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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
 
 
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