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P84715

- ANF39_ORNAN

UniProt

P84715 - ANF39_ORNAN

Protein

C-type natriuretic peptide

Gene
N/A
Organism
Ornithorhynchus anatinus (Duckbill platypus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.5 Publications
    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.

    GO - Molecular functioni

    1. potassium channel activity Source: UniProtKB-KW
    2. sodium channel activity Source: UniProtKB-KW

    GO - Biological processi

    1. cGMP biosynthetic process Source: Ensembl
    2. growth plate cartilage chondrocyte differentiation Source: Ensembl
    3. growth plate cartilage chondrocyte proliferation Source: Ensembl
    4. positive regulation of mast cell degranulation in other organism Source: UniProtKB
    5. post-embryonic development Source: Ensembl
    6. receptor guanylyl cyclase signaling pathway Source: Ensembl
    7. regulation of multicellular organism growth Source: Ensembl
    8. vasodilation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hypotensive agent, Ion channel, Neurotoxin, Potassium channel, Sodium channel, Toxin, Vasoactive, Vasodilator

    Keywords - Biological processi

    Ion transport, Potassium transport, Sodium transport, Transport

    Keywords - Ligandi

    Potassium, Sodium

    Names & Taxonomyi

    Protein namesi
    OrganismiOrnithorhynchus anatinus (Duckbill platypus)
    Taxonomic identifieri9258 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaMonotremataOrnithorhynchidaeOrnithorhynchus
    ProteomesiUP000002279: Unplaced

    Subcellular locationi

    Secreted 3 Publications

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Propeptidei23 – 44221 PublicationPRO_0000393552Add
    BLAST
    Peptidei45 – 6319Venom peptide 10PRO_0000393553Add
    BLAST
    Peptidei45 – 6319Venom peptide 11PRO_0000393554Add
    BLAST
    Peptidei45 – 6218Venom peptide 8PRO_0000393555Add
    BLAST
    Peptidei47 – 6216Venom peptide 7PRO_0000393556Add
    BLAST
    Peptidei51 – 6212Venom peptide 6PRO_0000393557Add
    BLAST
    Peptidei52 – 6312Venom peptide 9PRO_0000393558Add
    BLAST
    Peptidei52 – 6211Venom peptide 5PRO_0000393559Add
    BLAST
    Propeptidei64 – 8219PRO_0000393560Add
    BLAST
    Peptidei83 – 12139C-type natriuretic peptide 39PRO_0000045067Add
    BLAST
    Peptidei83 – 919Venom peptide 4PRO_0000393561
    Peptidei83 – 897Venom peptide 3PRO_0000393562
    Peptidei85 – 917Venom peptide 1PRO_0000393563
    Peptidei86 – 916Venom peptide 2PRO_0000393564

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki45 ↔ 46Alanine isoaspartyl cyclopeptide (Ala-Asn); in form venom peptide 10
    Modified residuei84 – 841D-leucine; in forms ovCNP-39b, venom peptide 3 and venom peptide 42 Publications

    Post-translational modificationi

    Stereoinversion of L-Leu-84 (in ovCNP-39a) to D-Leu-84 (in ovCNP-39b).2 Publications

    Keywords - PTMi

    D-amino acid

    Expressioni

    Tissue specificityi

    Expressed by the venom gland.3 Publications

    Interactioni

    Protein-protein interaction databases

    STRINGi9258.ENSOANP00000019499.

    Family & Domainsi

    Sequence similaritiesi

    In the C-terminal section; belongs to the natriuretic peptide family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG43160.

    Family and domain databases

    InterProiIPR002406. C_natriurtcpep.
    IPR000663. Natr_peptide.
    [Graphical view]
    PfamiPF00212. ANP. 1 hit.
    [Graphical view]
    PRINTSiPR00713. CNATPEPTIDE.
    PR00710. NATPEPTIDES.
    SMARTiSM00183. NAT_PEP. 1 hit.
    [Graphical view]
    PROSITEiPS00263. NATRIURETIC_PEPTIDE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P84715-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHLSHLLAWA LLLTLLSLRA EAKPPSPQPQ VPRSPGDEAS EAVAANGGGK    50
    KGDKEPKGDR PRLLRELRLD TRSRGSRGVW TRLLHDHPNP RKYKPANKKG 100
    LSKGCFGLKL DRIGSTSGLG C 121
    Length:121
    Mass (Da):13,148
    Last modified:April 20, 2010 - v2
    Checksum:i4DB01932ABB50B64
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti90 – 901P → N AA sequence (PubMed:19928958)Curated

    Mass spectrometryi

    Molecular mass is 4207.9 Da from positions 83 - 121. Determined by MALDI. 1 Publication
    Molecular mass is 4208.3 Da from positions 83 - 121. Determined by MALDI. 1 Publication
    Molecular mass is 4212 Da from positions 83 - 121. Determined by MALDI. 1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAPN01060770 Genomic DNA. No translation available.
    AAPN01060771 Genomic DNA. No translation available.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AAPN01060770 Genomic DNA. No translation available.
    AAPN01060771 Genomic DNA. No translation available.

    3D structure databases

    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9258.ENSOANP00000019499.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi NOG43160.

    Family and domain databases

    InterProi IPR002406. C_natriurtcpep.
    IPR000663. Natr_peptide.
    [Graphical view ]
    Pfami PF00212. ANP. 1 hit.
    [Graphical view ]
    PRINTSi PR00713. CNATPEPTIDE.
    PR00710. NATPEPTIDES.
    SMARTi SM00183. NAT_PEP. 1 hit.
    [Graphical view ]
    PROSITEi PS00263. NATRIURETIC_PEPTIDE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [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, CYCLIZATION.
    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: Venom1 Publication.
    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.

    Entry informationi

    Entry nameiANF39_ORNAN
    AccessioniPrimary (citable) accession number: P84715
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 22, 2005
    Last sequence update: April 20, 2010
    Last modified: October 1, 2014
    This is version 39 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programAnimal Toxin Annotation Program
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3