PTHY_HUMAN
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 03-AUG-2022, entry version 208.
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";
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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 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 AlphaFoldDB; P01270; -.
DR BMRB; P01270; -.
DR SMR; P01270; -.
DR BioGRID; 111713; 10.
DR CORUM; P01270; -.
DR IntAct; P01270; 5.
DR STRING; 9606.ENSP00000282091; -.
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; P01270; -.
DR PeptideAtlas; P01270; -.
DR PRIDE; P01270; -.
DR ABCD; P01270; 13 sequenced antibodies.
DR Antibodypedia; 11928; 2222 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 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; 1482128at2759; -.
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 Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR SignaLink; P01270; -.
DR SIGNOR; P01270; -.
DR BioGRID-ORCS; 5741; 14 hits in 1038 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 pigmented layer of retina and 93 other tissues.
DR Genevisible; P01270; HS.
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:0047485; F:protein N-terminus binding; IMP:CAFA.
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:0006874; P:cellular calcium ion homeostasis; IEA:Ensembl.
DR GO; GO:0034645; P:cellular macromolecule biosynthetic process; IDA:MGI.
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: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: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; PTHR10541; 1.
DR Pfam; PF01279; Parathyroid; 1.
DR PIRSF; PIRSF001832; PTH; 1.
DR SMART; SM00087; PTH; 1.
DR PROSITE; PS00335; PARATHYROID; 1.
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
