PTHY_BOVIN
ID PTHY_BOVIN Reviewed; 115 AA.
AC P01268;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Parathyroid hormone;
DE Short=PTH;
DE AltName: Full=Parathyrin;
DE Flags: Precursor;
GN Name=PTH;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=388425; DOI=10.1073/pnas.76.10.4981;
RA Kronenberg H.M., McDevitt B.E., Majzoub J.A., Nathans J., Sharp P.A.,
RA Potts J.T. Jr., Rich A.;
RT "Cloning and nucleotide sequence of DNA coding for bovine preproparathyroid
RT hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 76:4981-4985(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=6170060; DOI=10.1073/pnas.78.7.4073;
RA Weaver C.A., Gordon D.F., Kemper B.;
RT "Introduction by molecular cloning of artifactual inverted sequences at the
RT 5' terminus of the sense strand of bovine parathyroid hormone cDNA.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:4073-4077(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=6185374; DOI=10.1016/0303-7207(82)90136-8;
RA Weaver C.A., Gordon D.F., Kemper B.;
RT "Nucleotide sequence of bovine parathyroid hormone messenger RNA.";
RL Mol. Cell. Endocrinol. 28:411-424(1982).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086460; DOI=10.1016/0378-1119(84)90149-5;
RA Weaver C.A., Gordon D.F., Kissil M.S., Mead D.A., Kemper B.;
RT "Isolation and complete nucleotide sequence of the gene for bovine
RT parathyroid hormone.";
RL Gene 28:319-329(1984).
RN [5]
RP PROTEIN SEQUENCE OF 26-115.
RX PubMed=4522780; DOI=10.1073/pnas.71.3.653;
RA Hamilton J.W., Niall H.D., Jacobs J.W., Keutmann H.T., Potts J.T. Jr.,
RA Cohn D.V.;
RT "The N-terminal amino-acid sequence of bovine proparathyroid hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 71:653-656(1974).
RN [6]
RP PROTEIN SEQUENCE OF 32-115.
RX PubMed=5531031;
RA Niall H.D., Keutmann H.T., Sauer R., Hogan M.L., Dawson B.F., Aurbach G.D.,
RA Potts J.T. Jr.;
RT "The amino acid sequence of bovine parathyroid hormone I.";
RL Hoppe-Seyler's Z. Physiol. Chem. 351:1586-1588(1970).
RN [7]
RP PROTEIN SEQUENCE OF 32-115.
RX PubMed=5275384; DOI=10.1073/pnas.67.4.1862;
RA Brewer H.B. Jr., Ronan R.;
RT "Bovine parathyroid hormone: amino acid sequence.";
RL Proc. Natl. Acad. Sci. U.S.A. 67:1862-1869(1970).
RN [8]
RP SYNTHESIS OF 32-65.
RX PubMed=4322265; DOI=10.1073/pnas.68.1.63;
RA Potts J.T. Jr., Tregear G.W., Keutmann H.T., Niall H.D., Sauer R.,
RA Deftos L.J., Dawson B.F., Hogan M.L., Aurbach G.D.;
RT "Synthesis of a biologically active N-terminal tetratriacontapeptide of
RT parathyroid hormone.";
RL Proc. Natl. Acad. Sci. U.S.A. 68:63-67(1971).
RN [9]
RP STRUCTURE BY NMR OF 32-68.
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).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PTH1R (via N-terminal extracellular domain).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the parathyroid hormone family. {ECO:0000305}.
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DR EMBL; V00106; CAA23439.1; -; mRNA.
DR EMBL; J00024; AAA30747.1; -; mRNA.
DR EMBL; K01938; AAA30749.1; -; Genomic_DNA.
DR EMBL; M25082; AAA30748.1; -; mRNA.
DR PIR; A24949; PTBO.
DR RefSeq; NP_776379.2; NM_173954.2.
DR PDB; 1ZWC; NMR; -; A=32-68.
DR PDBsum; 1ZWC; -.
DR AlphaFoldDB; P01268; -.
DR SMR; P01268; -.
DR STRING; 9913.ENSBTAP00000025399; -.
DR MetOSite; P01268; -.
DR PaxDb; P01268; -.
DR Ensembl; ENSBTAT00000025399; ENSBTAP00000025399; ENSBTAG00000019080.
DR GeneID; 280903; -.
DR KEGG; bta:280903; -.
DR CTD; 5741; -.
DR VEuPathDB; HostDB:ENSBTAG00000019080; -.
DR VGNC; VGNC:33513; PTH.
DR eggNOG; ENOG502SB2W; Eukaryota.
DR GeneTree; ENSGT00390000018603; -.
DR HOGENOM; CLU_164143_0_0_1; -.
DR InParanoid; P01268; -.
DR OrthoDB; 1482128at2759; -.
DR TreeFam; TF336197; -.
DR EvolutionaryTrace; P01268; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000019080; Expressed in Ammon's horn and 5 other tissues.
DR ExpressionAtlas; P01268; baseline.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0031856; F:parathyroid hormone receptor binding; IBA:GO_Central.
DR GO; GO:0051428; F:peptide hormone receptor binding; ISS:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IBA:GO_Central.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; IEA:InterPro.
DR GO; GO:0046326; P:positive regulation of glucose import; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
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; Hormone; Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:4522780"
FT PROPEP 26..31
FT /evidence="ECO:0000269|PubMed:5275384,
FT ECO:0000269|PubMed:5531031"
FT /id="PRO_0000023243"
FT CHAIN 32..115
FT /note="Parathyroid hormone"
FT /id="PRO_0000023244"
FT REGION 51..69
FT /note="Important for receptor binding"
FT /evidence="ECO:0000250"
FT REGION 77..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 106
FT /note="V -> G (in Ref. 4; AAA30749)"
FT /evidence="ECO:0000305"
FT HELIX 37..40
FT /evidence="ECO:0007829|PDB:1ZWC"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:1ZWC"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:1ZWC"
FT HELIX 53..60
FT /evidence="ECO:0007829|PDB:1ZWC"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:1ZWC"
SQ SEQUENCE 115 AA; 12980 MW; 2ED246B348880710 CRC64;
MMSAKDMVKV MIVMLAICFL ARSDGKSVKK RAVSEIQFMH NLGKHLSSME RVEWLRKKLQ
DVHNFVALGA SIAYRDGSSQ RPRKKEDNVL VESHQKSLGE ADKADVDVLI KAKPQ
