AIP_HUMAN
ID AIP_HUMAN Reviewed; 330 AA.
AC O00170; A0SZW3; A0SZW4; A0SZW5; A0SZW6; G9I2H4; Q2M3Q2; Q99606;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 3.
DT 03-AUG-2022, entry version 191.
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=Immunophilin homolog ARA9;
GN Name=AIP; Synonyms=XAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lymphoma;
RX PubMed=8972861; DOI=10.1093/nar/24.23.4741;
RA Kuzhandaivelu N., Cong Y.-S., Inouye C., Yang W.-M., Seto E.;
RT "XAP2, a novel hepatitis B virus X-associated protein that inhibits X
RT transactivation.";
RL Nucleic Acids Res. 24:4741-4750(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT LYS-228.
RC TISSUE=B-cell;
RX PubMed=9111057; DOI=10.1074/jbc.272.17.11452;
RA Carver L.A., Bradfield C.A.;
RT "Ligand-dependent interaction of the aryl hydrocarbon receptor with a novel
RT immunophilin homolog in vivo.";
RL J. Biol. Chem. 272:11452-11456(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT LYS-228, AND INVOLVEMENT IN
RP PITA1.
RX PubMed=16728643; DOI=10.1126/science.1126100;
RA Vierimaa O., Georgitsi M., Lehtonen R., Vahteristo P., Kokko A.,
RA Raitila A., Tuppurainen K., Ebeling T.M.L., Salmela P.I., Paschke R.,
RA Gundogdu S., de Menis E., Jaervinen M.J., Launonen V., Karhu A.,
RA Aaltonen L.A.;
RT "Pituitary adenoma predisposition caused by germline mutations in the AIP
RT gene.";
RL Science 312:1228-1230(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PITA1 47-GLY--ARG-54 DEL;
RP GLU-241 AND TRP-271, INVOLVEMENT IN PITA1, AND VARIANTS HIS-16 AND GLN-307.
RX PubMed=17244780; DOI=10.1210/jc.2006-2513;
RA Daly A.F., Vanbellinghen J.-F., Khoo S.K., Jaffrain-Rea M.-L., Naves L.A.,
RA Guitelman M.A., Murat A., Emy P., Gimenez-Roqueplo A.-P., Tamburrano G.,
RA Raverot G., Barlier A., De Herder W., Penfornis A., Ciccarelli E.,
RA Estour B., Lecomte P., Gatta B., Chabre O., Sabate M.I., Bertagna X.,
RA Garcia Basavilbaso N., Stalldecker G., Colao A., Ferolla P., Wemeau J.-L.,
RA Caron P., Sadoul J.-L., Oneto A., Archambeaud F., Calender A.,
RA Sinilnikova O., Montanana C.F., Cavagnini F., Hana V., Solano A.,
RA Delettieres D., Luccio-Camelo D.C., Basso A., Rohmer V., Brue T., Bours V.,
RA Teh B.T., Beckers A.;
RT "Aryl hydrocarbon receptor-interacting protein gene mutations in familial
RT isolated pituitary adenomas: analysis in 73 families.";
RL J. Clin. Endocrinol. Metab. 92:1891-1896(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=21753072; DOI=10.1530/eje-11-0304;
RA Tichomirowa M.A., Barlier A., Daly A.F., Jaffrain-Rea M.L., Ronchi C.,
RA Yaneva M., Urban J.D., Petrossians P., Elenkova A., Tabarin A.,
RA Desailloud R., Maiter D., Schurmeyer T., Cozzi R., Theodoropoulou M.,
RA Sievers C., Bernabeu I., Naves L.A., Chabre O., Montanana C.F., Hana V.,
RA Halaby G., Delemer B., Aizpun J.I., Sonnet E., Longas A.F.,
RA Hagelstein M.T., Caron P., Stalla G.K., Bours V., Zacharieva S., Spada A.,
RA Brue T., Beckers A.;
RT "High prevalence of AIP gene mutations following focused screening in young
RT patients with sporadic pituitary macroadenomas.";
RL Eur. J. Endocrinol. 165:509-515(2011).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LYS-228.
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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [9]
RP INVOLVEMENT IN PITA1.
RX PubMed=17341560; DOI=10.1210/jc.2006-2394;
RA Toledo R.A., Lourenco D.M. Jr., Liberman B., Cunha-Neto M.B.C.,
RA Cavalcanti M.G., Moyses C.B., Toledo S.P.A., Dahia P.L.M.;
RT "Germline mutation in the aryl hydrocarbon receptor interacting protein
RT gene in familial somatotropinoma.";
RL J. Clin. Endocrinol. Metab. 92:1934-1937(2007).
RN [10]
RP INVOLVEMENT IN PITA1, AND VARIANT LYS-228.
RX PubMed=17299063; DOI=10.1210/jc.2006-2702;
RA Barlier A., Vanbellinghen J.-F., Daly A.F., Silvy M., Jaffrain-Rea M.-L.,
RA Trouillas J., Tamagno G., Cazabat L., Bours V., Brue T., Enjalbert A.,
RA Beckers A.;
RT "Mutations in the aryl hydrocarbon receptor interacting protein gene are
RT not highly prevalent among subjects with sporadic pituitary adenomas.";
RL J. Clin. Endocrinol. Metab. 92:1952-1955(2007).
RN [11]
RP INTERACTION WITH RET.
RX PubMed=19366855; DOI=10.1210/jc.2008-1980;
RA Vargiolu M., Fusco D., Kurelac I., Dirnberger D., Baumeister R., Morra I.,
RA Melcarne A., Rimondini R., Romeo G., Bonora E.;
RT "The tyrosine kinase receptor RET interacts in vivo with aryl hydrocarbon
RT receptor-interacting protein to alter survivin availability.";
RL J. Clin. Endocrinol. Metab. 94:2571-2578(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 166-330 IN COMPLEX WITH HSP90 AND
RP TOMM20 PEPTIDES, AND TPR REPEATS.
RX PubMed=23300914; DOI=10.1371/journal.pone.0053339;
RA Morgan R.M., Hernandez-Ramirez L.C., Trivellin G., Zhou L., Roe S.M.,
RA Korbonits M., Prodromou C.;
RT "Structure of the TPR domain of AIP: lack of client protein interaction
RT with the C-terminal alpha-7 helix of the TPR domain of AIP is sufficient
RT for pituitary adenoma predisposition.";
RL PLoS ONE 7:E53339-E53339(2012).
RN [14]
RP VARIANT HIS-16, VARIANT PITA1 GLN-304, AND INVOLVEMENT IN PITA1.
RX PubMed=17360484; DOI=10.1073/pnas.0700004104;
RA Georgitsi M., Raitila A., Karhu A., Tuppurainen K., Maekinen M.J.,
RA Vierimaa O., Paschke R., Saeger W., van der Luijt R.B., Sane T.,
RA Robledo M., De Menis E., Weil R.J., Wasik A., Zielinski G., Lucewicz O.,
RA Lubinski J., Launonen V., Vahteristo P., Aaltonen L.A.;
RT "Molecular diagnosis of pituitary adenoma predisposition caused by aryl
RT hydrocarbon receptor-interacting protein gene mutations.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:4101-4105(2007).
RN [15]
RP VARIANT PITA1 TYR-248 DEL, AND INVOLVEMENT IN PITA1.
RX PubMed=18410548; DOI=10.1111/j.1365-2265.2008.03266.x;
RA Georgitsi M., De Menis E., Cannavo S., Maekinen M.J., Tuppurainen K.,
RA Pauletto P., Curto L., Weil R.J., Paschke R., Zielinski G., Wasik A.,
RA Lubinski J., Vahteristo P., Karhu A., Aaltonen L.A.;
RT "Aryl hydrocarbon receptor interacting protein (AIP) gene mutation analysis
RT in children and adolescents with sporadic pituitary adenomas.";
RL Clin. Endocrinol. (Oxf.) 69:621-627(2008).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] LYS-228, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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 {ECO:0000269|PubMed:19366855}.
CC -!- INTERACTION:
CC O00170; P00533: EGFR; NbExp=2; IntAct=EBI-704197, EBI-297353;
CC O00170; P08238: HSP90AB1; NbExp=8; IntAct=EBI-704197, EBI-352572;
CC O00170; Q92985: IRF7; NbExp=2; IntAct=EBI-704197, EBI-968267;
CC O00170; O00408: PDE2A; NbExp=6; IntAct=EBI-704197, EBI-1785967;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- TISSUE SPECIFICITY: Widely expressed. Higher levels seen in the heart,
CC placenta and skeletal muscle. Not expressed in the liver.
CC -!- DISEASE: Pituitary adenoma 1, multiple types (PITA1) [MIM:102200]: A
CC form of pituitary adenoma, a neoplasm of the pituitary gland and one of
CC the most common neuroendocrine tumors. Pituitary adenomas are
CC clinically classified as functional and non-functional tumors, and
CC manifest with a variety of features, including local invasion of
CC surrounding structures and excessive hormone secretion. Functional
CC pituitary adenomas are further classified by the type of hormone they
CC secrete: growth hormone (GH)-secreting, prolactin (PRL)-secreting,
CC adrenocorticotropin (ACTH)-secreting, thyroid- stimulating hormone
CC (TSH)-secreting, and plurihormonal (GH and TSH) tumors. Familial and
CC sporadic forms have been reported. {ECO:0000269|PubMed:16728643,
CC ECO:0000269|PubMed:17244780, ECO:0000269|PubMed:17299063,
CC ECO:0000269|PubMed:17341560, ECO:0000269|PubMed:17360484,
CC ECO:0000269|PubMed:18410548}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Prolactin-secreting pituitary adenoma (PSPA) [MIM:600634]:
CC Most common type of hormonally active pituitary adenoma.
CC {ECO:0000269|PubMed:16728643, ECO:0000305|PubMed:17244780}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/AIPID604ch11q13.html";
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DR EMBL; U31913; AAB39923.1; -; mRNA.
DR EMBL; U78521; AAB59004.1; -; mRNA.
DR EMBL; AM236341; CAJ85657.1; -; Genomic_DNA.
DR EMBL; EF066502; ABK60081.1; -; Genomic_DNA.
DR EMBL; EF066504; ABK60082.1; -; Genomic_DNA.
DR EMBL; EF066505; ABK60083.1; -; Genomic_DNA.
DR EMBL; EF066510; ABK60084.1; -; Genomic_DNA.
DR EMBL; JN561683; AEW31446.1; -; Genomic_DNA.
DR EMBL; AP001184; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003419; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF455413; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC104827; AAI04828.1; -; mRNA.
DR EMBL; BC104797; AAI04798.1; -; mRNA.
DR CCDS; CCDS8168.1; -.
DR RefSeq; NP_001289888.1; NM_001302959.1.
DR RefSeq; NP_001289889.1; NM_001302960.1.
DR RefSeq; NP_003968.3; NM_003977.3.
DR PDB; 2LKN; NMR; -; A=2-166.
DR PDB; 4AIF; X-ray; 2.01 A; A/B=172-315.
DR PDB; 4APO; X-ray; 1.90 A; A/B=166-330.
DR PDBsum; 2LKN; -.
DR PDBsum; 4AIF; -.
DR PDBsum; 4APO; -.
DR AlphaFoldDB; O00170; -.
DR BMRB; O00170; -.
DR SMR; O00170; -.
DR BioGRID; 114511; 117.
DR DIP; DIP-34068N; -.
DR IntAct; O00170; 75.
DR MINT; O00170; -.
DR STRING; 9606.ENSP00000279146; -.
DR ChEMBL; CHEMBL4295645; -.
DR GlyGen; O00170; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O00170; -.
DR MetOSite; O00170; -.
DR PhosphoSitePlus; O00170; -.
DR BioMuta; AIP; -.
DR CPTAC; CPTAC-307; -.
DR CPTAC; CPTAC-308; -.
DR EPD; O00170; -.
DR jPOST; O00170; -.
DR MassIVE; O00170; -.
DR MaxQB; O00170; -.
DR PaxDb; O00170; -.
DR PeptideAtlas; O00170; -.
DR PRIDE; O00170; -.
DR ProteomicsDB; 47760; -.
DR Antibodypedia; 1367; 425 antibodies from 36 providers.
DR DNASU; 9049; -.
DR Ensembl; ENST00000279146.8; ENSP00000279146.3; ENSG00000110711.11.
DR GeneID; 9049; -.
DR KEGG; hsa:9049; -.
DR MANE-Select; ENST00000279146.8; ENSP00000279146.3; NM_003977.4; NP_003968.3.
DR UCSC; uc001olv.4; human.
DR CTD; 9049; -.
DR DisGeNET; 9049; -.
DR GeneCards; AIP; -.
DR GeneReviews; AIP; -.
DR HGNC; HGNC:358; AIP.
DR HPA; ENSG00000110711; Low tissue specificity.
DR MalaCards; AIP; -.
DR MIM; 102200; phenotype.
DR MIM; 600634; phenotype.
DR MIM; 605555; gene.
DR neXtProt; NX_O00170; -.
DR OpenTargets; ENSG00000110711; -.
DR Orphanet; 963; Acromegaly.
DR Orphanet; 314777; Familial isolated pituitary adenoma.
DR Orphanet; 314790; Null pituitary adenoma.
DR Orphanet; 99725; Pituitary gigantism.
DR Orphanet; 2965; Prolactinoma.
DR Orphanet; 314786; Silent pituitary adenoma.
DR PharmGKB; PA24652; -.
DR VEuPathDB; HostDB:ENSG00000110711; -.
DR eggNOG; KOG0545; Eukaryota.
DR GeneTree; ENSGT00390000001289; -.
DR InParanoid; O00170; -.
DR OMA; QQHERNV; -.
DR OrthoDB; 1278789at2759; -.
DR PhylomeDB; O00170; -.
DR TreeFam; TF314507; -.
DR PathwayCommons; O00170; -.
DR Reactome; R-HSA-8937144; Aryl hydrocarbon receptor signalling.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR SignaLink; O00170; -.
DR SIGNOR; O00170; -.
DR BioGRID-ORCS; 9049; 85 hits in 1088 CRISPR screens.
DR ChiTaRS; AIP; human.
DR GeneWiki; AH_receptor-interacting_protein; -.
DR GenomeRNAi; 9049; -.
DR Pharos; O00170; Tbio.
DR PRO; PR:O00170; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O00170; protein.
DR Bgee; ENSG00000110711; Expressed in granulocyte and 165 other tissues.
DR ExpressionAtlas; O00170; baseline and differential.
DR Genevisible; O00170; HS.
DR GO; GO:0034751; C:aryl hydrocarbon receptor complex; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0017162; F:aryl hydrocarbon receptor binding; IEA:Ensembl.
DR GO; GO:0036004; F:GAF domain binding; IDA:UniProtKB.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:InterPro.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:HGNC-UCL.
DR GO; GO:0051344; P:negative regulation of cyclic-nucleotide phosphodiesterase activity; IEA:Ensembl.
DR GO; GO:0022417; P:protein maturation by protein folding; IDA:HGNC-UCL.
DR GO; GO:0006626; P:protein targeting to mitochondrion; IDA:HGNC-UCL.
DR GO; GO:0010738; P:regulation of protein kinase A signaling; IEA:Ensembl.
DR GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
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 3D-structure; Cushing syndrome; Cytoplasm; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..330
FT /note="AH receptor-interacting protein"
FT /id="PRO_0000075339"
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, ECO:0000269|PubMed:23300914"
FT REPEAT 231..264
FT /note="TPR 2"
FT /evidence="ECO:0000269|PubMed:23300914"
FT REPEAT 265..298
FT /note="TPR 3"
FT /evidence="ECO:0000255, ECO:0000255|PROSITE-
FT ProRule:PRU00339, ECO:0000269|PubMed:23300914"
FT MOD_RES 43
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 16
FT /note="R -> H (in dbSNP:rs145047094)"
FT /evidence="ECO:0000269|PubMed:17244780,
FT ECO:0000269|PubMed:17360484"
FT /id="VAR_043908"
FT VARIANT 47..54
FT /note="Missing (in PITA1; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:17244780"
FT /id="VAR_058407"
FT VARIANT 228
FT /note="Q -> K (in dbSNP:rs641081)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16728643, ECO:0000269|PubMed:17299063,
FT ECO:0000269|PubMed:9111057, ECO:0007744|PubMed:21269460"
FT /id="VAR_043909"
FT VARIANT 241
FT /note="K -> E (in PITA1; unknown pathological significance;
FT dbSNP:rs267606573)"
FT /evidence="ECO:0000269|PubMed:17244780"
FT /id="VAR_043910"
FT VARIANT 248
FT /note="Missing (in PITA1; ACTH-secreting pituitary adenoma;
FT unknown pathological significance; dbSNP:rs267606574)"
FT /evidence="ECO:0000269|PubMed:18410548"
FT /id="VAR_043911"
FT VARIANT 271
FT /note="R -> W (in PITA1; unknown pathological significance;
FT dbSNP:rs267606579)"
FT /evidence="ECO:0000269|PubMed:17244780"
FT /id="VAR_043912"
FT VARIANT 304
FT /note="R -> Q (in PITA1; ACTH-secreting pituitary adenoma;
FT dbSNP:rs104894190)"
FT /evidence="ECO:0000269|PubMed:17360484"
FT /id="VAR_043913"
FT VARIANT 307
FT /note="R -> Q (in dbSNP:rs4930199)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16728643, ECO:0000269|PubMed:8972861,
FT ECO:0000269|PubMed:9111057"
FT /id="VAR_061545"
FT HELIX 4..9
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:2LKN"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 72..77
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:2LKN"
FT TURN 113..117
FT /evidence="ECO:0007829|PDB:2LKN"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 140..143
FT /evidence="ECO:0007829|PDB:2LKN"
FT STRAND 149..158
FT /evidence="ECO:0007829|PDB:2LKN"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:2LKN"
FT HELIX 173..176
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 195..213
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 221..243
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 248..260
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 281..294
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 299..311
FT /evidence="ECO:0007829|PDB:4APO"
FT HELIX 314..324
FT /evidence="ECO:0007829|PDB:4APO"
SQ SEQUENCE 330 AA; 37664 MW; C331AA6D0F8D8F53 CRC64;
MADIIARLRE DGIQKRVIQE GRGELPDFQD GTKATFHYRT LHSDDEGTVL DDSRARGKPM
ELIIGKKFKL PVWETIVCTM REGEIAQFLC DIKHVVLYPL VAKSLRNIAV GKDPLEGQRH
CCGVAQMREH SSLGHADLDA LQQNPQPLIF HMEMLKVESP GTYQQDPWAM TDEEKAKAVP
LIHQEGNRLY REGHVKEAAA KYYDAIACLK NLQMKEQPGS PEWIQLDQQI TPLLLNYCQC
KLVVEEYYEV LDHCSSILNK YDDNVKAYFK RGKAHAAVWN AQEAQADFAK VLELDPALAP
VVSRELRALE ARIRQKDEED KARFRGIFSH
