PTHY_HORSE
ID PTHY_HORSE Reviewed; 115 AA.
AC Q27IM2; Q9N1V0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Parathyroid hormone;
DE Short=PTH;
DE AltName: Full=Parathyrin;
DE Flags: Precursor;
GN Name=PTH;
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rourke K.M., Kohn C.W., Rosol T.J., Toribio R.E.;
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 30-115.
RA Shiue Y.-L., Caetano A.R., Lyons L.A., O'Brien S.J., Laughlin T.F.,
RA Murray J.D., Bowling A.T.;
RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the parathyroid hormone family. {ECO:0000305}.
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DR EMBL; DQ399295; ABD59340.1; -; mRNA.
DR EMBL; AF134233; AAF62347.1; -; Genomic_DNA.
DR RefSeq; NP_001075386.1; NM_001081917.1.
DR PDB; 6FJ3; X-ray; 2.50 A; B=32-65.
DR PDBsum; 6FJ3; -.
DR AlphaFoldDB; Q27IM2; -.
DR BMRB; Q27IM2; -.
DR SMR; Q27IM2; -.
DR STRING; 9796.ENSECAP00000017043; -.
DR PaxDb; Q27IM2; -.
DR Ensembl; ENSECAT00000020748; ENSECAP00000017043; ENSECAG00000019608.
DR GeneID; 100034104; -.
DR KEGG; ecb:100034104; -.
DR CTD; 5741; -.
DR VGNC; VGNC:21998; PTH.
DR GeneTree; ENSGT00390000018603; -.
DR HOGENOM; CLU_164143_0_0_1; -.
DR InParanoid; Q27IM2; -.
DR OMA; HNLGEHR; -.
DR OrthoDB; 1482128at2759; -.
DR TreeFam; TF336197; -.
DR Proteomes; UP000002281; Chromosome 7.
DR Bgee; ENSECAG00000019608; Expressed in retina and 3 other tissues.
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:0047485; F:protein N-terminus binding; IEA:Ensembl.
DR GO; GO:0031857; F:type 1 parathyroid hormone receptor binding; IEA:Ensembl.
DR GO; GO:0007202; P:activation of phospholipase C activity; IEA:Ensembl.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Ensembl.
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:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IEA:Ensembl.
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; ISS:UniProtKB.
DR GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; ISS:UniProtKB.
DR GO; GO:0060732; P:positive regulation of inositol phosphate biosynthetic process; IEA:Ensembl.
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; IEA:Ensembl.
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; Hormone;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT PROPEP 26..31
FT /evidence="ECO:0000250"
FT /id="PRO_0000252460"
FT CHAIN 32..115
FT /note="Parathyroid hormone"
FT /id="PRO_0000252461"
FT REGION 51..69
FT /note="Important for receptor binding"
FT /evidence="ECO:0000250"
FT REGION 73..115
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 34..64
FT /evidence="ECO:0007829|PDB:6FJ3"
SQ SEQUENCE 115 AA; 13062 MW; D67FFC0BE238C4CB CRC64;
MMSAKNMVKV MIVMFAIFLL AKSDGKPVRK RSVSEIQLMH NLGKHLNSVE RVEWLRKKLQ
DVHNFIALGA PIFHRDGGSQ RPRKKEDNVL IESHQKSLGE ADKADVDVLS KTKSQ
