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