ID   PTHR_SHEEP              Reviewed;         121 AA.
AC   Q9GK30;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Parathyroid hormone-related protein;
DE            Short=PTH-rP;
DE            Short=PTHrP;
DE   Flags: Precursor; Fragment;
GN   Name=PTHLH;
OS   Ovis aries (Sheep).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Caprinae; Ovis.
OX   NCBI_TaxID=9940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Ovary;
RA   Hastie P.M., Beck N.F.G.;
RT   "Expression of mRNA encoding parathyroid hormone-related peptide (PTH-rP)
RT   in ovine ovarian follicles.";
RL   Submitted (DEC-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   -!- 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; AF327654; AAG48348.1; -; mRNA.
DR   AlphaFoldDB; Q9GK30; -.
DR   SMR; Q9GK30; -.
DR   MINT; Q9GK30; -.
DR   STRING; 9940.ENSOARP00000021119; -.
DR   eggNOG; ENOG502S3J9; Eukaryota.
DR   Proteomes; UP000002356; 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; IEA:UniProtKB-KW.
DR   GO; GO:0051428; F:peptide hormone receptor binding; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Calcium; Cleavage on pair of basic residues; Cytoplasm; Hormone; Nucleus;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          <1..14
FT                   /evidence="ECO:0000255"
FT   PROPEP          15..24
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000023238"
FT   CHAIN           27..>121
FT                   /note="Parathyroid hormone-related protein"
FT                   /id="PRO_0000023239"
FT   REGION          47..58
FT                   /note="Important for receptor binding"
FT                   /evidence="ECO:0000250"
FT   REGION          61..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           98..119
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        64..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT   NON_TER         121
SQ   SEQUENCE   121 AA;  13658 MW;  FA9437F5A5E041E1 CRC64;
     VGVFLLSYSV PSCGRSVEEL GRRLKRAVSE HQLLHDKGKS IQDLRRRFFL HHLIAEIHTA
     EIRATSEVSP NSKPAPNTKN HPVRFGSDDE GKYLTQETNK VETYKEQPLK TPGKKKKGKP
     G