
CC   -!- FUNCTION: May play a positive role in AHR-mediated (aromatic
CC       hydrocarbon receptor) signaling, possibly by influencing its
CC       receptivity for ligand and/or its nuclear targeting.
CC   -!- FUNCTION: Cellular negative regulator of the hepatitis B virus (HBV) X
CC       protein.
CC   -!- SUBUNIT: Interacts with RET in the pituitary gland; this interaction
CC       prevents the formation of the AIP-survivin complex.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR   EMBL; AF090949; AAD13759.1; -; mRNA.
DR   AlphaFoldDB; O97628; -.
DR   BMRB; O97628; -.
DR   SMR; O97628; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   Gene3D; 1.25.40.10; -; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR031208; AIP.
DR   InterPro; IPR039663; AIP/AIPL1.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR11242; PTHR11242; 1.
DR   PANTHER; PTHR11242:SF3; PTHR11242:SF3; 1.
DR   Pfam; PF00254; FKBP_C; 1.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50059; FKBP_PPIASE; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Phosphoprotein; Repeat; TPR repeat.
FT   CHAIN           1..330
FT                   /note="AH receptor-interacting protein"
FT                   /id="PRO_0000075338"
FT   DOMAIN          54..146
FT                   /note="PPIase FKBP-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00277"
FT   REPEAT          179..212
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255"
FT   REPEAT          231..264
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000250|UniProtKB:O00170"
FT   REPEAT          265..298
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT                   ProRule:PRU00339"
FT   MOD_RES         43
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00170"
SQ   SEQUENCE   330 AA;  37531 MW;  A0E9D2767BCBCE6C CRC64;
     MADIIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHYRT LHSDNEGTVL DDSRVRGKPM
     ELIIGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLGNIAV GKDPLEGQRH
     CCGVAQMHEH SSLGHADLDA LQQNPQPLVF HMEMLKVESP GTYQQDPWAM TDEEKAKAVP
     LIHQEGNRLY REGHVKEAAA KYYDAIACLK NLQMKEQPGS PEWIQLDQQI TPLLLNYCQC
     KLVAEEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
     VVSRELRALE ARIRQKDEED KARFRGIFSH