P84715 (ANF39_ORNAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names	Recommended name: C-type natriuretic peptide Cleaved into the following 12 chains: C-type natriuretic peptide 39 Alternative name(s): ovCNP-39 Venom peptide 1 Venom peptide 2 Venom peptide 3 Venom peptide 4 Venom peptide 5 Venom peptide 6 Venom peptide 7 Venom peptide 8 Venom peptide 9 Venom peptide 10 Venom peptide 11
Organism	Ornithorhynchus anatinus (Duckbill platypus)
Taxonomic identifier	9258 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Monotremata › Ornithorhynchidae › Ornithorhynchus

Protein attributes

Sequence length	121 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Venom component with vasorelaxant activity. In vitro stimulates the production of cGMP in rat aortic smooth muscle cells and histamine release from rat peritoneal mast cells. Induces relaxation of isolated rat uterus. Induces local edema following subplantar injection into rat hind paw. Forms voltage-dependent cation channels which are weakly selective for potassium relative to sodium, and whose conductance decreases with increasing dehydration energy of the monovalent cation. The activity of the fast cation channels is calcium dependent and is characterized by short bursts of current separated by long periods of inactivation. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Venom peptide 1 induces slow and continuous calcium influx in IMR-32 human neuroblastoma cells. Venom peptide 4 weakly induces calcium influx in IMR-32 human neuroblastoma cells while venom peptide 2 was not observed to induce calcium influx. Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7
Subcellular location	Secreted Ref.3 Ref.4 Ref.5.
Tissue specificity	Expressed by the venom gland. Ref.3 Ref.4 Ref.5
Post-translational modification	Stereoinversion of L-Leu-84 (in ovCNP-39a) to D-Leu-84 (in ovCNP-39b).
Sequence similarities	Belongs to the natriuretic peptide family.
Mass spectrometry	Molecular mass is 4207.9 Da from positions 83 - 121. Determined by MALDI. Ref.3 Molecular mass is 4208.3 Da from positions 83 - 121. Determined by MALDI. Ref.3 Molecular mass is 4212 Da from positions 83 - 121. Determined by MALDI. Ref.4

Ontologies

Keywords
Biological process	Ion transport Potassium transport Sodium transport Transport
Cellular component	Secreted
Domain	Signal
Ligand	Potassium Sodium
Molecular function	Ionic channel Neurotoxin Potassium channel Sodium channel Toxin Vasoactive
PTM	D-amino acid
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of mast cell degranulation in other organism Inferred from direct assay Ref.5. Source: UniProtKB regulation of blood vessel size Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	hormone activity Inferred from electronic annotation. Source: InterPro potassium channel activity Inferred from electronic annotation. Source: UniProtKB-KW sodium channel activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Propeptide	23 – 44	22			PRO_0000393552
	Peptide	45 – 63	19	Venom peptide 10 Ref.2		PRO_0000393553
	Peptide	45 – 63	19	Venom peptide 11 Ref.2		PRO_0000393554
	Peptide	45 – 62	18	Venom peptide 8		PRO_0000393555
	Peptide	47 – 62	16	Venom peptide 7		PRO_0000393556
	Peptide	51 – 62	12	Venom peptide 6		PRO_0000393557
	Peptide	52 – 63	12	Venom peptide 9		PRO_0000393558
	Peptide	52 – 62	11	Venom peptide 5		PRO_0000393559
	Propeptide	64 – 82	19			PRO_0000393560
	Peptide	83 – 121	39	C-type natriuretic peptide 39 Ref.3		PRO_0000045067
	Peptide	83 – 91	9	Venom peptide 4		PRO_0000393561
	Peptide	83 – 89	7	Venom peptide 3		PRO_0000393562
	Peptide	85 – 91	7	Venom peptide 1		PRO_0000393563
	Peptide	86 – 91	6	Venom peptide 2		PRO_0000393564
Amino acid modifications
	Modified residue	84	1	D-leucine; in forms ovCNP-39b, venom peptide 3 and venom peptide 4 Ref.2 Ref.8
	Cross-link	45 ↔ 46		Alanine isoaspartyl cyclopeptide (Ala-Asn); in form venom peptide 10
Experimental info
	Sequence conflict	90	1	P → N AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P84715 [UniParc]. Last modified April 20, 2010. Version 2. Checksum: 4DB01932ABB50B64	FASTA	121	13,148
	10 20 30 40 50 60 MHLSHLLAWA LLLTLLSLRA EAKPPSPQPQ VPRSPGDEAS EAVAANGGGK KGDKEPKGDR 70 80 90 100 110 120 PRLLRELRLD TRSRGSRGVW TRLLHDHPNP RKYKPANKKG LSKGCFGLKL DRIGSTSGLG C

References

[1]	"Genome analysis of the platypus reveals unique signatures of evolution." Warren W.C., Hillier L.W., Marshall Graves J.A., Birney E., Ponting C.P., Grutzner F., Belov K., Miller W., Clarke L., Chinwalla A.T., Yang S.P., Heger A., Locke D.P., Miethke P., Waters P.D., Veyrunes F., Fulton L., Fulton B. , Graves T., Wallis J., Puente X.S., Lopez-Otin C., Ordonez G.R., Eichler E.E., Chen L., Cheng Z., Deakin J.E., Alsop A., Thompson K., Kirby P., Papenfuss A.T., Wakefield M.J., Olender T., Lancet D., Huttley G.A., Smit A.F., Pask A., Temple-Smith P., Batzer M.A., Walker J.A., Konkel M.K., Harris R.S., Whittington C.M., Wong E.S., Gemmell N.J., Buschiazzo E., Vargas Jentzsch I.M., Merkel A., Schmitz J., Zemann A., Churakov G., Kriegs J.O., Brosius J., Murchison E.P., Sachidanandam R., Smith C., Hannon G.J., Tsend-Ayush E., McMillan D., Attenborough R., Rens W., Ferguson-Smith M., Lefevre C.M., Sharp J.A., Nicholas K.R., Ray D.A., Kube M., Reinhardt R., Pringle T.H., Taylor J., Jones R.C., Nixon B., Dacheux J.L., Niwa H., Sekita Y., Huang X., Stark A., Kheradpour P., Kellis M., Flicek P., Chen Y., Webber C., Hardison R., Nelson J., Hallsworth-Pepin K., Delehaunty K., Markovic C., Minx P., Feng Y., Kremitzki C., Mitreva M., Glasscock J., Wylie T., Wohldmann P., Thiru P., Nhan M.N., Pohl C.S., Smith S.M., Hou S., Nefedov M., de Jong P.J., Renfree M.B., Mardis E.R., Wilson R.K. Nature 453:175-183(2008) [PubMed: 18464734] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Duck-billed platypus venom peptides induce Ca2+ influx in neuroblastoma cells." Kita M., Black D.S., Ohno O., Yamada K., Kigoshi H., Uemura D. J. Am. Chem. Soc. 131:18038-18039(2009) [PubMed: 19928958] [Abstract] Cited for: PROTEIN SEQUENCE OF 45-63 AND 83-91, FUNCTION, D-AMINO ACID AT LEU-84, ALANINE ISOASPARTYL CYCLOPEPTIDE AT 45-46.
[3]	"A C-type natriuretic peptide from the venom of the platypus (Ornithorhynchus anatinus): structure and pharmacology." de Plater G.M., Martin R.L., Milburn P.J. Comp. Biochem. Physiol. 120C:99-110(1998) [PubMed: 9827022] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-121, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Venom.
[4]	"A pharmacological and biochemical investigation of the venom from the platypus (Ornithorhynchus anatinus)." de Plater G., Martin R.L., Milburn P.J. Toxicon 33:157-169(1995) [PubMed: 7597719] [Abstract] Cited for: PROTEIN SEQUENCE OF 83-92, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MASS SPECTROMETRY. Tissue: Venom.
[5]	"The natriuretic peptide (ovCNP-39) from platypus (Ornithorhynchus anatinus) venom relaxes the isolated rat uterus and promotes oedema and mast cell histamine release." de Plater G.M., Martin R.L., Milburn P.J. Toxicon 36:847-857(1998) [PubMed: 9663691] [Abstract] Cited for: FUNCTION.
[6]	"Calcium dependence of C-type natriuretic peptide-formed fast K(+) channel." Kourie J.I. Am. J. Physiol. 277:C43-C50(1999) [PubMed: 10409107] [Abstract] Cited for: FUNCTION.
[7]	"Characterization of a C-type natriuretic peptide (CNP-39)-formed cation-selective channel from platypus (Ornithorhynchus anatinus) venom." Kourie J.I. J. Physiol. (Lond.) 518:359-369(1999) [PubMed: 10381585] [Abstract] Cited for: FUNCTION.
[8]	"D-amino acid residue in the C-type natriuretic peptide from the venom of the mammal, Ornithorhynchus anatinus, the Australian platypus." Torres A.M., Menz I., Alewood P.F., Bansal P., Lahnstein J., Gallagher C.H., Kuchel P.W. FEBS Lett. 524:172-176(2002) [PubMed: 12135762] [Abstract] Cited for: D-AMINO ACID AT LEU-84.
[9]	"Conformations of platypus venom C-type natriuretic peptide in aqueous solution and sodium dodecyl sulfate micelles." Torres A.M., Alewood D., Alewood P.F., Gallagher C.H., Kuchel P.W. Toxicon 40:711-719(2002) [PubMed: 12175607] [Abstract] Cited for: STRUCTURE BY NMR OF 83-121.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AAPN01060770 Genomic DNA. No translation available. AAPN01060771 Genomic DNA. No translation available.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	P84715.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Phylogenomic databases
eggNOG	maNOG21151.
GeneTree	ENSGT00390000015492.
OrthoDB	EOG4RFKV7.
Family and domain databases
InterPro	IPR002406. C_natriurtcpep. IPR000663. Natr_peptide. [Graphical view]
Pfam	PF00212. ANP. 1 hit. [Graphical view]
PRINTS	PR00713. CNATPEPTIDE. PR00710. NATPEPTIDES.
SMART	SM00183. NAT_PEP. 1 hit. [Graphical view]
PROSITE	PS00263. NATRIURETIC_PEPTIDE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ANF39_ORNAN

Accession

Primary (citable) accession number: P84715

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 22, 2005
Last sequence update:	April 20, 2010
Last modified:	November 16, 2011
This is version 29 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Annotation program

Animal Toxin Annotation Program