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
