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   28-JAN-2026, entry version 208.
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; P68400: CSNK2A1; NbExp=2; IntAct=EBI-704197, EBI-347804;
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       O00170; O60809: PRAMEF10; NbExp=2; IntAct=EBI-704197, EBI-21648956;
CC       O00170; Q0VAF6: SYCN; NbExp=2; IntAct=EBI-704197, EBI-20898442;
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   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="https://atlasgeneticsoncology.org/gene/604/AIP";
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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_003977.4.
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   PDB; 7ZUB; EM; 2.85 A; C=1-330.
DR   PDB; 8QMO; EM; 2.76 A; C=1-330.
DR   PDBsum; 2LKN; -.
DR   PDBsum; 4AIF; -.
DR   PDBsum; 4APO; -.
DR   PDBsum; 7ZUB; -.
DR   PDBsum; 8QMO; -.
DR   AlphaFoldDB; O00170; -.
DR   BMRB; O00170; -.
DR   EMDB; EMD-14971; -.
DR   EMDB; EMD-18498; -.
DR   SMR; O00170; -.
DR   BioGRID; 114511; 204.
DR   CORUM; O00170; -.
DR   DIP; DIP-34068N; -.
DR   FunCoup; O00170; 2458.
DR   IntAct; O00170; 115.
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   jPOST; O00170; -.
DR   MassIVE; O00170; -.
DR   PaxDb; 9606-ENSP00000279146; -.
DR   PeptideAtlas; O00170; -.
DR   ProteomicsDB; 47760; -.
DR   Pumba; O00170; -.
DR   Antibodypedia; 1367; 418 antibodies from 35 providers.
DR   DNASU; 9049; -.
DR   Ensembl; ENST00000279146.8; ENSP00000279146.3; ENSG00000110711.12.
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   AGR; HGNC:358; -.
DR   ClinPGx; PA24652; -.
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; 605555; gene.
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   VEuPathDB; HostDB:ENSG00000110711; -.
DR   eggNOG; KOG0545; Eukaryota.
DR   GeneTree; ENSGT00390000001289; -.
DR   InParanoid; O00170; -.
DR   OMA; SHCCGMM; -.
DR   OrthoDB; 5829758at2759; -.
DR   PAN-GO; O00170; 0 GO annotations based on evolutionary models.
DR   PhylomeDB; O00170; -.
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   Agora; ENSG00000110711; -.
DR   BioGRID-ORCS; 9049; 88 hits in 1166 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; AIP; human.
DR   EvolutionaryTrace; O00170; -.
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 167 other cell types or tissues.
DR   ExpressionAtlas; O00170; baseline and differential.
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; IDA:HGNC-UCL.
DR   GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR   GO; GO:0051082; F:unfolded protein binding; IDA:HGNC-UCL.
DR   GO; GO:0051604; P:protein maturation; IDA:HGNC-UCL.
DR   GO; GO:0006626; P:protein targeting to mitochondrion; IDA:HGNC-UCL.
DR   GO; GO:0006805; P:xenobiotic metabolic process; IEA:Ensembl.
DR   FunFam; 1.25.40.10:FF:000052; Aryl-hydrocarbon-interacting protein-like 1; 1.
DR   FunFam; 3.10.50.40:FF:000018; Aryl-hydrocarbon-interacting protein-like 1; 1.
DR   Gene3D; 3.10.50.40; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   InterPro; IPR039663; AIP/AIPL1/TTC9.
DR   InterPro; IPR056277; PPIase_AIP.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR001179; PPIase_FKBP_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR11242:SF3; AH RECEPTOR-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR11242; ARYL HYDROCARBON RECEPTOR INTERACTING PROTEIN RELATED; 1.
DR   Pfam; PF23322; PPIase_AIP; 1.
DR   SUPFAM; SSF54534; FKBP-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 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   Proteomics identification; 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; uncertain 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; uncertain significance;
FT                   dbSNP:rs267606573)"
FT                   /evidence="ECO:0000269|PubMed:17244780"
FT                   /id="VAR_043910"
FT   VARIANT         248
FT                   /note="Missing (in PITA1; uncertain significance;
FT                   ACTH-secreting pituitary adenoma; dbSNP:rs267606574)"
FT                   /evidence="ECO:0000269|PubMed:18410548"
FT                   /id="VAR_043911"
FT   VARIANT         271
FT                   /note="R -> W (in PITA1; uncertain 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..11
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          15..19
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          33..46
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          49..53
FT                   /evidence="ECO:0007829|PDB:7ZUB"
FT   TURN            54..57
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          60..66
FT                   /evidence="ECO:0007829|PDB:7ZUB"
FT   HELIX           72..78
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          85..88
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   TURN            92..94
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   HELIX           98..100
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   TURN            101..107
FT                   /evidence="ECO:0007829|PDB:8QMO"
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..142
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   STRAND          148..158
FT                   /evidence="ECO:0007829|PDB:8QMO"
FT   TURN            160..162
FT                   /evidence="ECO:0007829|PDB:2LKN"
FT   HELIX           167..169
FT                   /evidence="ECO:0007829|PDB:8QMO"
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"
FT   STRAND          325..327
FT                   /evidence="ECO:0007829|PDB:7ZUB"
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
//