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Database: UniProt
Entry: L5KG38_PTEAL
LinkDB: L5KG38_PTEAL
Original site: L5KG38_PTEAL 
ID   L5KG38_PTEAL            Unreviewed;       249 AA.
AC   L5KG38;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Natriuretic peptides A {ECO:0000256|ARBA:ARBA00020078};
DE   AltName: Full=Atrial natriuretic factor prohormone {ECO:0000256|ARBA:ARBA00031619};
DE   AltName: Full=Atrial natriuretic peptide prohormone {ECO:0000256|ARBA:ARBA00032736};
DE   AltName: Full=Atriopeptigen {ECO:0000256|ARBA:ARBA00031144};
DE   AltName: Full=Cardiodilatin {ECO:0000256|ARBA:ARBA00030903};
DE   AltName: Full=preproCDD-ANF {ECO:0000256|ARBA:ARBA00033220};
GN   ORFNames=PAL_GLEAN10012987 {ECO:0000313|EMBL:ELK10515.1};
OS   Pteropus alecto (Black flying fox).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC   Pteropodinae; Pteropus.
OX   NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK10515.1, ECO:0000313|Proteomes:UP000010552};
RN   [1] {ECO:0000313|Proteomes:UP000010552}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23258410; DOI=10.1126/science.1230835;
RA   Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA   Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA   Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA   Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA   Wang J.;
RT   "Comparative analysis of bat genomes provides insight into the evolution of
RT   flight and immunity.";
RL   Science 339:456-460(2013).
CC   -!- FUNCTION: Hormone produced in the kidneys that appears to be important
CC       for maintaining cardio-renal homeostasis. Mediates vasodilation,
CC       natriuresis and diuresis primarily in the renal system, in order to
CC       maintain the extracellular fluid volume and control the fluid-
CC       electrolyte balance. Specifically binds and stimulates cGMP production
CC       by renal transmembrane receptors, likely NPR1. Urodilatin not ANP, may
CC       be the natriuretic peptide responsible for the regulation of sodium and
CC       water homeostasis in the kidney. {ECO:0000256|ARBA:ARBA00002857}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of diuresis and inhibiting aldosterone synthesis. In vitro,
CC       promotes the production of cGMP and induces vasodilation. May promote
CC       natriuresis, at least in part, by enhancing prostaglandin E2 synthesis
CC       resulting in the inhibition of renal Na+-K+-ATPase. May have a role in
CC       potassium excretion but not sodium excretion (natriuresis). Possibly
CC       enhances protein excretion in urine by decreasing proximal tubular
CC       protein reabsorption. {ECO:0000256|ARBA:ARBA00003298}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis and vasodilation. In vivo promotes
CC       natriuresis and in vitro, vasodilates renal artery strips.
CC       {ECO:0000256|ARBA:ARBA00002352}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis and vasodilation. In vivo promotes
CC       natriuresis. In vitro, selectively vasodilates intestinal and vascular
CC       smooth muscle strips. {ECO:0000256|ARBA:ARBA00003360}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis and vasodilation. In vivo promotes
CC       natriuresis. In vitro, selectively vasodilates intestinal smooth muscle
CC       but not vascular smooth muscle strips. {ECO:0000256|ARBA:ARBA00002948}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis, diuresis, and vasodilation. In vitro,
CC       promotes the production of cGMP and induces vasodilation. May promote
CC       natriuresis, at least in part, by enhancing prostaglandin E2 synthesis
CC       resulting in the inhibition of renal Na+-K+-ATPase. However reports on
CC       the involvement of this peptide in mammal blood volume and blood
CC       pressure homeostasis are conflicting; according to a report it is not
CC       sufficient to activate cGMP and does not inhibit collecting duct
CC       transport nor effect diuresis and natriuresis. Appears to bind to
CC       specific receptors that are distinct from the receptors bound by the
CC       atrial natriuretic and long-acting natriuretic peptides. Possibly
CC       functions in protein excretion in urine by maintaining the integrity of
CC       the proximal tubules and enhancing protein excretion by decreasing
CC       proximal tubular protein reabsorption. {ECO:0000256|ARBA:ARBA00002727}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of natriuresis, diuresis, vasodilation, and inhibiting
CC       aldosterone synthesis. In vitro, promotes the production of cGMP and
CC       induces vasodilation. May promote natriuresis, at least in part, by
CC       enhancing prostaglandin E2 synthesis resulting in the inhibition of
CC       renal Na+-K+-ATPase (By similarity). However reports on the involvement
CC       of this peptide in mammal blood volume and blood pressure homeostasis
CC       are conflicting; according to a report, in vivo it is not sufficient to
CC       activate cGMP and does not inhibit collecting duct transport nor effect
CC       diuresis and natriuresis (By similarity). Appears to bind to specific
CC       receptors that are distinct from the receptors bound by atrial
CC       natriuretic peptide and vessel dilator. Possibly enhances protein
CC       excretion in urine by decreasing proximal tubular protein reabsorption.
CC       {ECO:0000256|ARBA:ARBA00024972}.
CC   -!- FUNCTION: May have a role in cardio-renal homeostasis through
CC       regulation of regulation of natriuresis and vasodilation. In vivo
CC       promotes natriuresis. In vitro, vasodilates intestinal smooth muscle
CC       but not smooth muscle strips. {ECO:0000256|ARBA:ARBA00003244}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked antiparallel dimer.
CC       {ECO:0000256|ARBA:ARBA00011384}.
CC   -!- SUBCELLULAR LOCATION: Cell projection {ECO:0000256|ARBA:ARBA00004316}.
CC       Perikaryon {ECO:0000256|ARBA:ARBA00004484}. Secreted
CC       {ECO:0000256|ARBA:ARBA00004613, 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   EMBL; KB030727; ELK10515.1; -; Genomic_DNA.
DR   AlphaFoldDB; L5KG38; -.
DR   STRING; 9402.L5KG38; -.
DR   eggNOG; ENOG502S9RQ; Eukaryota.
DR   InParanoid; L5KG38; -.
DR   Proteomes; UP000010552; Unassembled WGS sequence.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005179; F:hormone activity; IEA:UniProtKB-KW.
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; IPR002407; Natriuretic_peptide_atrial.
DR   PANTHER; PTHR14066; ATRIAL NATRIURETIC FACTOR PRECURSOR; 1.
DR   PANTHER; PTHR14066:SF2; NATRIURETIC PEPTIDES A; 1.
DR   Pfam; PF00212; ANP; 1.
DR   PRINTS; PR00711; ANATPEPTIDE.
DR   PRINTS; PR00710; NATPEPTIDES.
DR   SMART; SM00183; NAT_PEP; 1.
DR   PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE   3: Inferred from homology;
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Hormone {ECO:0000256|ARBA:ARBA00022702};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010552};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW   Vasoactive {ECO:0000256|RuleBase:RU003686}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..249
FT                   /note="Natriuretic peptides A"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003969117"
FT   REGION          66..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   249 AA;  27108 MW;  2719096684AF3E90 CRC64;
     MGSFSTITTS FLLLLVLQLP GQTSANPLYS SVSNADLMDF KNLLDHLEDK MPLEDEVVPP
     QVLSEQNEEA EAALSPLPEV PPWTGEVSPA QRDGGTLGRG PWDSSDRSAL LKNKLRALLA
     APRSLRRSSC FGGRMDRIGA QSGLGCNSFR VRESGDGMWK RDGEKGNRGF IEAYALSKNT
     SRGYVQQQRD QHRSLLPWKF LPQLGGGPMN HGTMTSFLAT ACRVSAEGKI TAMSTGNLKC
     SWAKSPSYS
//
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