ID A0A3Q2FU32_CYPVA Unreviewed; 120 AA.
AC A0A3Q2FU32;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Natriuretic peptide C {ECO:0000313|Ensembl:ENSCVAP00000010475.1};
OS Cyprinodon variegatus (Sheepshead minnow).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Cyprinodontidae;
OC Cyprinodon.
OX NCBI_TaxID=28743 {ECO:0000313|Ensembl:ENSCVAP00000010475.1, ECO:0000313|Proteomes:UP000265020};
RN [1] {ECO:0000313|Ensembl:ENSCVAP00000010475.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Exhibits natriuretic and vasodepressant activity. Has cGMP-
CC stimulating activity. May help to regulate body fluid homeostasis in a
CC variety of aquatic environments. {ECO:0000256|ARBA:ARBA00002179}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613,
CC ECO:0000256|RuleBase:RU003686}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family.
CC {ECO:0000256|ARBA:ARBA00009041, ECO:0000256|RuleBase:RU003686}.
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DR RefSeq; XP_015228546.1; XM_015373060.1.
DR AlphaFoldDB; A0A3Q2FU32; -.
DR STRING; 28743.ENSCVAP00000010475; -.
DR Ensembl; ENSCVAT00000017182.1; ENSCVAP00000010475.1; ENSCVAG00000012612.1.
DR GeneID; 107083669; -.
DR KEGG; cvg:107083669; -.
DR CTD; 4880; -.
DR GeneTree; ENSGT00390000015492; -.
DR OMA; SHFLACG; -.
DR OrthoDB; 4269066at2759; -.
DR Proteomes; UP000265020; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IEA:InterPro.
DR GO; GO:0097746; P:blood vessel diameter maintenance; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002408; Natriuretic_peptide_brain.
DR PANTHER; PTHR12167; C-TYPE NATRIURETIC PEPTIDE; 1.
DR PANTHER; PTHR12167:SF2; C-TYPE NATRIURETIC PEPTIDE; 1.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00712; BNATPEPTIDE.
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 {ECO:0000256|ARBA:ARBA00022685};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000265020};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Vasoactive {ECO:0000256|ARBA:ARBA00022858, ECO:0000256|RuleBase:RU003686}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..120
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018539760"
FT REGION 78..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 120 AA; 13450 MW; B81927AFFA0157A0 CRC64;
MNLSYLVACG LLVSLLSEKM TAKPLTQTHQ SFQSLLGEEL AEILESDERE RRIDAVRSRM
RLLRDLRMDT KARGMWARLL NDQPAPRRHK SGSKKAGSTS RSGCFGHKMD RIGTISGMGC
//
