ANF39_ORNAN
ID ANF39_ORNAN Reviewed; 121 AA.
AC P84715;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 2.
DT 25-MAY-2022, entry version 63.
DE RecName: Full=C-type natriuretic peptide;
DE Short=CNP;
DE Contains:
DE RecName: Full=Venom peptide 1;
DE Contains:
DE RecName: Full=Venom peptide 2;
DE Contains:
DE RecName: Full=Venom peptide 3;
DE Contains:
DE RecName: Full=Venom peptide 4;
DE Contains:
DE RecName: Full=Venom peptide 5;
DE Contains:
DE RecName: Full=Venom peptide 6;
DE Contains:
DE RecName: Full=Venom peptide 7;
DE Contains:
DE RecName: Full=Venom peptide 8;
DE Contains:
DE RecName: Full=Venom peptide 9;
DE Contains:
DE RecName: Full=Venom peptide 10;
DE Contains:
DE RecName: Full=Venom peptide 11;
DE Contains:
DE RecName: Full=C-type natriuretic peptide 39;
DE AltName: Full=ovCNP-39;
DE Flags: Precursor;
OS Ornithorhynchus anatinus (Duckbill platypus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Monotremata; Ornithorhynchidae; Ornithorhynchus.
OX NCBI_TaxID=9258;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=18464734; DOI=10.1038/nature06936;
RA Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P.,
RA Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P.,
RA Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L.,
RA Fulton B., Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R.,
RA Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K.,
RA Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D.,
RA Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A.,
RA Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S.,
RA Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J.,
RA Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P.,
RA Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D.,
RA Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A.,
RA Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J.,
RA Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A.,
RA Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R.,
RA Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P.,
RA Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P.,
RA Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M.,
RA de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K.;
RT "Genome analysis of the platypus reveals unique signatures of evolution.";
RL Nature 453:175-183(2008).
RN [2]
RP PROTEIN SEQUENCE OF 45-63 AND 83-91, FUNCTION, D-AMINO ACID AT LEU-84, AND
RP CYCLIZATION.
RX PubMed=19928958; DOI=10.1021/ja908148z;
RA Kita M., Black D.S., Ohno O., Yamada K., Kigoshi H., Uemura D.;
RT "Duck-billed platypus venom peptides induce Ca2+ influx in neuroblastoma
RT cells.";
RL J. Am. Chem. Soc. 131:18038-18039(2009).
RN [3] {ECO:0000305}
RP PROTEIN SEQUENCE OF 83-121, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom;
RX PubMed=9827022; DOI=10.1016/s0742-8413(98)00030-9;
RA de Plater G.M., Martin R.L., Milburn P.J.;
RT "A C-type natriuretic peptide from the venom of the platypus
RT (Ornithorhynchus anatinus): structure and pharmacology.";
RL Comp. Biochem. Physiol. 120C:99-110(1998).
RN [4] {ECO:0000305}
RP PROTEIN SEQUENCE OF 83-92, FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MASS SPECTROMETRY.
RC TISSUE=Venom {ECO:0000269|PubMed:7597719};
RX PubMed=7597719; DOI=10.1016/0041-0101(94)00150-7;
RA de Plater G., Martin R.L., Milburn P.J.;
RT "A pharmacological and biochemical investigation of the venom from the
RT platypus (Ornithorhynchus anatinus).";
RL Toxicon 33:157-169(1995).
RN [5] {ECO:0000305}
RP FUNCTION.
RX PubMed=9663691; DOI=10.1016/s0041-0101(97)00176-1;
RA de Plater G.M., Martin R.L., Milburn P.J.;
RT "The natriuretic peptide (ovCNP-39) from platypus (Ornithorhynchus
RT anatinus) venom relaxes the isolated rat uterus and promotes oedema and
RT mast cell histamine release.";
RL Toxicon 36:847-857(1998).
RN [6] {ECO:0000305}
RP FUNCTION.
RX PubMed=10409107; DOI=10.1152/ajpcell.1999.277.1.c43;
RA Kourie J.I.;
RT "Calcium dependence of C-type natriuretic peptide-formed fast K(+)
RT channel.";
RL Am. J. Physiol. 277:C43-C50(1999).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=10381585; DOI=10.1111/j.1469-7793.1999.0359p.x;
RA Kourie J.I.;
RT "Characterization of a C-type natriuretic peptide (CNP-39)-formed cation-
RT selective channel from platypus (Ornithorhynchus anatinus) venom.";
RL J. Physiol. (Lond.) 518:359-369(1999).
RN [8] {ECO:0000305}
RP D-AMINO ACID AT LEU-84.
RX PubMed=12135762; DOI=10.1016/s0014-5793(02)03050-8;
RA Torres A.M., Menz I., Alewood P.F., Bansal P., Lahnstein J.,
RA Gallagher C.H., Kuchel P.W.;
RT "D-amino acid residue in the C-type natriuretic peptide from the venom of
RT the mammal, Ornithorhynchus anatinus, the Australian platypus.";
RL FEBS Lett. 524:172-176(2002).
RN [9] {ECO:0000305}
RP STRUCTURE BY NMR OF 83-121.
RX PubMed=12175607; DOI=10.1016/s0041-0101(01)00266-5;
RA Torres A.M., Alewood D., Alewood P.F., Gallagher C.H., Kuchel P.W.;
RT "Conformations of platypus venom C-type natriuretic peptide in aqueous
RT solution and sodium dodecyl sulfate micelles.";
RL Toxicon 40:711-719(2002).
CC -!- FUNCTION: Venom component with vasorelaxant activity. In vitro
CC stimulates the production of cGMP in rat aortic smooth muscle cells and
CC histamine release from rat peritoneal mast cells. Induces relaxation of
CC isolated rat uterus. Induces local edema following subplantar injection
CC into rat hind paw. Forms voltage-dependent cation channels which are
CC weakly selective for potassium relative to sodium, and whose
CC conductance decreases with increasing dehydration energy of the
CC monovalent cation. The activity of the fast cation channels is calcium
CC dependent and is characterized by short bursts of current separated by
CC long periods of inactivation. {ECO:0000269|PubMed:10381585,
CC ECO:0000269|PubMed:10409107, ECO:0000269|PubMed:7597719,
CC ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}.
CC -!- FUNCTION: Venom peptide 1 induces slow and continuous calcium influx in
CC IMR-32 human neuroblastoma cells. Venom peptide 4 weakly induces
CC calcium influx in IMR-32 human neuroblastoma cells while venom peptide
CC 2 was not observed to induce calcium influx.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7597719,
CC ECO:0000269|PubMed:9663691, ECO:0000269|PubMed:9827022}.
CC -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC {ECO:0000269|PubMed:7597719, ECO:0000269|PubMed:9663691,
CC ECO:0000269|PubMed:9827022}.
CC -!- PTM: Stereoinversion of L-Leu-84 (in ovCNP-39a) to D-Leu-84 (in ovCNP-
CC 39b). {ECO:0000269|PubMed:12135762, ECO:0000269|PubMed:19928958}.
CC -!- MASS SPECTROMETRY: [C-type natriuretic peptide 39]: Mass=4207.9;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9827022};
CC -!- MASS SPECTROMETRY: [C-type natriuretic peptide 39]: Mass=4208.3;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:9827022};
CC -!- MASS SPECTROMETRY: [C-type natriuretic peptide 39]: Mass=4212;
CC Method=MALDI; Evidence={ECO:0000269|PubMed:7597719};
CC -!- SIMILARITY: In the C-terminal section; belongs to the natriuretic
CC peptide family. {ECO:0000305}.
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DR EMBL; AAPN01060770; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAPN01060771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; P84715; -.
DR STRING; 9258.ENSOANP00000019499; -.
DR Proteomes; UP000002279; Unplaced.
DR GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR GO; GO:0005179; F:hormone activity; IBA:GO_Central.
DR GO; GO:0051427; F:hormone receptor binding; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0005272; F:sodium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0090729; F:toxin activity; IDA:UniProtKB.
DR GO; GO:0006182; P:cGMP biosynthetic process; IBA:GO_Central.
DR GO; GO:0044398; P:envenomation resulting in induction of edema in another organism; IDA:UniProtKB.
DR GO; GO:0035896; P:positive regulation of mast cell degranulation in another organism; IDA:UniProtKB.
DR GO; GO:0044619; P:positive regulation of relaxation of uterine smooth muscle in another organism; IDA:UniProtKB.
DR GO; GO:0007168; P:receptor guanylyl cyclase signaling pathway; IBA:GO_Central.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:UniProtKB-KW.
DR GO; GO:0042311; P:vasodilation; IEA:UniProtKB-KW.
DR InterPro; IPR002406; C_natriurtcpep.
DR InterPro; IPR000663; Natr_peptide.
DR InterPro; IPR030480; Natr_peptide_CS.
DR Pfam; PF00212; ANP; 1.
DR PRINTS; PR00713; CNATPEPTIDE.
DR PRINTS; PR00710; NATPEPTIDES.
DR SMART; SM00183; NAT_PEP; 1.
DR PROSITE; PS00263; NATRIURETIC_PEPTIDE; 1.
PE 1: Evidence at protein level;
KW D-amino acid; Direct protein sequencing; Hypotensive agent; Ion channel;
KW Ion transport; Neurotoxin; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Secreted; Signal; Sodium;
KW Sodium channel; Sodium transport; Toxin; Transport; Vasoactive;
KW Vasodilator.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..44
FT /evidence="ECO:0000269|PubMed:19928958"
FT /id="PRO_0000393552"
FT PEPTIDE 45..63
FT /note="Venom peptide 10"
FT /id="PRO_0000393553"
FT PEPTIDE 45..63
FT /note="Venom peptide 11"
FT /id="PRO_0000393554"
FT PEPTIDE 45..62
FT /note="Venom peptide 8"
FT /id="PRO_0000393555"
FT PEPTIDE 47..62
FT /note="Venom peptide 7"
FT /id="PRO_0000393556"
FT PEPTIDE 51..62
FT /note="Venom peptide 6"
FT /id="PRO_0000393557"
FT PEPTIDE 52..63
FT /note="Venom peptide 9"
FT /id="PRO_0000393558"
FT PEPTIDE 52..62
FT /note="Venom peptide 5"
FT /id="PRO_0000393559"
FT PROPEP 64..82
FT /id="PRO_0000393560"
FT PEPTIDE 83..121
FT /note="C-type natriuretic peptide 39"
FT /id="PRO_0000045067"
FT PEPTIDE 83..91
FT /note="Venom peptide 4"
FT /id="PRO_0000393561"
FT PEPTIDE 83..89
FT /note="Venom peptide 3"
FT /id="PRO_0000393562"
FT PEPTIDE 85..91
FT /note="Venom peptide 1"
FT /id="PRO_0000393563"
FT PEPTIDE 86..91
FT /note="Venom peptide 2"
FT /id="PRO_0000393564"
FT REGION 22..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..70
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 84
FT /note="D-leucine; in forms ovCNP-39b, venom peptide 3 and
FT venom peptide 4"
FT /evidence="ECO:0000269|PubMed:12135762,
FT ECO:0000269|PubMed:19928958"
FT CROSSLNK 45..46
FT /note="Alanine isoaspartyl cyclopeptide (Ala-Asn); in form
FT venom peptide 10"
FT CONFLICT 90
FT /note="P -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 121 AA; 13148 MW; 4DB01932ABB50B64 CRC64;
MHLSHLLAWA LLLTLLSLRA EAKPPSPQPQ VPRSPGDEAS EAVAANGGGK KGDKEPKGDR
PRLLRELRLD TRSRGSRGVW TRLLHDHPNP RKYKPANKKG LSKGCFGLKL DRIGSTSGLG
C
