ID PTHR_HUMAN Reviewed; 177 AA.
AC P12272; Q15251; Q6FH74;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 29-MAY-2013, entry version 153.
DE RecName: Full=Parathyroid hormone-related protein;
DE Short=PTH-rP;
DE Short=PTHrP;
DE AltName: Full=Parathyroid hormone-like protein;
DE Short=PLP;
DE Contains:
DE RecName: Full=PTHrP[1-36];
DE Contains:
DE RecName: Full=PTHrP[38-94];
DE Contains:
DE RecName: Full=Osteostatin;
DE AltName: Full=PTHrP[107-139];
DE Flags: Precursor;
GN Name=PTHLH; Synonyms=PTHRP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=3616618; DOI=10.1126/science.3616618;
RA Suva L.J., Winslow G.A., Wettenhall R.E.H., Hammonds R.G.,
RA Moseley J.M., Diefenbach-Jagger H., Rodda C.P., Kemp B.E.,
RA Rodriguez H., Chen E.Y., Hudson P.J., Martin T.J., Wood W.I.;
RT "A parathyroid hormone-related protein implicated in malignant
RT hypercalcemia: cloning and expression.";
RL Science 237:893-896(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2829195; DOI=10.1073/pnas.85.2.597;
RA Mangin M., Webb A.C., Dreyer B.E., Posillico J.T., Ikeda K.,
RA Weir E.C., Stewart A.F., Bander N.H., Milstone L., Barton D.E.,
RA Francke U., Broadus A.E.;
RT "Identification of a cDNA encoding a parathyroid hormone-like peptide
RT from a human tumor associated with humoral hypercalcemia of
RT malignancy.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:597-601(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2708388;
RA Yasuda T., Banville D., Hendy G.N., Goltzman D.;
RT "Characterization of the human parathyroid hormone-like peptide gene.
RT Functional and evolutionary aspects.";
RL J. Biol. Chem. 264:7720-7725(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=3290897; DOI=10.1073/pnas.85.13.4605;
RA Thiede M.A., Strewler G.J., Nissenson R.A., Rosenblatt M., Rodan G.A.;
RT "Human renal carcinoma expresses two messages encoding a parathyroid
RT hormone-like peptide: evidence for the alternative splicing of a
RT single-copy gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4605-4609(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE OF 1-33.
RC TISSUE=Liver;
RX PubMed=2744490; DOI=10.1016/0378-1119(89)90363-6;
RA Suva L.J., Mather K.A., Gillespie M.T., Webb G.C., Ng K.W.,
RA Winslow G.A., Wood W.I., Martin T.J., Hudson P.J.;
RT "Structure of the 5' flanking region of the gene encoding human
RT parathyroid-hormone-related protein (PTHrP).";
RL Gene 77:95-105(1989).
RN [9]
RP PROTEIN SEQUENCE OF 37-52.
RX PubMed=2885845; DOI=10.1073/pnas.84.14.5048;
RA Moseley J.M., Kubota M., Diefenbach-Jagger H., Wettenhall R.E.H.,
RA Kemp B.E., Suva L.J., Rodda C.P., Ebeling P.R., Hudson P.J.,
RA Zajac J.D., Martin T.J.;
RT "Parathyroid hormone-related protein purified from a human lung cancer
RT cell line.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:5048-5052(1987).
RN [10]
RP ALTERNATIVE SPLICING (ISOFORM 3).
RX PubMed=2928340; DOI=10.1073/pnas.86.7.2408;
RA Mangin M., Ikeda K., Dreyer B.E., Broadus A.E.;
RT "Isolation and characterization of the human parathyroid hormone-like
RT peptide gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2408-2412(1989).
RN [11]
RP CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
RX PubMed=1915066;
RA Fenton A.J., Kemp B.E., Kent G.N., Moseley J.M., Zheng M.H.,
RA Rowe D.J., Britto J.M., Martin T.J., Nicholson G.C.;
RT "A carboxyl-terminal peptide from the parathyroid hormone-related
RT protein inhibits bone resorption by osteoclasts.";
RL Endocrinology 129:1762-1768(1991).
RN [12]
RP CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
RX PubMed=1954916;
RA Fenton A.J., Kemp B.E., Hammonds R.G., Mitchelhill K., Moseley J.M.,
RA Martin T.J., Nicholson G.C.;
RT "A potent inhibitor of osteoclastic bone resorption within a highly
RT conserved pentapeptide region of parathyroid hormone-related protein;
RT PTHrP107-111.";
RL Endocrinology 129:3424-3426(1991).
RN [13]
RP CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
RX PubMed=9144344; DOI=10.1359/jbmr.1997.12.5.778;
RA Martinez M.E., Garcia-Ocana A., Sanchez M., Medina S., del Campo T.,
RA Valin A., Sanchez-Cabezudo M.J., Esbrit P.;
RT "C-terminal parathyroid hormone-related protein inhibits proliferation
RT and differentiation of human osteoblast-like cells.";
RL J. Bone Miner. Res. 12:778-785(1997).
RN [14]
RP CHARACTERIZATION OF OSTEOSTATIN ACTIVITY.
RX PubMed=9048639; DOI=10.1210/en.138.3.1299;
RA Cornish J., Callon K.E., Nicholson G.C., Reid I.R.;
RT "Parathyroid hormone-related protein-(107-139) inhibits bone
RT resorption in vivo.";
RL Endocrinology 138:1299-1304(1997).
RN [15]
RP NUCLEOCYTOPLASMIC SHUTTLING.
RX PubMed=12852260; DOI=10.1016/S0083-6729(03)01010-0;
RA Jans D.A., Thomas R.J., Gillespie M.T.;
RT "Parathyroid hormone-related protein (PTHrP): a nucleocytoplasmic
RT shuttling protein with distinct paracrine and intracrine roles.";
RL Vitam. Horm. 66:345-384(2003).
RN [16]
RP NUCLEAR LOCALIZATION SIGNAL.
RX PubMed=11401507; DOI=10.1006/bbrc.2001.4607;
RA Lam M.H., Hu W., Xiao C.Y., Gillespie M.T., Jans D.A.;
RT "Molecular dissection of the importin beta1-recognized nuclear
RT targeting signal of parathyroid hormone-related protein.";
RL Biochem. Biophys. Res. Commun. 282:629-634(2001).
RN [17]
RP REVIEW.
RX PubMed=12538599; DOI=10.1210/en.2002-220818;
RA Fiaschi-Taesch N.M., Stewart A.F.;
RT "Minireview: parathyroid hormone-related protein as an intracrine
RT factor -- trafficking mechanisms and functional consequences.";
RL Endocrinology 144:407-411(2003).
RN [18]
RP FUNCTION.
RX PubMed=20637541; DOI=10.1016/j.canlet.2010.06.009;
RA Mula R.V., Bhatia V., Falzon M.;
RT "PTHrP promotes colon cancer cell migration and invasion in an
RT integrin alpha6beta4-dependent manner through activation of Rac1.";
RL Cancer Lett. 298:119-127(2010).
RN [19]
RP STRUCTURE BY NMR OF 37-70.
RX PubMed=10050767; DOI=10.1016/S0014-5793(98)01658-5;
RA Weidler M., Marx U.C., Seidel G., Schafer W., Hoffmann E., Esswein A.,
RA Rosch P.;
RT "The structure of human parathyroid hormone-related protein(1-34) in
RT near-physiological solution.";
RL FEBS Lett. 444:239-244(1999).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 103-130.
RX PubMed=12504010; DOI=10.1016/S1097-2765(02)00727-X;
RA Cingolani G., Bednenko J., Gillespie M.T., Gerace L.;
RT "Molecular basis for the recognition of a nonclassical nuclear
RT localization signal by importin beta.";
RL Mol. Cell 10:1345-1353(2002).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (1.94 ANGSTROMS) OF 48-70 IN COMPLEX WITH PTH1R,
RP INTERACTION WITH PTH1R, AND MUTAGENESIS OF ARG-57; PHE-59; LEU-60;
RP LEU-63; ILE-64 AND HIS-68.
RX PubMed=19674967; DOI=10.1074/jbc.M109.022905;
RA Pioszak A.A., Parker N.R., Gardella T.J., Xu H.E.;
RT "Structural basis for parathyroid hormone-related protein binding to
RT the parathyroid hormone receptor and design of conformation-selective
RT peptides.";
RL J. Biol. Chem. 284:28382-28391(2009).
RN [22]
RP VARIANT [LARGE SCALE ANALYSIS] THR-169.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal
RT cancers.";
RL Science 314:268-274(2006).
RN [23]
RP VARIANTS BDE2 PRO-44 AND PRO-60.
RX PubMed=20170896; DOI=10.1016/j.ajhg.2010.01.023;
RA Klopocki E., Hennig B.P., Dathe K., Koll R., de Ravel T., Baten E.,
RA Blom E., Gillerot Y., Weigel J.F., Krueger G., Hiort O., Seemann P.,
RA Mundlos S.;
RT "Deletion and point mutations of PTHLH cause brachydactyly type E.";
RL Am. J. Hum. Genet. 86:434-439(2010).
CC -!- FUNCTION: Neuroendocrine peptide which is a critical regulator of
CC cellular and organ growth, development, migration, differentiation
CC and survival and of epithelial calcium ion transport. Regulates
CC endochondral bone development and epithelial-mesenchymal
CC interactions during the formation of the mammary glands and teeth.
CC Required for skeletal homeostasis. Promotes mammary mesenchyme
CC differentiation and bud outgrowth by modulating mesenchymal cell
CC responsiveness to BMPs. Upregulates BMPR1A expression in the
CC mammary mesenchyme and this increases the sensitivity of these
CC cells to BMPs and allows them to respond to BMP4 in a paracrine
CC and/or autocrine fashion. BMP4 signaling in the mesenchyme, in
CC turn, triggers epithelial outgrowth and augments MSX2 expression,
CC which causes the mammary mesenchyme to inhibit hair follicle
CC formation within the nipple sheath (By similarity). Promotes colon
CC cancer cell migration and invasion in an integrin alpha-6/beta-1-
CC dependent manner through activation of Rac1.
CC -!- FUNCTION: Osteostatin is a potent inhibitor of osteoclastic bone
CC resorption.
CC -!- SUBUNIT: PTHrP interacts with PTH1R (via N-terminal extracellular
CC domain).
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Comment=Additional isoforms seem to exist;
CC Name=1;
CC IsoId=P12272-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P12272-2; Sequence=VSP_004534;
CC Name=3;
CC IsoId=P12272-3; Sequence=VSP_004535;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Also expressed in the mammary
CC gland.
CC -!- PTM: There are 3 principal secretory forms, called PTHrP[1-36],
CC PTHrP[38-94], and osteostatin (PTHrP[107-139]) arising from
CC endoproteolytic cleavage of the initial translation product. Each
CC of these secretory forms is believed to have one or more of its
CC own receptors that mediates the normal paracrine, autocrine and
CC endocrine actions.
CC -!- DISEASE: Brachydactyly E2 (BDE2) [MIM:613382]: A form of
CC brachydactyly. Brachydactyly defines a group of inherited
CC malformations characterized by shortening of the digits due to
CC abnormal development of the phalanges and/or the metacarpals.
CC Brachydactyly type E is characterized by shortening of the fingers
CC mainly in the metacarpals and metatarsals. Wide variability in the
CC number of digits affected occurs from person to person, even in
CC the same family. Some individuals are moderately short of stature.
CC In brachydactyly type E2 variable combinations of metacarpals are
CC involved, with shortening also of the first and third distal and
CC the second and fifth middle phalanges. Note=The disease is caused
CC by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the parathyroid hormone family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/PTHLHID41897ch12p11.html";
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DR EMBL; M17183; AAA60221.1; -; Genomic_DNA.
DR EMBL; X14304; CAA32480.1; -; Genomic_DNA.
DR EMBL; J03580; AAA60216.1; ALT_SEQ; mRNA.
DR EMBL; M24349; AAA60358.1; -; Genomic_DNA.
DR EMBL; M24348; AAA60358.1; JOINED; Genomic_DNA.
DR EMBL; M24350; AAA60359.1; -; Genomic_DNA.
DR EMBL; M24348; AAA60359.1; JOINED; Genomic_DNA.
DR EMBL; M24349; AAA60359.1; JOINED; Genomic_DNA.
DR EMBL; M24351; AAA60360.1; -; Genomic_DNA.
DR EMBL; M24348; AAA60360.1; JOINED; Genomic_DNA.
DR EMBL; M24349; AAA60360.1; JOINED; Genomic_DNA.
DR EMBL; CR541882; CAG46680.1; -; mRNA.
DR EMBL; CH471094; EAW96573.1; -; Genomic_DNA.
DR EMBL; BC005961; AAH05961.1; -; mRNA.
DR EMBL; J03802; AAA60218.1; -; mRNA.
DR EMBL; M34071; AAA60217.1; -; mRNA.
DR IPI; IPI00221080; -.
DR IPI; IPI00221081; -.
DR IPI; IPI00414875; -.
DR PIR; A33360; PTHU2L.
DR PIR; C33360; PTHU3L.
DR RefSeq; NP_002811.1; NM_002820.2.
DR RefSeq; NP_945315.1; NM_198964.1.
DR RefSeq; NP_945316.1; NM_198965.1.
DR RefSeq; NP_945317.1; NM_198966.1.
DR UniGene; Hs.591159; -.
DR PDB; 1BZG; NMR; -; A=37-70.
DR PDB; 1ET3; Model; -; A=37-70.
DR PDB; 1M5N; X-ray; 2.90 A; Q=103-130.
DR PDB; 3FFD; X-ray; 2.00 A; P=37-144.
DR PDB; 3H3G; X-ray; 1.94 A; B=48-70.
DR PDBsum; 1BZG; -.
DR PDBsum; 1ET3; -.
DR PDBsum; 1M5N; -.
DR PDBsum; 3FFD; -.
DR PDBsum; 3H3G; -.
DR DisProt; DP00138; -.
DR ProteinModelPortal; P12272; -.
DR IntAct; P12272; 1.
DR MINT; MINT-1742626; -.
DR STRING; 9606.ENSP00000379213; -.
DR PhosphoSite; P12272; -.
DR DMDM; 131542; -.
DR PaxDb; P12272; -.
DR PRIDE; P12272; -.
DR DNASU; 5744; -.
DR Ensembl; ENST00000201015; ENSP00000201015; ENSG00000087494.
DR Ensembl; ENST00000354417; ENSP00000346398; ENSG00000087494.
DR Ensembl; ENST00000395868; ENSP00000379209; ENSG00000087494.
DR Ensembl; ENST00000395872; ENSP00000379213; ENSG00000087494.
DR Ensembl; ENST00000535992; ENSP00000440613; ENSG00000087494.
DR Ensembl; ENST00000538310; ENSP00000441890; ENSG00000087494.
DR Ensembl; ENST00000539239; ENSP00000441571; ENSG00000087494.
DR Ensembl; ENST00000545234; ENSP00000441765; ENSG00000087494.
DR GeneID; 5744; -.
DR KEGG; hsa:5744; -.
DR UCSC; uc001rik.3; human.
DR CTD; 5744; -.
DR GeneCards; GC12M028111; -.
DR HGNC; HGNC:9607; PTHLH.
DR HPA; HPA035982; -.
DR MIM; 168470; gene.
DR MIM; 613382; phenotype.
DR neXtProt; NX_P12272; -.
DR Orphanet; 93387; Brachydactyly type E.
DR PharmGKB; PA33952; -.
DR eggNOG; NOG40343; -.
DR HOGENOM; HOG000115765; -.
DR HOVERGEN; HBG003236; -.
DR InParanoid; P12272; -.
DR OMA; PATNTKN; -.
DR OrthoDB; EOG4N8R63; -.
DR Pathway_Interaction_DB; hedgehog_2pathway; Signaling events mediated by the Hedgehog family.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; P12272; -.
DR GenomeRNAi; 5744; -.
DR NextBio; 22362; -.
DR PMAP-CutDB; P12272; -.
DR ArrayExpress; P12272; -.
DR Bgee; P12272; -.
DR CleanEx; HS_PTHLH; -.
DR Genevestigator; P12272; -.
DR GermOnline; ENSG00000087494; Homo sapiens.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005179; F:hormone activity; TAS:ProtInc.
DR GO; GO:0051428; F:peptide hormone receptor binding; IDA:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G-protein coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0046058; P:cAMP metabolic process; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0001958; P:endochondral ossification; IEA:Compara.
DR GO; GO:0007492; P:endoderm development; IEA:Compara.
DR GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Compara.
DR GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR GO; GO:0048286; P:lung alveolus development; IEA:Compara.
DR GO; GO:0060649; P:mammary gland bud elongation; IEA:Compara.
DR GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IDA:MGI.
DR GO; GO:0043433; P:negative regulation of sequence-specific DNA binding transcription factor activity; IEA:Compara.
DR GO; GO:0060659; P:nipple sheath formation; IEA:Compara.
DR GO; GO:0002076; P:osteoblast development; IEA:Compara.
DR GO; GO:0030819; P:positive regulation of cAMP biosynthetic process; IDA:MGI.
DR GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
DR GO; GO:0016485; P:protein processing; IEA:Compara.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0001501; P:skeletal system development; IDA:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; IEA:Compara.
DR InterPro; IPR003626; PTH-rel.
DR InterPro; IPR001415; PTH/PTH-rel.
DR PANTHER; PTHR17223; PTHR17223; 1.
DR Pfam; PF01279; Parathyroid; 1.
DR SMART; SM00087; PTH; 1.
DR PROSITE; PS00335; PARATHYROID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium;
KW Cleavage on pair of basic residues; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Disease mutation; Hormone; Nucleus;
KW Polymorphism; Reference proteome; Secreted; Signal.
FT SIGNAL 1 24 Potential.
FT PROPEP 25 34
FT /FTId=PRO_0000023224.
FT CHAIN 37 177 Parathyroid hormone-related protein.
FT /FTId=PRO_0000023225.
FT PEPTIDE 37 72 PTHrP[1-36].
FT /FTId=PRO_0000023226.
FT PEPTIDE 74 130 PTHrP[38-94].
FT /FTId=PRO_0000023227.
FT PEPTIDE 143 175 Osteostatin.
FT /FTId=PRO_0000023228.
FT REGION 57 68 Important for receptor binding.
FT MOTIF 108 129 Nuclear localization signal.
FT VAR_SEQ 176 177 Missing (in isoform 2).
FT /FTId=VSP_004534.
FT VAR_SEQ 176 177 RH -> TALLWGLKKKKENNRRTHHMQLMISLFKSPLLLL
FT (in isoform 3).
FT /FTId=VSP_004535.
FT VARIANT 44 44 L -> P (in BDE2).
FT /FTId=VAR_063711.
FT VARIANT 60 60 L -> P (in BDE2).
FT /FTId=VAR_063712.
FT VARIANT 169 169 S -> T (in a breast cancer sample;
FT somatic mutation).
FT /FTId=VAR_036433.
FT MUTAGEN 57 57 R->A: Strongly reduced affinity for
FT PTH1R.
FT MUTAGEN 59 59 F->A: Reduced affinity for PTH1R.
FT MUTAGEN 60 60 L->A,K: Strongly reduced affinity for
FT PTH1R.
FT MUTAGEN 63 63 L->A: Reduced affinity for PTH1R.
FT MUTAGEN 64 64 I->A: Reduced affinity for PTH1R.
FT MUTAGEN 68 68 H->A: Reduced affinity for PTH1R.
FT HELIX 41 44
FT HELIX 51 67
FT STRAND 114 116
FT HELIX 117 119
SQ SEQUENCE 177 AA; 20194 MW; 449FDFEE954C51DB CRC64;
MQRRLVQQWS VAVFLLSYAV PSCGRSVEGL SRRLKRAVSE HQLLHDKGKS IQDLRRRFFL
HHLIAEIHTA EIRATSEVSP NSKPSPNTKN HPVRFGSDDE GRYLTQETNK VETYKEQPLK
TPGKKKKGKP GKRKEQEKKK RRTRSAWLDS GVTGSGLEGD HLSDTSTTSL ELDSRRH
//
