LOCUS       NP_062024                376 aa            linear   ROD 17-SEP-2024
DEFINITION  growth/differentiation factor 8 precursor [Rattus norvegicus].
ACCESSION   NP_062024
VERSION     NP_062024.1
DBSOURCE    REFSEQ: accession NM_019151.2
KEYWORDS    RefSeq; RefSeq Select.
SOURCE      Rattus norvegicus (Norway rat)
  ORGANISM  Rattus norvegicus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Rattus.
REFERENCE   1  (residues 1 to 376)
  AUTHORS   Rahmani,N., Motamedi,P., Amani-Shalamzari,S., Escobar,K.A. and
            Suzuki,K.
  TITLE     Swimming in cold water increases the browning process by
            diminishing the Myostatin pathway
  JOURNAL   Mol Biol Rep 51 (1), 884 (2024)
   PUBMED   39093510
  REMARK    GeneRIF: Swimming in cold water increases the browning process by
            diminishing the Myostatin pathway.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 376)
  AUTHORS   Chen,Y., Banie,L., Breyer,B.N., Tan,Y., Wang,Z., Zhou,F., Wang,G.,
            Lin,G., Liu,J., Qi,L.S. and Lue,T.F.
  TITLE     Enhanced Myogenesis by Silencing Myostatin with Nonviral Delivery
            of a dCas9 Ribonucleoprotein Complex
  JOURNAL   CRISPR J 5 (4), 598-608 (2022)
   PUBMED   35758824
  REMARK    GeneRIF: Enhanced Myogenesis by Silencing Myostatin with Nonviral
            Delivery of a dCas9 Ribonucleoprotein Complex.
REFERENCE   3  (residues 1 to 376)
  AUTHORS   Tang,L., Zhao,T., Kang,Y., An,S., Fan,X. and Sun,L.
  TITLE     MSTN is an important myokine for weight-bearing training to
            attenuate bone loss in ovariectomized rats
  JOURNAL   J Physiol Biochem 78 (1), 61-72 (2022)
   PUBMED   34453705
  REMARK    GeneRIF: MSTN is an important myokine for weight-bearing training
            to attenuate bone loss in ovariectomized rats.
REFERENCE   4  (residues 1 to 376)
  AUTHORS   Barisione,C., Verzola,D., Garibaldi,S., Ferrari,P.F., Garibotto,G.,
            Ameri,P., Pane,B., Spinella,G., Pratesi,G. and Palombo,D.
  TITLE     Renal Ischemia/Reperfusion Early Induces Myostatin and PCSK9
            Expression in Rat Kidneys and HK-2 Cells
  JOURNAL   Int J Mol Sci 22 (18), 9884 (2021)
   PUBMED   34576046
  REMARK    GeneRIF: Renal Ischemia/Reperfusion Early Induces Myostatin and
            PCSK9 Expression in Rat Kidneys and HK-2 Cells.
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 376)
  AUTHORS   Szabo,Z., Vainio,L., Lin,R., Swan,J., Hulmi,J.J., Rahtu-Korpela,L.,
            Serpi,R., Laitinen,M., Pasternack,A., Ritvos,O., Kerkela,R. and
            Magga,J.
  TITLE     Systemic blockade of ACVR2B ligands attenuates muscle wasting in
            ischemic heart failure without compromising cardiac function
  JOURNAL   FASEB J 34 (8), 9911-9924 (2020)
   PUBMED   32427381
REFERENCE   6  (residues 1 to 376)
  AUTHORS   Lee,S.J. and McPherron,A.C.
  TITLE     Regulation of myostatin activity and muscle growth
  JOURNAL   Proc Natl Acad Sci U S A 98 (16), 9306-9311 (2001)
   PUBMED   11459935
REFERENCE   7  (residues 1 to 376)
  AUTHORS   Lalani,R., Bhasin,S., Byhower,F., Tarnuzzer,R., Grant,M., Shen,R.,
            Asa,S., Ezzat,S. and Gonzalez-Cadavid,N.F.
  TITLE     Myostatin and insulin-like growth factor-I and -II expression in
            the muscle of rats exposed to the microgravity environment of the
            NeuroLab space shuttle flight
  JOURNAL   J Endocrinol 167 (3), 417-428 (2000)
   PUBMED   11115768
REFERENCE   8  (residues 1 to 376)
  AUTHORS   Mendler,L., Zador,E., Ver Heyen,M., Dux,L. and Wuytack,F.
  TITLE     Myostatin levels in regenerating rat muscles and in myogenic cell
            cultures
  JOURNAL   J Muscle Res Cell Motil 21 (6), 551-563 (2000)
   PUBMED   11206133
REFERENCE   9  (residues 1 to 376)
  AUTHORS   McPherron,A.C. and Lee,S.J.
  TITLE     Double muscling in cattle due to mutations in the myostatin gene
  JOURNAL   Proc Natl Acad Sci U S A 94 (23), 12457-12461 (1997)
   PUBMED   9356471
REFERENCE   10 (residues 1 to 376)
  AUTHORS   McPherron,A.C., Lawler,A.M. and Lee,S.J.
  TITLE     Regulation of skeletal muscle mass in mice by a new TGF-beta
            superfamily member
  JOURNAL   Nature 387 (6628), 83-90 (1997)
   PUBMED   9139826
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            JAXUCZ010000009.1.
            
            Summary: This gene encodes a member of the TGF-beta (transforming
            growth factor-beta) family of proteins. The encoded preproprotein
            is proteolytically processed to generate an N-terminal propeptide
            and a C-terminal subunit. The C-terminal subunits form the mature
            homodimer, which negatively regulates skeletal muscle cell
            proliferation and differentiation. Mutations in this gene are
            associated with increased skeletal muscle mass in humans and other
            mammals. [provided by RefSeq, Jun 2016].
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: FQ224469.1, SRR26643289.25521.1
                                           [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMEA5760386, SAMEA5760393
                                           [ECO:0000348]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            RefSeq Select criteria :: based on single protein-coding transcript
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..376
                     /organism="Rattus norvegicus"
                     /strain="BN"
                     /db_xref="taxon:10116"
                     /chromosome="9"
                     /map="9q22"
     Protein         1..376
                     /product="growth/differentiation factor 8 precursor"
                     /note="growth/differentiation factor 8; GDF-8"
                     /calculated_mol_wt=40061
     sig_peptide     1..24
                     /note="/evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35312.1)"
                     /calculated_mol_wt=2786
     Region          37..254
                     /region_name="TGFb_propeptide"
                     /note="TGF-beta propeptide; cl46657"
                     /db_xref="CDD:480997"
     Site            72
                     /site_type="glycosylation"
                     /note="N-linked (GlcNAc...) asparagine.
                     /evidence=ECO:0000255; propagated from
                     UniProtKB/Swiss-Prot (O35312.1)"
     Site            99..100
                     /site_type="cleavage"
                     /note="Cleavage. /evidence=ECO:0000250|UniProtKB:O08689;
                     propagated from UniProtKB/Swiss-Prot (O35312.1)"
     mat_peptide     268..376
                     /product="Growth/differentiation factor 8.
                     /id=PRO_0000033963"
                     /note="propagated from UniProtKB/Swiss-Prot (O35312.1)"
                     /calculated_mol_wt=12407
     Region          269..376
                     /region_name="TGF_beta_GDF8"
                     /note="transforming growth factor beta (TGF-beta) like
                     domain found in growth/differentiation factor 8 (GDF8) and
                     similar proteins; cd19388"
                     /db_xref="CDD:381658"
     Site            order(269..271,279,281,287,294..298,300,303,305..309,311,
                     316..319,322..324,326..328,330..331,333..335,340,342,346,
                     350..362,365..368,370,376)
                     /site_type="other"
                     /note="polypeptide substrate binding site 2 [polypeptide
                     binding]"
                     /db_xref="CDD:381658"
     Site            order(287,289,291,294,296,298,305,307..311,319..320,
                     322..324,326..328,331..332,334..338,340..343,346,351,353,
                     365..368,370,376)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:381658"
     Site            order(292,297..298,300..303,350,352,354,358..362)
                     /site_type="other"
                     /note="polypeptide substrate binding site 1 [polypeptide
                     binding]"
                     /db_xref="CDD:381658"
     CDS             1..376
                     /gene="Mstn"
                     /gene_synonym="Gdf8"
                     /coded_by="NM_019151.2:125..1255"
                     /db_xref="GeneID:29152"
                     /db_xref="RGD:3115"
ORIGIN      
        1 miqkpqmyvy iylfvliaag pvdlnedser eanvekeglc nacawrqntr ysrieaikiq
       61 ilsklrleta pniskdairq llprapplre lidqydvqrd dssdgsledd dyhattetii
      121 tmptesdflm qadgkpkccf fkfsskiqyn kvvkaqlwiy lravktpttv fvqilrlikp
      181 mkdgtrytgi rslkldmspg tgiwqsidvk tvlqnwlkqp esnlgieika ldenghdlav
      241 tfpgpgedgl npflevkvtd tpkrsrrdfg ldcdehstes rccrypltvd feafgwdwii
      301 apkrykanyc sgecefvflq kyphthlvhq anprgsagpc ctptkmspin mlyfngkeqi
      361 iygkipamvv drcgcs
//
