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AIP_RAT
ID   AIP_RAT                 Reviewed;         330 AA.
AC   Q5FWY5; Q8CGW7;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=AH receptor-interacting protein;
DE            Short=AIP;
DE   AltName: Full=Aryl-hydrocarbon receptor-interacting protein;
DE   AltName: Full=Immunophilin XAP2;
GN   Name=Aip; Synonyms=Xap2;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Sprague-Dawley;
RX   PubMed=12810716; DOI=10.1074/jbc.m303269200;
RA   Bolger G.B., Peden A.H., Steele M.R., MacKenzie C., McEwan D.G.,
RA   Wallace D.A., Huston E., Baillie G.S., Houslay M.D.;
RT   "Attenuation of the activity of the cAMP-specific phosphodiesterase PDE4A5
RT   by interaction with the immunophilin XAP2.";
RL   J. Biol. Chem. 278:33351-33363(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   PROTEIN SEQUENCE OF 68-78; 242-260 AND 291-304, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=Sprague-Dawley; TISSUE=Hippocampus;
RA   Lubec G., Diao W.;
RL   Submitted (APR-2007) to UniProtKB.
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. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RET in the pituitary gland; this interaction
CC       prevents the formation of the AIP-survivin complex.
CC   -!- INTERACTION:
CC       Q5FWY5; Q01062: Pde2a; NbExp=2; IntAct=EBI-1786045, EBI-1786062;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; AF543560; AAN77242.1; -; mRNA.
DR   EMBL; BC089110; AAH89110.1; -; mRNA.
DR   RefSeq; NP_758830.2; NM_172327.2.
DR   RefSeq; XP_006230761.1; XM_006230699.3.
DR   RefSeq; XP_006230762.1; XM_006230700.3.
DR   AlphaFoldDB; Q5FWY5; -.
DR   SMR; Q5FWY5; -.
DR   BioGRID; 251863; 3.
DR   IntAct; Q5FWY5; 2.
DR   STRING; 10116.ENSRNOP00000000599; -.
DR   PhosphoSitePlus; Q5FWY5; -.
DR   jPOST; Q5FWY5; -.
DR   PaxDb; Q5FWY5; -.
DR   PRIDE; Q5FWY5; -.
DR   Ensembl; ENSRNOT00000091542; ENSRNOP00000075162; ENSRNOG00000022289.
DR   GeneID; 282827; -.
DR   KEGG; rno:282827; -.
DR   UCSC; RGD:628619; rat.
DR   CTD; 9049; -.
DR   RGD; 628619; Aip.
DR   eggNOG; KOG0545; Eukaryota.
DR   GeneTree; ENSGT00390000001289; -.
DR   HOGENOM; CLU_052244_0_1_1; -.
DR   InParanoid; Q5FWY5; -.
DR   OMA; QQHERNV; -.
DR   OrthoDB; 1278789at2759; -.
DR   PhylomeDB; Q5FWY5; -.
DR   TreeFam; TF314507; -.
DR   Reactome; R-RNO-8937144; Aryl hydrocarbon receptor signalling.
DR   PRO; PR:Q5FWY5; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000022289; Expressed in skeletal muscle tissue and 20 other tissues.
DR   Genevisible; Q5FWY5; RN.
DR   GO; GO:0034751; C:aryl hydrocarbon receptor complex; ISO:RGD.
DR   GO; GO:0005829; C:cytosol; IDA:RGD.
DR   GO; GO:0016020; C:membrane; ISO:RGD.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0017162; F:aryl hydrocarbon receptor binding; ISO:RGD.
DR   GO; GO:0036004; F:GAF domain binding; ISO:RGD.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR   GO; GO:0003712; F:transcription coregulator activity; ISO:RGD.
DR   GO; GO:0051082; F:unfolded protein binding; ISS:HGNC-UCL.
DR   GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IDA:RGD.
DR   GO; GO:0022417; P:protein maturation by protein folding; ISS:HGNC-UCL.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; ISS:HGNC-UCL.
DR   GO; GO:0010738; P:regulation of protein kinase A signaling; IDA:RGD.
DR   GO; GO:0006805; P:xenobiotic metabolic process; ISO:RGD.
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   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Phosphoprotein; Reference proteome;
KW   Repeat; TPR repeat.
FT   CHAIN           1..330
FT                   /note="AH receptor-interacting protein"
FT                   /id="PRO_0000288800"
FT   DOMAIN          31..121
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"
FT   CONFLICT        62
FT                   /note="L -> F (in Ref. 1; AAN77242)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        89
FT                   /note="L -> F (in Ref. 1; AAN77242)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   330 AA;  37599 MW;  FE96E23EBFAA2924 CRC64;
     MADLIARLRE DGIQKRVIQE GRGELPEFQD GTKATFHFRT LHSDPEGSVI DDSRARGKPM
     ELIIGKKFKL PVWETIVRTM REGETAQFLC DVKHTVLYPL VAKSLRNIAE GKDPLEGQRH
     CCGIAQMHEH SSLGHADLDA LQQNPQPLIF HIEMLKVESP GTYQQDPWAM TDEEKAKAVP
     LIHQEGNRLY REGQVKEAAA KYYDAIACLK NLQMKEQPGS PDWIQLDLQI TPLLLNYCQC
     KLVAQEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
     VVSRELRALE ARIRQKDEED KARFRGIFSH
 
 
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