OSTN_RAT
ID OSTN_RAT Reviewed; 132 AA.
AC P61365;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Osteocrin {ECO:0000303|PubMed:14523025};
DE AltName: Full=Musclin {ECO:0000303|PubMed:15044443};
DE Contains:
DE RecName: Full=Processed Osteocrin {ECO:0000250|UniProtKB:P61364};
DE Flags: Precursor;
GN Name=Ostn {ECO:0000312|RGD:1303110};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP INDUCTION.
RC STRAIN=Wistar; TISSUE=Bone marrow;
RX PubMed=14523025; DOI=10.1074/jbc.m307310200;
RA Thomas G., Moffatt P., Salois P., Gaumond M.-H., Gingras R., Godin E.,
RA Miao D., Goltzman D., Lanctot C.;
RT "Osteocrin, a novel bone-specific secreted protein that modulates the
RT osteoblast phenotype.";
RL J. Biol. Chem. 278:50563-50571(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=15044443; DOI=10.1074/jbc.c400066200;
RA Nishizawa H., Matsuda M., Yamada Y., Kawai K., Suzuki E., Makishima M.,
RA Kitamura T., Shimomura I.;
RT "Musclin, a novel skeletal muscle-derived secretory factor.";
RL J. Biol. Chem. 279:19391-19395(2004).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=17951249; DOI=10.1074/jbc.m708596200;
RA Moffatt P., Thomas G., Sellin K., Bessette M.C., Lafreniere F.,
RA Akhouayri O., St-Arnaud R., Lanctot C.;
RT "Osteocrin is a specific ligand of the natriuretic Peptide clearance
RT receptor that modulates bone growth.";
RL J. Biol. Chem. 282:36454-36462(2007).
CC -!- FUNCTION: Hormone that acts as a ligand for natriuretic peptide
CC receptor NPR3/NPR-C and promotes bone growth and physical endurance in
CC muscle. Acts as a regulator of osteoblast differentiation and bone
CC growth by binding to natriuretic peptide receptor NPR3/NPR-C, thereby
CC preventing binding between NPR3/NPR-C and natriuretic peptides, leading
CC to increase cGMP production. Required to enhance physical endurance:
CC induced following physical exercise in muscle and promotes cGMP
CC production, probably by interacting with NPR3/NPR-C. May act as an
CC autocrine and paracrine factor linked to glucose metabolism in skeletal
CC muscle. {ECO:0000250|UniProtKB:P61364}.
CC -!- SUBUNIT: Interacts with NPR3. {ECO:0000250|UniProtKB:P61364}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14523025}.
CC -!- TISSUE SPECIFICITY: Highly expressed in skeletal muscle
CC (PubMed:15044443). Also expressed in leg tendons/ligaments and
CC osteoblasts (PubMed:17951249). In long bones and teeth, present in knee
CC joint and periodontal ligaments (at protein level) (PubMed:17951249).
CC {ECO:0000269|PubMed:15044443, ECO:0000269|PubMed:17951249}.
CC -!- DEVELOPMENTAL STAGE: Expression was highest in embryos and neonates,
CC peaking at 4 days of age in both calvaria and long bones and decreasing
CC steadily with age to very low levels in 8-month-old long bones. The
CC age-related decrease was less marked in calvaria by 8 months.
CC {ECO:0000269|PubMed:14523025}.
CC -!- INDUCTION: Is down-regulated by 1,25-dihydroxy vitamin D3.
CC {ECO:0000269|PubMed:14523025}.
CC -!- SIMILARITY: Belongs to the Osteocrin family. {ECO:0000305}.
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DR EMBL; AY398682; AAQ94967.1; -; mRNA.
DR EMBL; AY573934; AAS87600.1; -; mRNA.
DR RefSeq; NP_997495.1; NM_207612.2.
DR RefSeq; XP_008767023.1; XM_008768801.2.
DR AlphaFoldDB; P61365; -.
DR STRING; 10116.ENSRNOP00000043654; -.
DR PaxDb; P61365; -.
DR Ensembl; ENSRNOT00000049841; ENSRNOP00000043654; ENSRNOG00000030462.
DR GeneID; 360730; -.
DR KEGG; rno:360730; -.
DR UCSC; RGD:1303110; rat.
DR CTD; 344901; -.
DR RGD; 1303110; Ostn.
DR eggNOG; ENOG502S2R3; Eukaryota.
DR GeneTree; ENSGT00390000001750; -.
DR HOGENOM; CLU_155967_0_0_1; -.
DR InParanoid; P61365; -.
DR OMA; AIFLMQW; -.
DR OrthoDB; 1512795at2759; -.
DR PhylomeDB; P61365; -.
DR TreeFam; TF333399; -.
DR PRO; PR:P61365; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000030462; Expressed in quadriceps femoris and 5 other tissues.
DR GO; GO:0005615; C:extracellular space; ISO:RGD.
DR GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; ISO:RGD.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:RGD.
DR GO; GO:0003416; P:endochondral bone growth; ISO:RGD.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; ISO:RGD.
DR GO; GO:1903860; P:negative regulation of dendrite extension; ISO:RGD.
DR GO; GO:0046325; P:negative regulation of glucose import; ISO:RGD.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR InterPro; IPR021088; Osteocrin.
DR PANTHER; PTHR35353; PTHR35353; 1.
DR Pfam; PF11037; Musclin; 1.
PE 1: Evidence at protein level;
KW Amidation; Cleavage on pair of basic residues; Developmental protein;
KW Differentiation; Hormone; Osteogenesis; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..132
FT /note="Osteocrin"
FT /evidence="ECO:0000250|UniProtKB:P61364"
FT /id="PRO_0000439031"
FT PEPTIDE 82..131
FT /note="Processed Osteocrin"
FT /evidence="ECO:0000250|UniProtKB:P61364"
FT /id="PRO_0000021970"
FT MOD_RES 131
FT /note="Arginine amide"
FT /evidence="ECO:0000255"
SQ SEQUENCE 132 AA; 14636 MW; 35D0D2DCB1732A7A CRC64;
MLDWRLASAH FLLAMILMLW GSGKAFSVDL ASEASEFGAE SLQSPPTTRE EKSATELAAK
LLLLDDLVSL ENDVFETKKK RSFSGFGSPL DRLSAGSVEH RGKQRRVVDH SKKRFGIPMD
RIGRNRLSSS RG