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Protein

C-type natriuretic peptide

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

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

GO - Biological processi

Complete GO annotation...

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
Proteomesi
  • UP000002279 Componentsi: Unassembled WGS sequence, Unplaced

Subcellular locationi

GO - Cellular componenti

  • extracellular region Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
PropeptideiPRO_000039355223 – 441 PublicationAdd BLAST22
PeptideiPRO_000039355345 – 63Venom peptide 10Add BLAST19
PeptideiPRO_000039355445 – 63Venom peptide 11Add BLAST19
PeptideiPRO_000039355545 – 62Venom peptide 8Add BLAST18
PeptideiPRO_000039355647 – 62Venom peptide 7Add BLAST16
PeptideiPRO_000039355751 – 62Venom peptide 6Add BLAST12
PeptideiPRO_000039355852 – 63Venom peptide 9Add BLAST12
PeptideiPRO_000039355952 – 62Venom peptide 5Add BLAST11
PropeptideiPRO_000039356064 – 82Add BLAST19
PeptideiPRO_000004506783 – 121C-type natriuretic peptide 39Add BLAST39
PeptideiPRO_000039356183 – 91Venom peptide 49
PeptideiPRO_000039356283 – 89Venom peptide 37
PeptideiPRO_000039356385 – 91Venom peptide 17
PeptideiPRO_000039356486 – 91Venom peptide 26

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki45 ↔ 46Alanine isoaspartyl cyclopeptide (Ala-Asn); in form venom peptide 10
Modified residuei84D-leucine; in forms ovCNP-39b, venom peptide 3 and venom peptide 42 Publications1

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

Gene expression databases

BgeeiENSOANG00000012322.

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

eggNOGiENOG410IZBQ. Eukaryota.
ENOG410YUR4. LUCA.

Family and domain databases

InterProiIPR002406. C_natriurtcpep.
IPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
[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

        10         20         30         40         50
MHLSHLLAWA LLLTLLSLRA EAKPPSPQPQ VPRSPGDEAS EAVAANGGGK
60 70 80 90 100
KGDKEPKGDR PRLLRELRLD TRSRGSRGVW TRLLHDHPNP RKYKPANKKG
110 120
LSKGCFGLKL DRIGSTSGLG C
Length:121
Mass (Da):13,148
Last modified:April 20, 2010 - v2
Checksum:i4DB01932ABB50B64
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti90P → N AA sequence (PubMed:19928958).Curated1

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:
EMBLi
GenBanki
DDBJi
Links Updated
AAPN01060770 Genomic DNA. No translation available.
AAPN01060771 Genomic DNA. No translation available.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AAPN01060770 Genomic DNA. No translation available.
AAPN01060771 Genomic DNA. No translation available.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9258.ENSOANP00000019499.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG410IZBQ. Eukaryota.
ENOG410YUR4. LUCA.

Gene expression databases

BgeeiENSOANG00000012322.

Family and domain databases

InterProiIPR002406. C_natriurtcpep.
IPR000663. Natr_peptide.
IPR030480. Natr_peptide_CS.
[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]
ProtoNetiSearch...

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: September 7, 2016
This is version 47 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
Annotation programAnimal Toxin Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.