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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
 
 
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