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Database: UniProt
Entry: P12272
LinkDB: P12272
Original site: P12272 
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   03-SEP-2014, entry version 165.
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; DOI=10.1210/endo-129-4-1762;
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; DOI=10.1210/endo-129-6-3424;
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   CCDS; CCDS44853.1; -. [P12272-1]
DR   CCDS; CCDS8715.1; -. [P12272-2]
DR   PIR; A33360; PTHU2L.
DR   PIR; C33360; PTHU3L.
DR   RefSeq; NP_002811.1; NM_002820.2. [P12272-2]
DR   RefSeq; NP_945315.1; NM_198964.1. [P12272-2]
DR   RefSeq; NP_945316.1; NM_198965.1. [P12272-1]
DR   RefSeq; NP_945317.1; NM_198966.1. [P12272-1]
DR   RefSeq; XP_005253491.1; XM_005253434.1.
DR   RefSeq; XP_006719178.1; XM_006719115.1. [P12272-1]
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   SMR; P12272; 37-70.
DR   BioGrid; 111716; 5.
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. [P12272-2]
DR   Ensembl; ENST00000354417; ENSP00000346398; ENSG00000087494. [P12272-3]
DR   Ensembl; ENST00000395868; ENSP00000379209; ENSG00000087494. [P12272-2]
DR   Ensembl; ENST00000395872; ENSP00000379213; ENSG00000087494. [P12272-1]
DR   Ensembl; ENST00000535992; ENSP00000440613; ENSG00000087494. [P12272-2]
DR   Ensembl; ENST00000538310; ENSP00000441890; ENSG00000087494. [P12272-3]
DR   Ensembl; ENST00000539239; ENSP00000441571; ENSG00000087494. [P12272-1]
DR   Ensembl; ENST00000545234; ENSP00000441765; ENSG00000087494. [P12272-1]
DR   GeneID; 5744; -.
DR   KEGG; hsa:5744; -.
DR   UCSC; uc001rik.3; human. [P12272-1]
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; EOG7FBRK8; -.
DR   PhylomeDB; P12272; -.
DR   TreeFam; TF332953; -.
DR   Reactome; REACT_18372; Class B/2 (Secretin family receptors).
DR   Reactome; REACT_19327; G alpha (s) signalling events.
DR   EvolutionaryTrace; P12272; -.
DR   GeneWiki; Parathyroid_hormone-related_protein; -.
DR   GenomeRNAi; 5744; -.
DR   NextBio; 22362; -.
DR   PMAP-CutDB; P12272; -.
DR   PRO; PR:P12272; -.
DR   ArrayExpress; P12272; -.
DR   Bgee; P12272; -.
DR   CleanEx; HS_PTHLH; -.
DR   Genevestigator; P12272; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:HPA.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:Ensembl.
DR   GO; GO:0007492; P:endoderm development; IEA:Ensembl.
DR   GO; GO:0008544; P:epidermis development; TAS:ProtInc.
DR   GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR   GO; GO:0007565; P:female pregnancy; TAS:ProtInc.
DR   GO; GO:0048286; P:lung alveolus development; IEA:Ensembl.
DR   GO; GO:0060649; P:mammary gland bud elongation; IEA:Ensembl.
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:Ensembl.
DR   GO; GO:0060659; P:nipple sheath formation; IEA:Ensembl.
DR   GO; GO:0002076; P:osteoblast development; IEA:Ensembl.
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:Ensembl.
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:Ensembl.
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
//
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