PTHR_CHICK
ID PTHR_CHICK Reviewed; 176 AA.
AC P17251;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Parathyroid hormone-related protein;
DE Short=PTH-rP;
DE Short=PTHrP;
DE Contains:
DE RecName: Full=Osteostatin;
DE AltName: Full=PTHrP[107-139];
DE Flags: Precursor;
GN Name=PTHLH;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2349111; DOI=10.1093/nar/18.10.3062;
RA Thiede M.A., Rutledge S.J.;
RT "Nucleotide sequence of a parathyroid hormone-related peptide expressed by
RT the 10 day chicken embryo.";
RL Nucleic Acids Res. 18:3062-3062(1990).
RN [2]
RP STRUCTURE BY NMR OF 145-176.
RX PubMed=10366729; DOI=10.1016/s0167-4838(99)00078-3;
RA Cuthbertson R.M., Kemp B.E., Barden J.A.;
RT "Structure study of osteostatin PTHrP[Thr107](107-139).";
RL Biochim. Biophys. Acta 1432:64-72(1999).
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. {ECO:0000250}.
CC -!- FUNCTION: Osteostatin is a potent inhibitor of osteoclastic bone
CC resorption. {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; X52131; CAA36376.1; -; mRNA.
DR PIR; S10202; S10202.
DR AlphaFoldDB; P17251; -.
DR SMR; P17251; -.
DR STRING; 9031.ENSGALP00000029396; -.
DR PaxDb; P17251; -.
DR Ensembl; ENSGALT00000079807; ENSGALP00000055214; ENSGALG00000017295.
DR VEuPathDB; HostDB:geneid_396281; -.
DR eggNOG; ENOG502S3J9; Eukaryota.
DR GeneTree; ENSGT00390000004933; -.
DR HOGENOM; CLU_095189_0_0_1; -.
DR InParanoid; P17251; -.
DR OMA; MFAKLFQ; -.
DR OrthoDB; 1359745at2759; -.
DR PRO; PR:P17251; -.
DR Proteomes; UP000000539; Chromosome 1.
DR Bgee; ENSGALG00000017295; Expressed in lung and 7 other tissues.
DR ExpressionAtlas; P17251; baseline and differential.
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; IBA:GO_Central.
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:1903042; P:negative regulation of chondrocyte hypertrophy; IMP:AgBase.
DR GO; GO:0002076; P:osteoblast development; IBA:GO_Central.
DR GO; GO:0032330; P:regulation of chondrocyte differentiation; IBA:GO_Central.
DR GO; GO:1902733; P:regulation of growth plate cartilage chondrocyte differentiation; IMP:AgBase.
DR GO; GO:0003420; P:regulation of growth plate cartilage chondrocyte proliferation; IMP:AgBase.
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 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Cytoplasm; Hormone; Nucleus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT PROPEP 26..37
FT /evidence="ECO:0000250"
FT /id="PRO_0000023240"
FT CHAIN 38..176
FT /note="Parathyroid hormone-related protein"
FT /id="PRO_0000023241"
FT PEPTIDE 145..176
FT /note="Osteostatin"
FT /id="PRO_0000023242"
FT REGION 76..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 109..130
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT COMPBIAS 76..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..141
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 176 AA; 20226 MW; 60C8AB30ACF5293B CRC64;
MMFTKLFQQW SFAVFLLSYS VPSYGRSVEG ISRRLKRAVS EHQLLHDKGK SIQDLRRRIF
LQNLIEGVNT AEIRATSEVS PNPKPATNTK NYPVRFGSED EGRYLTQETN KSQTYKEQPL
KVSGKKKKAK PGKRKEQEKK KRRARSAWLN SGMYGSNVTE SPVLDNSVTT HNHILR
