ID   ANFC_SHEEP              Reviewed;         126 AA.
AC   P56283;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=C-type natriuretic peptide;
DE   Contains:
DE     RecName: Full=CNP-22;
DE   Contains:
DE     RecName: Full=CNP-29;
DE   Contains:
DE     RecName: Full=CNP-53;
DE   Flags: Precursor;
GN   Name=NPPC; Synonyms=CNP;
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 [GENOMIC DNA].
RX   PubMed=10219521; DOI=10.1016/s0739-7240(99)00005-3;
RA   Aitken G.D., Raizis A.M., Yandle T.G., George P.M., Espiner E.A.,
RA   Cameron V.A.;
RT   "The characterization of ovine genes for atrial, brain, and C-type
RT   natriuretic peptides.";
RL   Domest. Anim. Endocrinol. 16:115-121(1999).
CC   -!- FUNCTION: [CNP-22]: Hormone which plays a role in endochondral
CC       ossification through regulation of cartilaginous growth plate
CC       chondrocytes proliferation and differentiation (By similarity). May
CC       also be vasoactive and natriuretic. Acts by specifically binding and
CC       stimulating NPR2 to produce cGMP. Binds the clearance receptor NPR3 (By
CC       similarity). {ECO:0000250|UniProtKB:P23582,
CC       ECO:0000250|UniProtKB:Q61839}.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: [CNP-22]: Degraded by IDE (in vitro).
CC       {ECO:0000250|UniProtKB:P23582}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR   EMBL; AF037467; AAB92261.1; -; Genomic_DNA.
DR   RefSeq; NP_001009479.1; NM_001009479.1.
DR   AlphaFoldDB; P56283; -.
DR   STRING; 9940.ENSOARP00000001044; -.
DR   Ensembl; ENSOART00020018098; ENSOARP00020014955; ENSOARG00020011896.
DR   GeneID; 493773; -.
DR   KEGG; oas:493773; -.
DR   CTD; 4880; -.
DR   eggNOG; ENOG502S2QY; Eukaryota.
DR   OrthoDB; 1491136at2759; -.
DR   Proteomes; UP000002356; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0032991; C:protein-containing complex; IEA:Ensembl.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0051427; F:hormone receptor binding; IEA:Ensembl.
DR   GO; GO:0005102; F:signaling receptor binding; ISS:AgBase.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0003418; P:growth plate cartilage chondrocyte differentiation; ISS:UniProtKB.
DR   GO; GO:0003419; P:growth plate cartilage chondrocyte proliferation; ISS:UniProtKB.
DR   GO; GO:0051321; P:meiotic cell cycle; IEA:Ensembl.
DR   GO; GO:0051447; P:negative regulation of meiotic cell cycle; IEA:Ensembl.
DR   GO; GO:1900194; P:negative regulation of oocyte maturation; IEA:Ensembl.
DR   GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
DR   GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
DR   GO; GO:0006457; P:protein folding; IEA:Ensembl.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; IEA:Ensembl.
DR   InterPro; IPR002406; C_natriurtcpep.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00713; CNATPEPTIDE.
DR   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   3: Inferred from homology;
KW   Cleavage on pair of basic residues; Disulfide bond; Hormone; Osteogenesis;
KW   Reference proteome; Secreted; Signal; Vasoactive.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   PROPEP          24..73
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000001569"
FT   PEPTIDE         74..126
FT                   /note="CNP-53"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001570"
FT   PEPTIDE         98..126
FT                   /note="CNP-29"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001571"
FT   PEPTIDE         105..126
FT                   /note="CNP-22"
FT                   /id="PRO_0000001572"
FT   REGION          20..71
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        110..126
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   126 AA;  13317 MW;  83C21B3C49A8F18B CRC64;
     MHLSQLLACA LLLSLLSLRP SEAKPGAPPK VPRTPPGEEV AEPQAAGGGQ KKGDKTPGGG
     GANLKDDRSR LLRDLRVDTK SRAAWTRLLH EHPNARKYKG GNKKGLSKGC FGLKLDRIGS
     MSGLGC