P23582 (ANFC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	126 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	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 process	Osteogenesis
Cellular component	Secreted
Coding sequence diversity	Polymorphism
Domain	Signal
Molecular function	Hormone Vasoactive
PTM	Cleavage on pair of basic residues Disulfide bond
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cGMP 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: Compara negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara ossification Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of cGMP biosynthetic process Inferred from electronic annotation. Source: Compara positive regulation of osteoblast differentiation Inferred from electronic annotation. Source: Compara positive regulation of vasodilation Inferred from electronic annotation. Source: Compara post-embryonic development Inferred from electronic annotation. Source: Compara receptor guanylyl cyclase signaling pathway Inferred from direct assay Ref.6. Source: UniProtKB regulation of blood pressure Non-traceable author statement. Source: UniProtKB regulation of blood vessel size Inferred from electronic annotation. Source: UniProtKB-KW regulation of multicellular organism growth Inferred from electronic annotation. Source: Compara regulation of smooth muscle cell proliferation Inferred from electronic annotation. Source: Compara regulation of vasoconstriction Non-traceable author statement. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Compara response to ethanol Inferred from electronic annotation. Source: Compara response to hypoxia Inferred from electronic annotation. Source: Compara
Cellular_component	extracellular region Non-traceable author statement. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Potential

Propeptide

24 – 73

50

PRO_0000001553

Peptide

74 – 126

53

CNP-53

PRO_0000001554

Peptide

98 – 126

29

CNP-29 Ref.5

PRO_0000001555

Peptide

105 – 126

22

CNP-22

PRO_0000001556

Amino acid modifications

Disulfide bond

110 ↔ 126

Ref.7

Natural variations

Natural variant

82

1

R → Q.
Corresponds to variant rs5267 [ dbSNP | Ensembl ].

VAR_014583

Secondary structure

1

.

.

.

126

Helix Strand Turn

Details...

Turn

116 – 117

2

Sequences

	Sequence		Length	Mass (Da)
	P23582 [UniParc]. Last modified November 1, 1991. Version 1. Checksum: 58F6E657868F9A2D	FASTA	126	13,246
	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

References

	« Hide 'large scale' referencesShow '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. , 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.

IPI

IPI00012075.

PIR

AWHUC. JT0567.

RefSeq

NP_077720.1. NM_024409.2.

UniGene

Hs.247916.
Hs.627236.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JDP	X-ray	2.00	H	105-126	[»]

ProteinModelPortal

P23582.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000295440.

Protein family/group databases

TCDB

1.C.46.1.1. C-type natriuretic peptide (CNP) family.

Polymorphism databases

DMDM

113850.

Proteomic databases

PaxDb

P23582.

PRIDE

P23582.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000295440; ENSP00000295440; ENSG00000163273.
ENST00000409852; ENSP00000387159; ENSG00000163273.

GeneID

4880.

KEGG

hsa:4880.

UCSC

uc002vsl.2. human.

Organism-specific databases

CTD

4880.

GeneCards

GC02M232786.

HGNC

HGNC:7941. NPPC.

HPA

HPA035362.

MIM

600296. gene.

neXtProt

NX_P23582.

PharmGKB

PA31735.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG43160.

HOGENOM

HOG000010304.

HOVERGEN

HBG004229.

InParanoid

P23582.

KO

K12336.

OMA

HKMDRIG.

OrthoDB

EOG4RFKV7.

PhylomeDB

P23582.

Gene expression databases

ArrayExpress

P23582.

Bgee

P23582.

CleanEx

HS_NPPC.

Genevestigator

P23582.

GermOnline

ENSG00000163273. Homo sapiens.

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...

Other

EvolutionaryTrace

P23582.

GenomeRNAi

4880.

NextBio

18784.

PMAP-CutDB

P23582.

SOURCE

Search...

Entry information

Entry name

ANFC_HUMAN

Accession

Primary (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 3, 2013
This is version 117 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.