ANF_PIG
ID ANF_PIG Reviewed; 150 AA.
AC P24259;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=Natriuretic peptides A {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANF {ECO:0000250|UniProtKB:P01161};
DE Short=proANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atrial natriuretic peptide prohormone {ECO:0000250|UniProtKB:P01160};
DE Short=preproANP {ECO:0000250|UniProtKB:P01160};
DE Short=proANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atriopeptigen {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Cardiodilatin {ECO:0000250|UniProtKB:P01160};
DE Short=CDD {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=preproCDD-ANF {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Long-acting natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=LANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Long-acting natriuretic hormone {ECO:0000305};
DE Short=LANH {ECO:0000305};
DE AltName: Full=Pro atrial natriuretic factor 1-30 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 1-30 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 1-30 {ECO:0000305};
DE Short=proANP 1-30 {ECO:0000305};
DE Contains:
DE RecName: Full=Vessel dilator {ECO:0000250|UniProtKB:P01160};
DE Short=VSDL {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic factor 31-67 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 31-67 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 31-67 {ECO:0000305};
DE Short=proANP 31-67 {ECO:0000305};
DE Contains:
DE RecName: Full=Kaliuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=KP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic factor 79-98 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 79-98 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 79-98 {ECO:0000305};
DE Short=proANP 79-98 {ECO:0000305};
DE Contains:
DE RecName: Full=Urodilatin {ECO:0000250|UniProtKB:P01160};
DE Short=URO {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD 95-126 {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANP (95-126) {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Pro atrial natriuretic peptide 95-126 {ECO:0000250|UniProtKB:P01160};
DE Short=proANP 95-126 {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Auriculin-C {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 1-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 1-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Auriculin-D {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 3-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 3-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atrial natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE Short=ANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Alpha-atrial natriuretic peptide {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Alpha-hANP {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Atrial natriuretic factor {ECO:0000250|UniProtKB:P01160};
DE Short=ANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANF {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=CDD-ANP (99-126) {ECO:0000250|UniProtKB:P01160};
DE AltName: Full=Cardionatrin {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Pro atrial natriuretic factor 99-126 {ECO:0000250|UniProtKB:P01160};
DE Short=proANF 99-126 {ECO:0000250|UniProtKB:P01160};
DE Contains:
DE RecName: Full=Auriculin-B {ECO:0000305};
DE AltName: Full=Atrial natriuretic factor 8-33 {ECO:0000250|UniProtKB:P01161};
DE Short=ANF 8-33 {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Auriculin-A {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-1 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin I {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-2 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin II {ECO:0000250|UniProtKB:P01161};
DE Contains:
DE RecName: Full=Atriopeptin-3 {ECO:0000250|UniProtKB:P01161};
DE AltName: Full=Atriopeptin III {ECO:0000250|UniProtKB:P01161};
DE Flags: Precursor;
GN Name=NPPA;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart right atrium;
RX PubMed=2147477; DOI=10.1093/nar/18.22.6704;
RA Maegert H.-J., Appelhans H., Gassen H.G., Forssmann W.-G.;
RT "Nucleotide sequence of a porcine prepro atrial natriuretic peptide (ANP)
RT cDNA.";
RL Nucleic Acids Res. 18:6704-6704(1990).
RN [2]
RP PROTEIN SEQUENCE OF 25-150.
RC TISSUE=Heart right atrium;
RX PubMed=6549270; DOI=10.1007/bf00219856;
RA Forssmann W.-G., Birr C., Carlquist M., Christmann M., Finke R.,
RA Henschen A., Hock D., Kirchheim H., Kreye V., Lottspeich F., Metz J.,
RA Mutt V., Reinecke M.;
RT "The auricular myocardiocytes of the heart constitute an endocrine organ.
RT Characterization of a porcine cardiac peptide hormone, cardiodilatin-126.";
RL Cell Tissue Res. 238:425-430(1984).
RN [3]
RP PROTEIN SEQUENCE OF 25-54.
RC TISSUE=Heart right atrium;
RX PubMed=6689515; DOI=10.1007/bf00304269;
RA Forssmann W.-G., Hock D., Lottspeich F., Henschen A., Kreye V.,
RA Christmann M., Reinecke M., Metz J., Carlquist M., Mutt V.;
RT "The right auricle of the heart is an endocrine organ. Cardiodilatin as a
RT peptide hormone candidate.";
RL Anat. Embryol. (Berl.) 168:307-313(1983).
RN [4]
RP FUNCTION (ATRIAL NATRIURETIC PEPTIDE), AND TISSUE SPECIFICITY (ATRIAL
RP NATRIURETIC PEPTIDE).
RC TISSUE=Brain {ECO:0000303|PubMed:2964562};
RX PubMed=2964562; DOI=10.1038/332078a0;
RA Sudoh T., Kangawa K., Minamino N., Matsuo H.;
RT "A new natriuretic peptide in porcine brain.";
RL Nature 332:78-81(1988).
CC -!- FUNCTION: [Atrial natriuretic peptide]: Hormone that plays a key role
CC in mediating cardio-renal homeostasis, and is involved in vascular
CC remodeling and regulating energy metabolism (By similarity). Acts by
CC specifically binding and stimulating NPR1 to produce cGMP, which in
CC turn activates effector proteins, such as PRKG1, that drive various
CC biological responses (By similarity). Regulates vasodilation,
CC natriuresis, diuresis and aldosterone synthesis and is therefore
CC essential for regulating blood pressure, controlling the extracellular
CC fluid volume and maintaining the fluid-electrolyte balance
CC (PubMed:2964562). Also involved in inhibiting cardiac remodeling and
CC cardiac hypertrophy by inducing cardiomyocyte apoptosis and attenuating
CC the growth of cardiomyocytes and fibroblasts (By similarity). Plays a
CC role in female pregnancy by promoting trophoblast invasion and spiral
CC artery remodeling in uterus, and thus prevents pregnancy-induced
CC hypertension (By similarity). In adipose tissue, acts in various
CC cGMP- and PKG-dependent pathways to regulate lipid metabolism and
CC energy homeostasis (By similarity). This includes up-regulating lipid
CC metabolism and mitochondrial oxygen utilization by activating the AMP-
CC activated protein kinase (AMPK), and increasing energy expenditure by
CC acting via MAPK11 to promote the UCP1-dependent thermogenesis of brown
CC adipose tissue (By similarity). Binds the clearance receptor NPR3 which
CC removes the hormone from circulation (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P05125,
CC ECO:0000269|PubMed:2964562}.
CC -!- FUNCTION: [Long-acting natriuretic peptide]: May have a role in cardio-
CC renal homeostasis through regulation of natriuresis, diuresis,
CC vasodilation, and inhibiting aldosterone synthesis. In vitro, promotes
CC 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 (By similarity).
CC However reports on the involvement of this peptide in mammal blood
CC volume and blood pressure homeostasis are conflicting; according to a
CC report, in vivo it is not sufficient to activate cGMP and does not
CC inhibit collecting duct transport nor effect diuresis and natriuresis
CC (By similarity). Appears to bind to specific receptors that are
CC distinct from the receptors bound by atrial natriuretic peptide and
CC vessel dilator. Possibly enhances protein excretion in urine by
CC decreasing proximal tubular protein reabsorption (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Vessel dilator]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis, diuresis, and vasodilation. In
CC vitro, promotes the production of cGMP and induces vasodilation. May
CC promote natriuresis, at least in part, by enhancing prostaglandin E2
CC synthesis resulting in the inhibition of renal Na+-K+-ATPase. However
CC reports on the involvement of this peptide in mammal blood volume and
CC blood pressure homeostasis are conflicting; according to a report it is
CC not 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:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Kaliuretic peptide]: May have a role in cardio-renal
CC homeostasis through regulation of diuresis and inhibiting aldosterone
CC synthesis. In vitro, promotes the production of cGMP and induces
CC vasodilation. May promote natriuresis, at least in part, by enhancing
CC prostaglandin E2 synthesis resulting in the inhibition of renal Na+-K+-
CC ATPase. May have a role in potassium excretion but not sodium excretion
CC (natriuresis). Possibly enhances protein excretion in urine by
CC decreasing proximal tubular protein reabsorption.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Urodilatin]: Hormone produced in the kidneys that appears to
CC be important for maintaining cardio-renal homeostasis. Mediates
CC vasodilation, natriuresis and diuresis primarily in the renal system,
CC in order to maintain the extracellular fluid volume and control the
CC fluid-electrolyte balance. Specifically binds and stimulates cGMP
CC production by renal transmembrane receptors, likely NPR1. Urodilatin
CC not ANP, may be the natriuretic peptide responsible for the regulation
CC of sodium and water homeostasis in the kidney.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- FUNCTION: [Auriculin-D]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis and in vitro, vasodilates renal artery strips.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Auriculin-B]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis and in vitro, vasodilates renal artery strips.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Auriculin-A]: May have a role in cardio-renal homeostasis
CC through regulation of regulation of natriuresis and vasodilation. In
CC vivo promotes natriuresis. In vitro, vasodilates intestinal smooth
CC muscle but not smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Atriopeptin-2]: May have a role in cardio-renal homeostasis
CC through regulation of natriuresis and vasodilation. In vivo promotes
CC natriuresis. In vitro, selectively vasodilates intestinal and vascular
CC smooth muscle strips. {ECO:0000250|UniProtKB:P01161}.
CC -!- FUNCTION: [Atriopeptin-1]: May have a role in cardio-renal homeostasis
CC through 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:0000250|UniProtKB:P01161}.
CC -!- SUBUNIT: [Atrial natriuretic peptide]: Homodimer; disulfide-linked
CC antiparallel dimer. {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Long-acting natriuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Vessel dilator]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Kaliuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood.
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Urodilatin]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in urine. Not detected in
CC blood. Increased electrolytes, osmolality and intracellular cAMP levels
CC increase peptide secretion/excretion. {ECO:0000250|UniProtKB:P01160}.
CC -!- SUBCELLULAR LOCATION: [Atrial natriuretic peptide]: Secreted
CC {ECO:0000250|UniProtKB:P01160}. Perikaryon
CC {ECO:0000250|UniProtKB:P01160}. Cell projection
CC {ECO:0000250|UniProtKB:P01160}. Note=Detected in blood. Detected in
CC urine in one study. However, in another study, was not detected in
CC urine. Detected in cytoplasmic bodies and neuronal processes of
CC pyramidal neurons (layers II-VI) (By similarity). Increased secretion
CC in response to the vasopressin AVP (By similarity). Likely to be
CC secreted in response to an increase in atrial pressure or atrial
CC stretch. In kidney cells, secretion increases in response to activated
CC guanylyl cyclases and increased intracellular cAMP levels. Plasma
CC levels increase 15 minutes after a high-salt meal, and decrease back to
CC normal plasma levels 1 hr later (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- SUBCELLULAR LOCATION: [Atriopeptin-3]: Secreted
CC {ECO:0000250|UniProtKB:P01161}. Note=Detected in blood. Slight increase
CC in secretion in response to the vasopressin AVP.
CC {ECO:0000250|UniProtKB:P01161}.
CC -!- TISSUE SPECIFICITY: [Atrial natriuretic peptide]: Brain (at protein
CC level). {ECO:0000269|PubMed:2964562}.
CC -!- PTM: The precursor molecule is proteolytically cleaved by CORIN at Arg-
CC 122 to produce the atrial natriuretic peptide (By similarity).
CC Undergoes further proteolytic cleavage by unknown proteases to give
CC rise to long-acting natriuretic peptide, vessel dilator and kaliuretic
CC peptide (By similarity). Additional processing gives rise to the
CC auriculin and atriopeptin peptides (By similarity). In the kidneys,
CC alternative processing by an unknown protease results in the peptide
CC urodilatin (By similarity). {ECO:0000250|UniProtKB:P01160,
CC ECO:0000250|UniProtKB:P01161}.
CC -!- PTM: [Atrial natriuretic peptide]: Cleavage by MME initiates
CC degradation of the factor and thereby regulates its activity.
CC Degradation by IDE results in reduced activation of NPR1 (in vitro).
CC During IDE degradation, the resulting products can temporarily
CC stimulate NPR2 to produce cGMP, before the fragments are completely
CC degraded and inactivated by IDE (in vitro).
CC {ECO:0000250|UniProtKB:P01160}.
CC -!- PTM: [Urodilatin]: Degraded by IDE. {ECO:0000250|UniProtKB:P01160}.
CC -!- PTM: [Urodilatin]: Phosphorylation on Ser-128 decreases vasorelaxant
CC activity. {ECO:0000250|UniProtKB:P01160}.
CC -!- SIMILARITY: Belongs to the natriuretic peptide family. {ECO:0000305}.
CC -!- CAUTION: [Long-acting natriuretic peptide]: Results concerning the
CC involvement of this peptide in blood volume and blood pressure
CC homeostasis are conflicting. Several studies utilising in vitro and
CC heterologous expression systems show that it is able to activate cGMP
CC and promote vasodilation and natriuresis (By similarity). However, an
CC in vivo study in rat found that it is not sufficient to induce any
CC diuretic, natriuretic, nor hypotensive responses, and is unable to bind
CC NPR1 nor increase guanylyl cyclase activity (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
CC -!- CAUTION: [Vessel dilator]: Results concerning the involvement of this
CC peptide in blood volume and blood pressure homeostasis are conflicting.
CC Several studies utilising in vitro and heterologous expression systems
CC show that it is able to activate cGMP and promote vasodilation and
CC natriuresis (By similarity). However, a heterologous and in vivo
CC expression study in rat found that it is not sufficient to induce any
CC diuretic, natriuretic, nor hypotensive responses, and is unable to bind
CC NPR1 nor increase guanylyl cyclase activity (By similarity).
CC {ECO:0000250|UniProtKB:P01160, ECO:0000250|UniProtKB:P01161}.
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DR EMBL; X54669; CAA38480.1; -; mRNA.
DR PIR; S13107; S13107.
DR RefSeq; NP_999425.1; NM_214260.2.
DR AlphaFoldDB; P24259; -.
DR STRING; 9823.ENSSSCP00000003721; -.
DR BindingDB; P24259; -.
DR PaxDb; P24259; -.
DR GeneID; 397496; -.
DR KEGG; ssc:397496; -.
DR CTD; 4878; -.
DR eggNOG; ENOG502S9RQ; Eukaryota.
DR InParanoid; P24259; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
DR GO; GO:0006182; P:cGMP biosynthetic process; ISS:UniProtKB.
DR GO; GO:0019934; P:cGMP-mediated signaling; IBA:GO_Central.
DR GO; GO:0007565; P:female pregnancy; ISS:UniProtKB.
DR GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; IBA:GO_Central.
DR GO; GO:0007218; P:neuropeptide signaling pathway; IBA:GO_Central.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; ISS:UniProtKB.
DR GO; GO:0008217; P:regulation of blood pressure; ISS:UniProtKB.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR InterPro; IPR002407; Natriuretic_peptide_atrial.
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 1: Evidence at protein level;
KW Cell projection; Direct protein sequencing; Disulfide bond; Hormone;
KW Phosphoprotein; Reference proteome; Secreted; Signal; Vasoactive;
KW Vasodilator.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:6549270,
FT ECO:0000269|PubMed:6689515"
FT CHAIN 25..150
FT /note="Natriuretic peptides A"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449744"
FT PROPEP 25..122
FT /evidence="ECO:0000305"
FT /id="PRO_0000001501"
FT PEPTIDE 25..54
FT /note="Long-acting natriuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449745"
FT PEPTIDE 55..91
FT /note="Vessel dilator"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449746"
FT PROPEP 92..102
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449747"
FT PEPTIDE 103..122
FT /note="Kaliuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449748"
FT PEPTIDE 118..150
FT /note="Auriculin-C"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449749"
FT PEPTIDE 119..150
FT /note="Urodilatin"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000449750"
FT PEPTIDE 120..144
FT /note="Auriculin-D"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449751"
FT PEPTIDE 123..150
FT /note="Atrial natriuretic peptide"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT /id="PRO_0000001502"
FT PEPTIDE 126..150
FT /note="Auriculin-B"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449752"
FT PEPTIDE 126..149
FT /note="Auriculin-A"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449753"
FT PEPTIDE 127..150
FT /note="Atriopeptin-3"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449754"
FT PEPTIDE 127..149
FT /note="Atriopeptin-2"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449755"
FT PEPTIDE 127..147
FT /note="Atriopeptin-1"
FT /evidence="ECO:0000250|UniProtKB:P01161"
FT /id="PRO_0000449756"
FT REGION 77..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 122..123
FT /note="Cleavage; by CORIN"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT SITE 129..130
FT /note="Cleavage; by MME"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT MOD_RES 128
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P01160"
FT DISULFID 129..145
FT /evidence="ECO:0000250|UniProtKB:P01160"
SQ SEQUENCE 150 AA; 16352 MW; 16CFE4FAF0BCE063 CRC64;
MSSFTITVSF LLVLVFQFPG QTRANPVYGS VSNADLMDFK NLLDHLEDKM PLEDEAMPPQ
VLSEQNEEVG APLSPLLEVP PWTGEVNPAQ RDGGALGRGP WDASDRSALL KSKLRALLAA
PRSLRRSSCF GGRMDRIGAQ SGLGCNSFRY
