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PTHR_HORSE
ID   PTHR_HORSE              Reviewed;         137 AA.
AC   Q9GMB7;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Parathyroid hormone-related protein;
DE            Short=PTH-rP;
DE            Short=PTHrP;
DE   Contains:
DE     RecName: Full=Osteostatin;
DE   Flags: Fragment;
GN   Name=PTHLH;
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   Nixon A.J., Bent S.J., Brower-Toland B.D.;
RT   "Partial nucleotide sequence from the 5' end of equine parathyroid hormone-
RT   related peptide mRNA.";
RL   Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Neuroendocrine peptide which is a critical regulator of
CC       cellular and organ growth, development, migration, differentiation and
CC       survival and of epithelial calcium ion transport. Regulates
CC       endochondral bone development and epithelial-mesenchymal interactions
CC       during the formation of the mammary glands and teeth. Required for
CC       skeletal homeostasis. Promotes mammary mesenchyme differentiation and
CC       bud outgrowth by modulating mesenchymal cell responsiveness to BMPs.
CC       Up-regulates BMPR1A expression in the mammary mesenchyme and this
CC       increases the sensitivity of these cells to BMPs and allows them to
CC       respond to BMP4 in a paracrine and/or autocrine fashion. BMP4 signaling
CC       in the mesenchyme, in turn, triggers epithelial outgrowth and augments
CC       MSX2 expression, which causes the mammary mesenchyme to inhibit hair
CC       follicle formation within the nipple sheath (By similarity).
CC       {ECO:0000250}.
CC   -!- FUNCTION: Osteostatin is a potent inhibitor of osteoclastic bone
CC       resorption. {ECO:0000250}.
CC   -!- SUBUNIT: PTHrP interacts with PTH1R (via N-terminal extracellular
CC       domain). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC       Secreted {ECO:0000250}.
CC   -!- PTM: There are several secretory forms, including osteostatin, arising
CC       from endoproteolytic cleavage of the initial translation product. Each
CC       of these secretory forms is believed to have one or more of its own
CC       receptors that mediates the normal paracrine, autocrine and endocrine
CC       actions (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the parathyroid hormone family. {ECO:0000305}.
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DR   EMBL; AY005821; AAF99386.1; -; mRNA.
DR   AlphaFoldDB; Q9GMB7; -.
DR   SMR; Q9GMB7; -.
DR   STRING; 9796.ENSECAP00000012364; -.
DR   PaxDb; Q9GMB7; -.
DR   HOGENOM; CLU_095189_0_0_1; -.
DR   InParanoid; Q9GMB7; -.
DR   Proteomes; UP000002281; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR   GO; GO:0051428; F:peptide hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0030282; P:bone mineralization; IEA:InterPro.
DR   GO; GO:0002076; P:osteoblast development; IBA:GO_Central.
DR   GO; GO:0032330; P:regulation of chondrocyte differentiation; IBA:GO_Central.
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.
PE   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Cytoplasm; Hormone; Nucleus;
KW   Reference proteome; Secreted.
FT   CHAIN           <1..137
FT                   /note="Parathyroid hormone-related protein"
FT                   /id="PRO_0000045385"
FT   PEPTIDE         103..135
FT                   /note="Osteostatin"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023223"
FT   REGION          17..28
FT                   /note="Important for receptor binding"
FT                   /evidence="ECO:0000250"
FT   REGION          31..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           68..89
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        84..100
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
SQ   SEQUENCE   137 AA;  15845 MW;  388DA1162EABAD34 CRC64;
     HQLLHDKGKS IQDLRRRFFL HHLIAEIHTA EIRATSEVSP NSKPAPNTKN HPVRFGSDDE
     GRYLTQETNK LEPYKEQPLK TPGKKKKGKP GKRKEQEKKK RRTRSAWLNS EVAESGLDGD
     HLSDFSTTSP ELYLRRH
 
 
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