ANF_ACITR
ID ANF_ACITR Reviewed; 142 AA.
AC P83964;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=Natriuretic peptides A;
DE AltName: Full=Prepronatriodilatin;
DE Contains:
DE RecName: Full=Atrial natriuretic factor;
DE Short=ANF;
DE AltName: Full=Atrial natriuretic peptide;
DE Short=ANP;
DE Flags: Precursor;
GN Name=nppa; Synonyms=anp;
OS Acipenser transmontanus (White sturgeon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Chondrostei; Acipenseriformes; Acipenseridae; Acipenser.
OX NCBI_TaxID=7904;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart atrium;
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 playing a key role in cardiovascular homeostasis
CC through regulation of natriuresis, diuresis, and vasodilation. Has a
CC cGMP-stimulating activity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed in heart atrium and to a lower extent in
CC heart ventricle, but not in brain. {ECO:0000269|PubMed:15072558}.
CC -!- PTM: Cleaved upon secretion to produce the functional hormone.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
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DR EMBL; AB087728; BAD02835.1; -; mRNA.
DR AlphaFoldDB; P83964; -.
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 InterPro; IPR002408; Natriuretic_peptide_brain.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00712; BNATPEPTIDE.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 2: Evidence at transcript level;
KW Disulfide bond; Hormone; Secreted; Signal; Vasoactive.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT PROPEP 24..112
FT /evidence="ECO:0000305"
FT /id="PRO_0000001517"
FT PEPTIDE 113..142
FT /note="Atrial natriuretic factor"
FT /evidence="ECO:0000250|UniProtKB:P18144"
FT /id="PRO_0000001518"
FT REGION 47..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..89
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 120..136
FT /evidence="ECO:0000250|UniProtKB:P18144"
SQ SEQUENCE 142 AA; 15888 MW; 382B87FB44178CD9 CRC64;
MMLKTVIYTG VLFLICNKVL VRADPLYSPY SSKDLANLKT LLERFEDTLG QDEGNDNQQD
YDIANPEAEG PQAGSPWDRE RERQWPASDY KKPQEGYQSQ SSRLRDLLMA PRNNRGSSGC
FGSRIDRIGS MSSMGCGGSR KG