AIP_MOUSE
ID AIP_MOUSE Reviewed; 330 AA.
AC O08915; Q3UJM2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=AH receptor-interacting protein;
DE Short=AIP;
DE AltName: Full=Aryl-hydrocarbon receptor-interacting protein;
GN Name=Aip;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9083006; DOI=10.1074/jbc.272.14.8912;
RA Ma Q., Whitlock J.P. Jr.;
RT "A novel cytoplasmic protein that interacts with the Ah receptor, contains
RT tetratricopeptide repeat motifs, and augments the transcriptional response
RT to 2,3,7,8-tetrachlorodibenzo-p-dioxin.";
RL J. Biol. Chem. 272:8878-8884(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=DBA/2J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; 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 [4]
RP PROTEIN SEQUENCE OF 291-304, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hippocampus;
RA Lubec G., Klug S.;
RL Submitted (MAR-2007) to UniProtKB.
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Liver, Lung, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- SUBUNIT: Interacts with RET in the pituitary gland; this interaction
CC prevents the formation of the AIP-survivin complex.
CC -!- INTERACTION:
CC O08915; P27601: Gna13; NbExp=3; IntAct=EBI-6935014, EBI-2255627;
CC O08915; P21279: Gnaq; NbExp=2; IntAct=EBI-6935014, EBI-771975;
CC O08915; P37242: Thrb; NbExp=2; IntAct=EBI-6935014, EBI-6935043;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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DR EMBL; U85489; AAB59009.1; -; mRNA.
DR EMBL; AK146390; BAE27133.1; -; mRNA.
DR EMBL; BC075614; AAH75614.1; -; mRNA.
DR CCDS; CCDS29415.1; -.
DR RefSeq; NP_001263213.1; NM_001276284.1.
DR RefSeq; NP_057875.1; NM_016666.3.
DR RefSeq; XP_006531704.2; XM_006531641.3.
DR RefSeq; XP_006531705.1; XM_006531642.3.
DR AlphaFoldDB; O08915; -.
DR SMR; O08915; -.
DR BioGRID; 198043; 25.
DR CORUM; O08915; -.
DR IntAct; O08915; 5.
DR MINT; O08915; -.
DR STRING; 10090.ENSMUSP00000113807; -.
DR iPTMnet; O08915; -.
DR PhosphoSitePlus; O08915; -.
DR REPRODUCTION-2DPAGE; O08915; -.
DR EPD; O08915; -.
DR MaxQB; O08915; -.
DR PaxDb; O08915; -.
DR PeptideAtlas; O08915; -.
DR PRIDE; O08915; -.
DR ProteomicsDB; 296144; -.
DR Antibodypedia; 1367; 425 antibodies from 36 providers.
DR DNASU; 11632; -.
DR Ensembl; ENSMUST00000025767; ENSMUSP00000025767; ENSMUSG00000024847.
DR Ensembl; ENSMUST00000117831; ENSMUSP00000113807; ENSMUSG00000024847.
DR GeneID; 11632; -.
DR KEGG; mmu:11632; -.
DR UCSC; uc008fyp.2; mouse.
DR CTD; 9049; -.
DR MGI; MGI:109622; Aip.
DR VEuPathDB; HostDB:ENSMUSG00000024847; -.
DR eggNOG; KOG0545; Eukaryota.
DR GeneTree; ENSGT00390000001289; -.
DR HOGENOM; CLU_052244_0_1_1; -.
DR InParanoid; O08915; -.
DR OMA; QQHERNV; -.
DR OrthoDB; 1278789at2759; -.
DR PhylomeDB; O08915; -.
DR TreeFam; TF314507; -.
DR Reactome; R-MMU-8937144; Aryl hydrocarbon receptor signalling.
DR BioGRID-ORCS; 11632; 13 hits in 77 CRISPR screens.
DR ChiTaRS; Aip; mouse.
DR PRO; PR:O08915; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; O08915; protein.
DR Bgee; ENSMUSG00000024847; Expressed in retinal neural layer and 77 other tissues.
DR ExpressionAtlas; O08915; baseline and differential.
DR Genevisible; O08915; MM.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IPI:MGI.
DR GO; GO:0036004; F:GAF domain binding; ISO:MGI.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003712; F:transcription coregulator activity; IPI:MGI.
DR GO; GO:0051082; F:unfolded protein binding; ISS:HGNC-UCL.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; IPI:MGI.
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; 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_0000075340"
FT DOMAIN 31..121
FT /note="PPIase FKBP-type"
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; 37605 MW; 25C61AB65F9064F2 CRC64;
MADLIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHFRT LHSDNEGSVI DDSRTRGKPM
ELIVGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLRNIAE GKDPLEGQRH
CCGIAQMHEH SSLGHADLDA LQQNPQPLIF HIEMLKVESP GTYQQDPWAM TDEEKAKAVP
VIHQEGNRLY REGQVKEAAA KYYDAIACLK NLQMKEQPGS PDWIQLDLQI TPLLLNYCQC
KLVAQEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
VVSRELRALE TRIRQKDEED KARFRGIFSH
