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P84715 (ANF39_ORNAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Protein attributes

Sequence length121 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

In the C-terminal section; 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 processIon transport
Potassium transport
Sodium transport
Transport
   Cellular componentSecreted
   DomainSignal
   LigandPotassium
Sodium
   Molecular functionIon channel
Neurotoxin
Potassium channel
Sodium channel
Toxin
Vasoactive
Vasodilator
   PTMD-amino acid
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcGMP biosynthetic process

Inferred from electronic annotation. Source: Compara

growth plate cartilage chondrocyte differentiation

Inferred from electronic annotation. Source: Compara

growth plate cartilage chondrocyte proliferation

Inferred from electronic annotation. Source: Compara

positive regulation of mast cell degranulation in other organism

Inferred from direct assay Ref.5. Source: UniProtKB

post-embryonic development

Inferred from electronic annotation. Source: Compara

receptor guanylyl cyclase signaling pathway

Inferred from electronic annotation. Source: Compara

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Compara

sodium ion transmembrane transport

Inferred from electronic annotation. Source: GOC

vasodilation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionpotassium 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Propeptide23 – 4422
PRO_0000393552
Peptide45 – 6319Venom peptide 10 Ref.2
PRO_0000393553
Peptide45 – 6319Venom peptide 11 Ref.2
PRO_0000393554
Peptide45 – 6218Venom peptide 8
PRO_0000393555
Peptide47 – 6216Venom peptide 7
PRO_0000393556
Peptide51 – 6212Venom peptide 6
PRO_0000393557
Peptide52 – 6312Venom peptide 9
PRO_0000393558
Peptide52 – 6211Venom peptide 5
PRO_0000393559
Propeptide64 – 8219
PRO_0000393560
Peptide83 – 12139C-type natriuretic peptide 39 Ref.3
PRO_0000045067
Peptide83 – 919Venom peptide 4
PRO_0000393561
Peptide83 – 897Venom peptide 3
PRO_0000393562
Peptide85 – 917Venom peptide 1
PRO_0000393563
Peptide86 – 916Venom peptide 2
PRO_0000393564

Amino acid modifications

Modified residue841D-leucine; in forms ovCNP-39b, venom peptide 3 and venom peptide 4 Ref.2 Ref.8
Cross-link45 ↔ 46Alanine isoaspartyl cyclopeptide (Ala-Asn); in form venom peptide 10

Experimental info

Sequence conflict901P → N AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
P84715 [UniParc].

Last modified April 20, 2010. Version 2.
Checksum: 4DB01932ABB50B64

FASTA12113,148
        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

« Hide

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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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

ModBaseSearch...

Protein-protein interaction databases

STRING9258.ENSOANP00000019499.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG43160.
OrthoDBEOG4RFKV7.

Family and domain databases

InterProIPR002406. C_natriurtcpep.
IPR000663. Natr_peptide.
[Graphical view]
PfamPF00212. ANP. 1 hit.
[Graphical view]
PRINTSPR00713. CNATPEPTIDE.
PR00710. NATPEPTIDES.
SMARTSM00183. NAT_PEP. 1 hit.
[Graphical view]
PROSITEPS00263. NATRIURETIC_PEPTIDE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameANF39_ORNAN
AccessionPrimary (citable) accession number: P84715
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: April 20, 2010
Last modified: May 1, 2013
This is version 35 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programAnimal Toxin Annotation Program
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents