ID PTHY_HUMAN Reviewed; 115 AA. AC P01270; Q4VB48; Q9UD38; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 27-MAR-2024, entry version 217. DE RecName: Full=Parathyroid hormone; DE Short=PTH; DE AltName: Full=Parathormone; DE AltName: Full=Parathyrin; DE Flags: Precursor; GN Name=PTH; 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]. RX PubMed=6950381; DOI=10.1073/pnas.78.12.7365; RA Hendy G.N., Kronenberg H.M., Potts J.T. Jr., Rich A.; RT "Nucleotide sequence of cloned cDNAs encoding human preproparathyroid RT hormone."; RL Proc. Natl. Acad. Sci. U.S.A. 78:7365-7369(1981). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=6220408; DOI=10.1073/pnas.80.8.2127; RA Vasicek T.J., McCevitt B.E., Freeman M.W., Fennick B.J., Hendy G.N., RA Potts J.T. Jr., Rich A., Kronenberg H.M.; RT "Nucleotide sequence of the human parathyroid hormone gene."; RL Proc. Natl. Acad. Sci. U.S.A. 80:2127-2131(1983). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. 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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-31, MUTAGENESIS OF ALA-16, AND VARIANT RP ARG-18. RX PubMed=7829495; DOI=10.1074/jbc.270.4.1629; RA Karaplis A.C., Lim S.-K., Baba H., Arnold A., Kronenberg H.M.; RT "Inefficient membrane targeting, translocation, and proteolytic processing RT by signal peptidase of a mutant preproparathyroid hormone protein."; RL J. Biol. Chem. 270:1629-1635(1995). RN [5] RP PROTEIN SEQUENCE OF 26-37. RX PubMed=4833516; DOI=10.1038/249155a0; RA Jacobs J.W., Kemper B., Niall H.D., Habener J.F., Potts J.T. Jr.; RT "Structural analysis of human proparathyroid hormone by a new RT microsequencing approach."; RL Nature 249:155-157(1974). RN [6] RP PROTEIN SEQUENCE OF 26-40. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally verified RT cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [7] RP PROTEIN SEQUENCE OF 32-68. RX PubMed=4521809; DOI=10.1073/pnas.71.2.384; RA Niall H.D., Sauer R.T., Jacobs J.W., Keutmann H.T., Segre G.V., RA O'Riordan J.L.H., Aurbach G.D., Potts J.T. Jr.; RT "The amino-acid sequence of the amino-terminal 37 residues of human RT parathyroid hormone."; RL Proc. Natl. Acad. Sci. U.S.A. 71:384-388(1974). RN [8] RP PROTEIN SEQUENCE OF 61-83 AND 84-115. RX PubMed=728431; DOI=10.1021/bi00619a019; RA Keutmann H.T., Sauer M.M., Hendy G.N., O'Riordan J.L.H., Potts J.T. Jr.; RT "Complete amino acid sequence of human parathyroid hormone."; RL Biochemistry 17:5723-5729(1978). RN [9] RP PROTEIN SEQUENCE OF 75-100. RA Keutmann H.T., Niall H.D., Jacobs J.W., Barling P.M., Hendy G.N., RA O'Riordan J.L.H., Potts J.T. Jr.; RL (In) Talmadge R.V., Owen M., Parsons J.A. (eds.); RL Calcium-regulating hormones, pp.9-14, Excerpta Medica Foundation, Amsterdam RL (1975). RN [10] RP SEQUENCE REVISION. RX PubMed=1125201; DOI=10.1021/bi00680a006; RA Keutmann H.T., Niall H.D., O'Riordan J.L.H., Potts J.T. Jr.; RT "A reinvestigation of the amino-terminal sequence of human parathyroid RT hormone."; RL Biochemistry 14:1842-1847(1975). RN [11] RP SYNTHESIS OF 32-65. RX PubMed=4474131; DOI=10.1515/bchm2.1974.355.1.415; RA Tregear G.W., van Rietschoten J., Green E., Niall H.D., Keutmann H.T., RA Parsons J.A., O'Riordan J.L.H., Potts J.T. Jr.; RT "Solid-phase synthesis of the biologically active N-terminal 1-34 peptide RT of human parathyroid hormone."; RL Hoppe-Seyler's Z. Physiol. Chem. 355:415-421(1974). RN [12] RP SYNTHESIS OF 32-65. RX PubMed=4721748; DOI=10.1002/hlca.19730560139; RA Andreatta R.H., Hartmann A., Joehl A., Kamber B., Maier R., Riniker B., RA Rittel W., Sieber P.; RT "Synthesis of sequence 1-34 of human parathyroid hormone."; RL Helv. Chim. Acta 56:470-473(1973). RN [13] RP FUNCTION. RX PubMed=21076856; DOI=10.1007/s11010-010-0634-z; RA Zoidis E., Ghirlanda-Keller C., Schmid C.; RT "Stimulation of glucose transport in osteoblastic cells by parathyroid RT hormone and insulin-like growth factor I."; RL Mol. Cell. Biochem. 348:33-42(2011). RN [14] RP STRUCTURE BY NMR OF 32-65. RX PubMed=2069952; DOI=10.1021/bi00242a018; RA Klaus W., Dieckmann T., Wray V., Schomburg D., Wingender E., Mayer H.; RT "Investigation of the solution structure of the human parathyroid hormone RT fragment (1-34) by 1H NMR spectroscopy, distance geometry, and molecular RT dynamics calculations."; RL Biochemistry 30:6936-6942(1991). RN [15] RP STRUCTURE BY NMR OF 32-65. RX PubMed=8344299; DOI=10.1111/j.1432-1033.1993.tb18037.x; RA Barden J.A., Cuthbertson R.M.; RT "Stabilized NMR structure of human parathyroid hormone(1-34)."; RL Eur. J. Biochem. 215:315-321(1993). RN [16] RP STRUCTURE BY NMR OF 32-68. RX PubMed=7797503; DOI=10.1074/jbc.270.25.15194; RA Marx U.C., Austermann S., Bayer P., Adermann K., Ejchart A., Sticht H., RA Walter S., Schmid F.-X., Jaenicke R., Forssmann W.-G., Roesch P.; RT "Structure of human parathyroid hormone 1-37 in solution."; RL J. Biol. Chem. 270:15194-15202(1995). RN [17] RP STRUCTURE BY NMR OF 32-70. RX PubMed=10623601; DOI=10.1006/bbrc.1999.1958; RA Marx U.C., Adermann K., Bayer P., Forssmann W.-G., Rosch P.; RT "Solution structures of human parathyroid hormone fragments hPTH(1-34) and RT hPTH(1-39) and bovine parathyroid hormone fragment bPTH(1-37)."; RL Biochem. Biophys. Res. Commun. 267:213-220(2000). RN [18] RP X-RAY CRYSTALLOGRAPHY (0.9 ANGSTROMS) OF 32-65. RX PubMed=10837469; DOI=10.1074/jbc.m001134200; RA Jin L., Briggs S.L., Chandrasekhar S., Chirgadze N.Y., Clawson D.K., RA Schevitz R.W., Smiley D.L., Tashjian A.H., Zhang F.; RT "Crystal structure of human parathyroid hormone 1-34 at 0.9-A resolution."; RL J. Biol. Chem. 275:27238-27244(2000). RN [19] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 46-65 IN COMPLEX WITH PTH1R, RP INTERACTION WITH PTH1R, AND MUTAGENESIS OF ARG-51; TRP-54; LEU-55; LYS-58 RP AND LEU-59. RX PubMed=18375760; DOI=10.1073/pnas.0801027105; RA Pioszak A.A., Xu H.E.; RT "Molecular recognition of parathyroid hormone by its G protein-coupled RT receptor."; RL Proc. Natl. Acad. Sci. U.S.A. 105:5034-5039(2008). RN [20] RP VARIANT FIH1 ARG-18. RX PubMed=2212001; DOI=10.1172/jci114811; RA Arnold A., Horst S.A., Gardella T.J., Baba H., Levine M.A., RA Kronenberg H.M.; RT "Mutation of the signal peptide-encoding region of the preproparathyroid RT hormone gene in familial isolated hypoparathyroidism."; RL J. Clin. Invest. 86:1084-1087(1990). RN [21] RP VARIANT FIH1 PRO-23. RX PubMed=10523031; DOI=10.1210/jcem.84.10.6070; RA Sunthornthepvarakul T., Churesigaew S., Ngowngarmratana S.; RT "A novel mutation of the signal peptide of the preproparathyroid hormone RT gene associated with autosomal recessive familial isolated RT hypoparathyroidism."; RL J. Clin. Endocrinol. Metab. 84:3792-3796(1999). RN [22] RP CHARACTERIZATION OF VARIANT FIH1 ARG-18. RX PubMed=18056632; DOI=10.1073/pnas.0708725104; RA Datta R., Waheed A., Shah G.N., Sly W.S.; RT "Signal sequence mutation in autosomal dominant form of hypoparathyroidism RT induces apoptosis that is corrected by a chemical chaperone."; RL Proc. Natl. Acad. Sci. U.S.A. 104:19989-19994(2007). CC -!- FUNCTION: PTH elevates calcium level by dissolving the salts in bone CC and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D- CC glucose (2DG) transport and glycogen synthesis in osteoblastic cells. CC {ECO:0000269|PubMed:21076856}. CC -!- SUBUNIT: Interacts with PTH1R (via N-terminal extracellular domain). CC {ECO:0000269|PubMed:18375760}. CC -!- INTERACTION: CC P01270; Q12797-6: ASPH; NbExp=3; IntAct=EBI-716817, EBI-12092171; CC P01270; Q03431: PTH1R; NbExp=6; IntAct=EBI-716817, EBI-2860297; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DISEASE: Hypoparathyroidism, familial isolated, 1 (FIH1) [MIM:146200]: CC A form of hypoparathyroidism, a disorder characterized by hypocalcemia CC and hyperphosphatemia due to a deficiency of parathyroid hormone. CC Clinical features include seizures, tetany and cramps. FIH1 inheritance CC can be autosomal dominant or recessive. {ECO:0000269|PubMed:10523031, CC ECO:0000269|PubMed:18056632, ECO:0000269|PubMed:2212001}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the parathyroid hormone family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Parathyroid hormone entry; CC URL="https://en.wikipedia.org/wiki/Parathyroid_hormone"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; V00597; CAA23843.1; -; mRNA. DR EMBL; J00301; AAA60215.1; -; Genomic_DNA. DR EMBL; BC096142; AAH96142.1; -; mRNA. DR EMBL; BC096143; AAH96143.1; -; mRNA. DR EMBL; BC096144; AAH96144.1; -; mRNA. DR EMBL; BC096145; AAH96145.1; -; mRNA. DR CCDS; CCDS7812.1; -. DR PIR; A19339; PTHU. DR RefSeq; NP_000306.1; NM_000315.3. DR PDB; 1BWX; NMR; -; A=32-70. DR PDB; 1ET1; X-ray; 0.90 A; A/B=32-65. DR PDB; 1FVY; NMR; -; A=32-62. DR PDB; 1HPH; NMR; -; A=32-68. DR PDB; 1HPY; NMR; -; A=32-65. DR PDB; 1HTH; NMR; -; A=32-65. DR PDB; 1ZWA; NMR; -; A=32-65. DR PDB; 1ZWB; NMR; -; A=33-68. DR PDB; 1ZWD; NMR; -; A=34-68. DR PDB; 1ZWE; NMR; -; A=35-68. DR PDB; 1ZWF; NMR; -; A=35-68. DR PDB; 1ZWG; NMR; -; A=35-68. DR PDB; 2L1X; NMR; -; A=32-65. DR PDB; 3C4M; X-ray; 1.95 A; C/D=46-65. DR PDB; 7VVK; EM; 3.30 A; P=32-65. DR PDB; 7VVL; EM; 2.80 A; P=32-65. DR PDB; 7VVM; EM; 3.20 A; P=32-65. DR PDB; 7VVN; EM; 3.80 A; P=32-65. DR PDB; 7VVO; EM; 4.10 A; P=32-65. DR PDB; 7Y36; EM; 2.80 A; P=32-65. DR PDB; 8FLQ; EM; 2.55 A; P=32-65. DR PDB; 8HA0; EM; 2.62 A; P=32-65. DR PDB; 8HAO; EM; 3.76 A; H/P=32-65. DR PDBsum; 1BWX; -. DR PDBsum; 1ET1; -. DR PDBsum; 1FVY; -. DR PDBsum; 1HPH; -. DR PDBsum; 1HPY; -. DR PDBsum; 1HTH; -. DR PDBsum; 1ZWA; -. DR PDBsum; 1ZWB; -. DR PDBsum; 1ZWD; -. DR PDBsum; 1ZWE; -. DR PDBsum; 1ZWF; -. DR PDBsum; 1ZWG; -. DR PDBsum; 2L1X; -. DR PDBsum; 3C4M; -. DR PDBsum; 7VVK; -. DR PDBsum; 7VVL; -. DR PDBsum; 7VVM; -. DR PDBsum; 7VVN; -. DR PDBsum; 7VVO; -. DR PDBsum; 7Y36; -. DR PDBsum; 8FLQ; -. DR PDBsum; 8HA0; -. DR PDBsum; 8HAO; -. DR AlphaFoldDB; P01270; -. DR BMRB; P01270; -. DR EMDB; EMD-32142; -. DR EMDB; EMD-32143; -. DR EMDB; EMD-32144; -. DR EMDB; EMD-32145; -. DR EMDB; EMD-32146; -. DR SMR; P01270; -. DR BioGRID; 111713; 10. DR CORUM; P01270; -. DR IntAct; P01270; 5. DR STRING; 9606.ENSP00000433208; -. DR BindingDB; P01270; -. DR DrugBank; DB05883; ABX-PTH. DR DrugBank; DB04419; D-norleucine. DR iPTMnet; P01270; -. DR MetOSite; P01270; -. DR PhosphoSitePlus; P01270; -. DR BioMuta; PTH; -. DR DMDM; 131547; -. DR PaxDb; 9606-ENSP00000282091; -. DR PeptideAtlas; P01270; -. DR ABCD; P01270; 13 sequenced antibodies. DR Antibodypedia; 11928; 2345 antibodies from 41 providers. DR DNASU; 5741; -. DR Ensembl; ENST00000282091.6; ENSP00000282091.1; ENSG00000152266.7. DR Ensembl; ENST00000529816.1; ENSP00000433208.1; ENSG00000152266.7. DR GeneID; 5741; -. DR KEGG; hsa:5741; -. DR MANE-Select; ENST00000282091.6; ENSP00000282091.1; NM_000315.4; NP_000306.1. DR UCSC; uc001mlb.4; human. DR AGR; HGNC:9606; -. DR CTD; 5741; -. DR DisGeNET; 5741; -. DR GeneCards; PTH; -. DR HGNC; HGNC:9606; PTH. DR HPA; ENSG00000152266; Tissue enriched (parathyroid). DR MalaCards; PTH; -. DR MIM; 146200; phenotype. DR MIM; 168450; gene. DR neXtProt; NX_P01270; -. DR OpenTargets; ENSG00000152266; -. DR Orphanet; 189466; Familial isolated hypoparathyroidism due to impaired PTH secretion. DR PharmGKB; PA33951; -. DR VEuPathDB; HostDB:ENSG00000152266; -. DR eggNOG; ENOG502SB2W; Eukaryota. DR GeneTree; ENSGT00390000018603; -. DR HOGENOM; CLU_164143_0_0_1; -. DR InParanoid; P01270; -. DR OMA; HNLGEHR; -. DR OrthoDB; 4209197at2759; -. DR PhylomeDB; P01270; -. DR TreeFam; TF336197; -. DR PathwayCommons; P01270; -. DR Reactome; R-HSA-373080; Class B/2 (Secretin family receptors). DR Reactome; R-HSA-418555; G alpha (s) signalling events. DR SignaLink; P01270; -. DR SIGNOR; P01270; -. DR BioGRID-ORCS; 5741; 14 hits in 1116 CRISPR screens. DR EvolutionaryTrace; P01270; -. DR GeneWiki; Parathyroid_hormone; -. DR GenomeRNAi; 5741; -. DR Pharos; P01270; Tbio. DR PRO; PR:P01270; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P01270; Protein. DR Bgee; ENSG00000152266; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 92 other cell types or tissues. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IBA:GO_Central. DR GO; GO:0005179; F:hormone activity; IMP:CAFA. DR GO; GO:0031856; F:parathyroid hormone receptor binding; IBA:GO_Central. DR GO; GO:0051428; F:peptide hormone receptor binding; IDA:UniProtKB. DR GO; GO:0048018; F:receptor ligand activity; IMP:CAFA. DR GO; GO:0031857; F:type 1 parathyroid hormone receptor binding; IMP:CAFA. DR GO; GO:0007202; P:activation of phospholipase C activity; IMP:CAFA. DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:MGI. DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl. DR GO; GO:0045453; P:bone resorption; NAS:UniProtKB. DR GO; GO:0046058; P:cAMP metabolic process; TAS:ProtInc. DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl. DR GO; GO:0008628; P:hormone-mediated apoptotic signaling pathway; TAS:ProtInc. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; IEA:Ensembl. DR GO; GO:0009059; P:macromolecule biosynthetic process; IDA:MGI. DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:Ensembl. DR GO; GO:0071866; P:negative regulation of apoptotic process in bone marrow cell; IEA:Ensembl. DR GO; GO:1900158; P:negative regulation of bone mineralization involved in bone maturation; IEA:Ensembl. DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IEA:Ensembl. DR GO; GO:0010629; P:negative regulation of gene expression; IDA:GO_Central. DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl. DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB. DR GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IEA:Ensembl. DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl. DR GO; GO:0046326; P:positive regulation of glucose import; IDA:UniProtKB. DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IDA:UniProtKB. DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IMP:CAFA. DR GO; GO:0090290; P:positive regulation of osteoclast proliferation; IEA:Ensembl. DR GO; GO:0009967; P:positive regulation of signal transduction; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI. DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl. DR GO; GO:0045471; P:response to ethanol; IEA:Ensembl. DR GO; GO:0071774; P:response to fibroblast growth factor; IEA:Ensembl. DR GO; GO:0010288; P:response to lead ion; IEA:Ensembl. DR GO; GO:0071107; P:response to parathyroid hormone; IEA:Ensembl. DR GO; GO:0033280; P:response to vitamin D; IEA:Ensembl. DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl. DR GO; GO:0007266; P:Rho protein signal transduction; IEA:Ensembl. DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc. DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl. DR InterPro; IPR003625; PTH. DR InterPro; IPR001415; PTH/PTH-rel. DR PANTHER; PTHR10541; PARATHYROID HORMONE; 1. DR PANTHER; PTHR10541:SF2; PARATHYROID HORMONE; 1. DR Pfam; PF01279; Parathyroid; 1. DR PIRSF; PIRSF001832; PTH; 1. DR SMART; SM00087; PTH; 1. DR PROSITE; PS00335; PARATHYROID; 1. DR Genevisible; P01270; HS. PE 1: Evidence at protein level; KW 3D-structure; Cleavage on pair of basic residues; KW Direct protein sequencing; Disease variant; Hormone; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..25 FT /evidence="ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:4833516" FT PROPEP 26..31 FT /evidence="ECO:0000269|PubMed:4521809" FT /id="PRO_0000023249" FT CHAIN 32..115 FT /note="Parathyroid hormone" FT /id="PRO_0000023250" FT REGION 51..69 FT /note="Important for receptor binding" FT REGION 73..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..102 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VARIANT 18 FT /note="C -> R (in FIH1; dominant form; leads to inefficient FT processing of the precursor; the expressed mutant hormone FT is trapped intracellularly in the endoplasmic reticulum FT resulting in apoptosis; mutant protein-expressing cells FT also show marked up-regulation of the endoplasmic reticulum FT stress-responsive hormones HSPA5 and EIF2AK3 and the FT proapoptotic transcription factor DDIT3; FT dbSNP:rs104894271)" FT /evidence="ECO:0000269|PubMed:18056632, FT ECO:0000269|PubMed:2212001, ECO:0000269|PubMed:7829495" FT /id="VAR_006047" FT VARIANT 23 FT /note="S -> P (in FIH1; recessive form; might lead to FT inefficient processing of the precursor; FT dbSNP:rs104894272)" FT /evidence="ECO:0000269|PubMed:10523031" FT /id="VAR_018464" FT MUTAGEN 16 FT /note="A->R: Abolishes processing of the precursor; when FT associated with variant R-18." FT /evidence="ECO:0000269|PubMed:7829495" FT MUTAGEN 51 FT /note="R->A: Reduced affinity for PTH1R." FT /evidence="ECO:0000269|PubMed:18375760" FT MUTAGEN 54 FT /note="W->A: Strongly reduced affinity for PTH1R." FT /evidence="ECO:0000269|PubMed:18375760" FT MUTAGEN 55 FT /note="L->A: Strongly reduced affinity for PTH1R." FT /evidence="ECO:0000269|PubMed:18375760" FT MUTAGEN 58 FT /note="K->A: Reduced affinity for PTH1R." FT /evidence="ECO:0000269|PubMed:18375760" FT MUTAGEN 59 FT /note="L->A: Strongly reduced affinity for PTH1R." FT /evidence="ECO:0000269|PubMed:18375760" FT CONFLICT 107 FT /note="N -> D (in Ref. 8; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 34..64 FT /evidence="ECO:0007829|PDB:1ET1" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1ZWF" SQ SEQUENCE 115 AA; 12861 MW; 849015736A6E5597 CRC64; MIPAKDMAKV MIVMLAICFL TKSDGKSVKK RSVSEIQLMH NLGKHLNSME RVEWLRKKLQ DVHNFVALGA PLAPRDAGSQ RPRKKEDNVL VESHEKSLGE ADKADVNVLT KAKSQ //