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P23582 (ANFC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-type natriuretic peptide

Cleaved into the following 3 chains:

  1. CNP-22
  2. CNP-29
  3. CNP-53
Gene names
Name:NPPC
Synonyms:CNP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length126 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hormone which plays a role in endochondral ossification through regulation of cartilaginous growth plate chondrocytes proliferation and differentiation. May also be vasoactive and natriuretic. Specifically binds and stimulates the cGMP production of the NPR2 receptor. Binds the clearance receptor NPR3 By similarity. Ref.6

Subcellular location

Secreted.

Sequence similarities

Belongs to the natriuretic peptide family.

Ontologies

Keywords
   Biological processOsteogenesis
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionHormone
Vasoactive
   PTMCleavage on pair of basic residues
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcGMP biosynthetic process

Inferred from direct assay Ref.6. Source: UniProtKB

growth plate cartilage chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

growth plate cartilage chondrocyte proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of DNA metabolic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of cGMP biosynthetic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of osteoblast differentiation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vasodilation

Inferred from electronic annotation. Source: Ensembl

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

receptor guanylyl cyclase signaling pathway

Inferred from direct assay Ref.6. Source: UniProtKB

regulation of blood vessel size

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: Ensembl

secretory granule

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionreceptor binding

Inferred from physical interaction PubMed 1660465Ref.6. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Propeptide24 – 7350
PRO_0000001553
Peptide74 – 12653CNP-53
PRO_0000001554
Peptide98 – 12629CNP-29 Ref.5
PRO_0000001555
Peptide105 – 12622CNP-22
PRO_0000001556

Amino acid modifications

Disulfide bond110 ↔ 126 Ref.7

Natural variations

Natural variant821R → Q.
Corresponds to variant rs5267 [ dbSNP | Ensembl ].
VAR_014583

Secondary structure

... 126
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P23582 [UniParc].

Last modified November 1, 1991. Version 1.
Checksum: 58F6E657868F9A2D

FASTA12613,246
        10         20         30         40         50         60 
MHLSQLLACA LLLTLLSLRP SEAKPGAPPK VPRTPPAEEL AEPQAAGGGQ KKGDKAPGGG 

        70         80         90        100        110        120 
GANLKGDRSR LLRDLRVDTK SRAAWARLLQ EHPNARKYKG ANKKGLSKGC FGLKLDRIGS 


MSGLGC 

« Hide

References

« Hide 'large scale' references
[1]"Gene and precursor structures of human C-type natriuretic peptide."
Tawaragi Y., Fuchimura K., Tanaka S., Minamino N., Kangawa K., Matsuo H.
Biochem. Biophys. Res. Commun. 175:645-651(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Human C-type natriuretic peptide. Characterization of the gene and peptide."
Ogawa Y., Nakao K., Nakagawa O., Komatsu Y., Hosoda K., Suga S., Arai H., Nagata K., Yoshida N., Imura H.
Hypertension 19:809-813(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Isolation and identification of C-type natriuretic peptide in human monocytic cell line, THP-1."
Ishizaka Y., Kangawa K., Minamino N., Ishii K., Takano S., Eto T., Matsuo H.
Biochem. Biophys. Res. Commun. 189:697-704(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 98-126.
[6]"Selective activation of the B natriuretic peptide receptor by C-type natriuretic peptide (CNP)."
Koller K.J., Lowe D.G., Bennett G.L., Minamino N., Kangawa K., Matsuo H., Goeddel D.V.
Science 252:120-123(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone."
He X.-L., Chow D.-C., Martick M.M., Garcia K.C.
Science 293:1657-1662(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-126 IN COMPLEX WITH NPR3, DISULFIDE BOND.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64710 Genomic DNA. Translation: AAA35703.1.
D90337 Genomic DNA. Translation: BAA14351.1.
AC013435 Genomic DNA. Translation: AAX88912.1.
BC069120 mRNA. Translation: AAH69120.1.
BC105065 mRNA. Translation: AAI05066.1.
BC105067 mRNA. Translation: AAI05068.1.
PIRAWHUC. JT0567.
RefSeqNP_077720.1. NM_024409.2.
UniGeneHs.247916.
Hs.627236.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JDPX-ray2.00H105-126[»]
ProteinModelPortalP23582.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110940. 3 interactions.
STRING9606.ENSP00000295440.

Protein family/group databases

TCDB1.C.46.1.1. the c-type natriuretic peptide (cnp) family.

Polymorphism databases

DMDM113850.

Proteomic databases

PaxDbP23582.
PRIDEP23582.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295440; ENSP00000295440; ENSG00000163273.
ENST00000409852; ENSP00000387159; ENSG00000163273.
GeneID4880.
KEGGhsa:4880.
UCSCuc002vsl.2. human.

Organism-specific databases

CTD4880.
GeneCardsGC02M232786.
HGNCHGNC:7941. NPPC.
HPAHPA035362.
MIM600296. gene.
neXtProtNX_P23582.
PharmGKBPA31735.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG43160.
HOGENOMHOG000010304.
HOVERGENHBG004229.
InParanoidP23582.
KOK12336.
OMAHKMDRIG.
OrthoDBEOG79CZ1S.
PhylomeDBP23582.
TreeFamTF106305.

Gene expression databases

ArrayExpressP23582.
BgeeP23582.
CleanExHS_NPPC.
GenevestigatorP23582.

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...

Other

EvolutionaryTraceP23582.
GenomeRNAi4880.
NextBio18784.
PMAP-CutDBP23582.
PROP23582.
SOURCESearch...

Entry information

Entry nameANFC_HUMAN
AccessionPrimary (citable) accession number: P23582
Secondary accession number(s): Q4ZG41
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: April 16, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM