ID   ANFC_ACITR              Reviewed;         150 AA.
AC   Q76KW6;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=C-type natriuretic peptide;
DE   Flags: Precursor;
GN   Name=cnp;
OS   Acipenser transmontanus (White sturgeon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX   NCBI_TaxID=7904 {ECO:0000312|EMBL:BAD02838.1};
RN   [1] {ECO:0000305, ECO:0000312|EMBL:BAD02838.1}
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX   PubMed=15072558; DOI=10.1677/jme.0.0320547;
RA   Kawakoshi A., Hyodo S., Inoue K., Kobayashi Y., Takei Y.;
RT   "Four natriuretic peptides (ANP, BNP, VNP and CNP) coexist in the sturgeon:
RT   identification of BNP in fish lineage.";
RL   J. Mol. Endocrinol. 32:547-555(2004).
CC   -!- FUNCTION: Hormone which plays a role in endochondral ossification
CC       through regulation of cartilaginous growth plate chondrocytes
CC       proliferation and differentiation. May also be vasoactive and
CC       natriuretic (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Expressed in brain, but not in atrium or ventricle.
CC       {ECO:0000269|PubMed:15072558}.
CC   -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000255}.
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DR   EMBL; AB087731; BAD02838.1; -; mRNA.
DR   AlphaFoldDB; Q76KW6; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
DR   GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR   InterPro; IPR000663; Natr_peptide.
DR   InterPro; IPR030480; Natr_peptide_CS.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   2: Evidence at transcript level;
KW   Cleavage on pair of basic residues; Disulfide bond; Hormone; Secreted;
KW   Signal; Vasoactive.
FT   SIGNAL          1..31
FT                   /evidence="ECO:0000255"
FT   PROPEP          32..127
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000001577"
FT   PEPTIDE         128..150
FT                   /note="C-type natriuretic peptide"
FT                   /evidence="ECO:0000250|UniProtKB:P18145"
FT                   /id="PRO_0000001578"
FT   REGION          60..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..109
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        134..150
FT                   /evidence="ECO:0000250|UniProtKB:P18145"
SQ   SEQUENCE   150 AA;  15990 MW;  D39D9682C35FEC94 CRC64;
     MSISSSSSSS SSSSSCLLLI SLMLLAASCQ GRPDLQHRNH KSQLAGLFGA EVAALLEDAG
     AADGSSGEEA ALSQRAPPSI RALHPRSGRL GLRDDLEAEP PAENKPRRRL LKDFMSSRKM
     FRGRTKKMQQ GRGCFGMKLD RIGSMSGLGC