P17342 (ANPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Atrial natriuretic peptide receptor 3

Alternative name(s):
Atrial natriuretic peptide clearance receptor
Atrial natriuretic peptide receptor type C
Short name=ANP-C
Short name=ANPR-C
Short name=NPR-C

Gene names

Name:	NPR3
Synonyms:	ANPRC, C5orf23, NPRC

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	541 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	Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity.
Subunit structure	Homodimer; disulfide-linked. Dimers can also be formed through the C-terminal cysteine of isoform 2. Ref.8 Ref.10 Ref.11
Subcellular location	Membrane; Single-pass type I membrane protein.
Miscellaneous	Has low affinity for peptide hormones in the absence of bound chloride.
Sequence similarities	Belongs to the ANF receptor family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Alternative splicing
Domain	Signal Transmembrane Transmembrane helix
Ligand	Chloride
Molecular function	Receptor
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	adenylate cyclase-inhibiting G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of adenylate cyclase activity Inferred from electronic annotation. Source: Compara osteoclast proliferation Inferred from sequence or structural similarity. Source: UniProtKB phospholipase C-activating G-protein coupled receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of nitric-oxide synthase activity Inferred from sequence or structural similarity. Source: BHF-UCL positive regulation of urine volume Inferred from sequence or structural similarity. Source: UniProtKB regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB regulation of osteoblast proliferation Inferred from sequence or structural similarity. Source: UniProtKB skeletal system development Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	integral to plasma membrane Inferred by curator Ref.9. Source: BHF-UCL
Molecular_function	G-protein coupled peptide receptor activity Inferred from sequence or structural similarity. Source: BHF-UCL natriuretic peptide receptor activity Inferred from direct assay Ref.9. Source: UniProtKB peptide hormone binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P17342-1)

Also known as: NPR-C5;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P17342-2)

Also known as: NPR-C6;

The sequence of this isoform differs from the canonical sequence as follows:
     476-477: SG → C

Isoform 3 (identifier: P17342-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-40: MPSLLVLTFS...GGGGGAGIGG → MEPSALGPWS...FRRECGQNEK
     41-256: Missing.
     476-477: SG → C

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 26

26

Potential

Chain

27 – 541

515

Atrial natriuretic peptide receptor 3

PRO_0000012370

Regions

Topological domain

27 – 481

455

Extracellular Potential

Transmembrane

482 – 504

23

Helical; Potential

Topological domain

505 – 541

37

Cytoplasmic Potential

Sites

Binding site

106

1

Chloride

Binding site

135

1

Chloride; via amide nitrogen

Binding site

136

1

Chloride; via amide nitrogen

Amino acid modifications

Glycosylation

86

1

N-linked (GlcNAc...) (complex) Ref.8 Ref.11

Glycosylation

293

1

N-linked (GlcNAc...) (high mannose) Ref.8 Ref.10 Ref.11

Glycosylation

394

1

N-linked (GlcNAc...) (complex) Ref.8 Ref.10 Ref.11

Disulfide bond

108 ↔ 136

Ref.8 Ref.10 Ref.11

Disulfide bond

213 ↔ 261

Ref.8 Ref.10 Ref.11

Disulfide bond

473

Interchain Ref.8 Ref.10 Ref.11

Natural variations

Alternative sequence

1 – 40

40

MPSLL…AGIGG → MEPSALGPWSLFPDLAPRDQ EGQVLAPRRCFRRECGQNEK in isoform 3.

VSP_045901

Alternative sequence

41 – 256

216

Missing in isoform 3.

VSP_045902

Alternative sequence

476 – 477

2

SG → C in isoform 2 and isoform 3.

VSP_001812

Experimental info

Sequence conflict

522

1

N → D in BAG61896. Ref.4

Secondary structure

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541

Helix Strand Turn

Details...

Beta strand

52 – 59

8

Helix

69 – 83

15

Beta strand

98 – 105

8

Helix

111 – 122

12

Turn

123 – 125

3

Beta strand

129 – 132

4

Helix

137 – 150

14

Beta strand

154 – 157

4

Helix

162 – 165

4

Turn

167 – 173

7

Beta strand

174 – 176

3

Helix

181 – 195

15

Beta strand

199 – 205

7

Beta strand

208 – 210

3

Helix

212 – 227

16

Beta strand

230 – 236

7

Beta strand

238 – 240

3

Helix

244 – 254

11

Beta strand

256 – 262

7

Helix

264 – 276

13

Turn

280 – 283

4

Beta strand

285 – 289

5

Helix

291 – 293

3

Turn

297 – 299

3

Helix

309 – 315

7

Helix

316 – 318

3

Beta strand

319 – 324

6

Helix

330 – 344

15

Turn

345 – 347

3

Helix

356 – 377

22

Helix

385 – 392

8

Beta strand

393 – 399

7

Beta strand

402 – 406

5

Beta strand

410 – 412

3

Beta strand

415 – 423

9

Turn

424 – 427

4

Beta strand

428 – 436

9

Turn

437 – 440

4

Beta strand

441 – 444

4

Beta strand

451 – 453

3

Helix

454 – 456

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (NPR-C5) [UniParc]. Last modified January 10, 2003. Version 2. Checksum: 8A66415F7F7D62B7	FASTA	541	59,808
	10 20 30 40 50 60 MPSLLVLTFS PCVLLGWALL AGGTGGGGVG GGGGGAGIGG GRQEREALPP QKIEVLVLLP 70 80 90 100 110 120 QDDSYLFSLT RVRPAIEYAL RSVEGNGTGR RLLPPGTRFQ VAYEDSDCGN RALFSLVDRV 130 140 150 160 170 180 AAARGAKPDL ILGPVCEYAA APVARLASHW DLPMLSAGAL AAGFQHKDSE YSHLTRVAPA 190 200 210 220 230 240 YAKMGEMMLA LFRHHHWSRA ALVYSDDKLE RNCYFTLEGV HEVFQEEGLH TSIYSFDETK 250 260 270 280 290 300 DLDLEDIVRN IQASERVVIM CASSDTIRSI MLVAHRHGMT SGDYAFFNIE LFNSSSYGDG 310 320 330 340 350 360 SWKRGDKHDF EAKQAYSSLQ TVTLLRTVKP EFEKFSMEVK SSVEKQGLNM EDYVNMFVEG 370 380 390 400 410 420 FHDAILLYVL ALHEVLRAGY SKKDGGKIIQ QTWNRTFEGI AGQVSIDANG DRYGDFSVIA 430 440 450 460 470 480 MTDVEAGTQE VIGDYFGKEG RFEMRPNVKY PWGPLKLRID ENRIVEHTNS SPCKSSGGLE 490 500 510 520 530 540 ESAVTGIVVG ALLGAGLLMA FYFFRKKYRI TIERRTQQEE SNLGKHRELR EDSIRSHFSV A
	Isoform 2 (NPR-C6) [UniParc]. Checksum: 53EE0020A296D6F5	FASTA	540	59,767
	10 20 30 40 50 60 MPSLLVLTFS PCVLLGWALL AGGTGGGGVG GGGGGAGIGG GRQEREALPP QKIEVLVLLP 70 80 90 100 110 120 QDDSYLFSLT RVRPAIEYAL RSVEGNGTGR RLLPPGTRFQ VAYEDSDCGN RALFSLVDRV 130 140 150 160 170 180 AAARGAKPDL ILGPVCEYAA APVARLASHW DLPMLSAGAL AAGFQHKDSE YSHLTRVAPA 190 200 210 220 230 240 YAKMGEMMLA LFRHHHWSRA ALVYSDDKLE RNCYFTLEGV HEVFQEEGLH TSIYSFDETK 250 260 270 280 290 300 DLDLEDIVRN IQASERVVIM CASSDTIRSI MLVAHRHGMT SGDYAFFNIE LFNSSSYGDG 310 320 330 340 350 360 SWKRGDKHDF EAKQAYSSLQ TVTLLRTVKP EFEKFSMEVK SSVEKQGLNM EDYVNMFVEG 370 380 390 400 410 420 FHDAILLYVL ALHEVLRAGY SKKDGGKIIQ QTWNRTFEGI AGQVSIDANG DRYGDFSVIA 430 440 450 460 470 480 MTDVEAGTQE VIGDYFGKEG RFEMRPNVKY PWGPLKLRID ENRIVEHTNS SPCKSCGLEE 490 500 510 520 530 540 SAVTGIVVGA LLGAGLLMAF YFFRKKYRIT IERRTQQEES NLGKHRELRE DSIRSHFSVA
	Isoform 3 [UniParc]. Checksum: C38DFF9C771B1A8B	FASTA	324	36,656
	10 20 30 40 50 60 MEPSALGPWS LFPDLAPRDQ EGQVLAPRRC FRRECGQNEK VVIMCASSDT IRSIMLVAHR 70 80 90 100 110 120 HGMTSGDYAF FNIELFNSSS YGDGSWKRGD KHDFEAKQAY SSLQTVTLLR TVKPEFEKFS 130 140 150 160 170 180 MEVKSSVEKQ GLNMEDYVNM FVEGFHDAIL LYVLALHEVL RAGYSKKDGG KIIQQTWNRT 190 200 210 220 230 240 FEGIAGQVSI DANGDRYGDF SVIAMTDVEA GTQEVIGDYF GKEGRFEMRP NVKYPWGPLK 250 260 270 280 290 300 LRIDENRIVE HTNSSPCKSC GLEESAVTGI VVGALLGAGL LMAFYFFRKK YRITIERRTQ 310 320 QEESNLGKHR ELREDSIRSH FSVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA sequence of the human atrial natriuretic peptide clearance receptor." Lowe D.G., Camerato T.R., Goeddel D.V. Nucleic Acids Res. 18:3412-3412(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Kidney.
[2]	"Isolation and functional expression of the human atrial natriuretic peptide clearance receptor cDNA." Porter J.G., Arfsten A., Fuller F., Miller J.A., Gregory L.C., Lewicki J.A. Biochem. Biophys. Res. Commun. 171:796-803(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]	"Human lens epithelial mRNA for atrial natriuretic peptide clearance receptor." Rae J.L., Shepard A.R. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Lens epithelium.
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Pericardium.
[5]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] (ISOFORM 1).
[8]	"The disulfide linkages and glycosylation sites of the human natriuretic peptide receptor-C homodimer." Stults J.T., O'Connell K.L., Garcia C., Wong S., Engel A.M., Garbers D.L., Lowe D.G. Biochemistry 33:11372-11381(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE (ISOFORMS 1 AND 2), DISULFIDE BONDS, GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394, STRUCTURE OF CARBOHYDRATES.
[9]	"Extracellular domain-IgG fusion proteins for three human natriuretic peptide receptors. Hormone pharmacology and application to solid phase screening of synthetic peptide antisera." Bennett B.D., Bennett G.L., Vitangcol R.V., Jewett J.R., Burnier J., Henzel W., Lowe D.G. J. Biol. Chem. 266:23060-23067(1991) [PubMed] [Europe PMC] [Abstract] Cited for: LIGAND-BINDING.
[10]	"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 44-485 IN COMPLEX WITH NATRIURETIC PEPTIDE, GLYCOSYLATION AT ASN-293 AND ASN-394, DISULFIDE BONDS, SUBUNIT.
[11]	"Structural determinants of natriuretic peptide receptor specificity and degeneracy." He X.-L., Dukkipati A., Garcia K.C. J. Mol. Biol. 361:698-714(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-480 IN COMPLEX WITH NATRIURETIC PEPTIDE AND CHLORIDE IONS, GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394, DISULFIDE BONDS.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X52282 mRNA. Translation: CAA36523.1.
M59305 mRNA. Translation: AAA51734.1.
AF025998 mRNA. Translation: AAB88801.1.
AK300094 mRNA. Translation: BAG61896.1.
AC008766 Genomic DNA. No translation available.
AC026703 Genomic DNA. No translation available.
CH471118 Genomic DNA. Translation: EAX10799.1.
BC131540 mRNA. Translation: AAI31541.1.

IPI

IPI00013826.
IPI00215700.
IPI00878409.

PIR

OYHUCR. S10150.

RefSeq

NP_000899.1. NM_000908.3.
NP_001191304.1. NM_001204375.1.
NP_001191305.1. NM_001204376.1.

UniGene

Hs.13528.
Hs.619466.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JDN	X-ray	2.90	A	44-475	[»]
1JDP	X-ray	2.00	A/B	44-475	[»]
1YK0	X-ray	2.40	A/B	1-480	[»]
1YK1	X-ray	2.90	A/B	2-480	[»]

ProteinModelPortal

P17342.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000398028.

PTM databases

PhosphoSite

P17342.

Polymorphism databases

DMDM

27735161.

Proteomic databases

PaxDb

P17342.

PRIDE

P17342.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000265074; ENSP00000265074; ENSG00000113389.
ENST00000415167; ENSP00000398028; ENSG00000113389.
ENST00000415685; ENSP00000402490; ENSG00000113389.

GeneID

4883.

KEGG

hsa:4883.

UCSC

uc003jhv.3. human.

Organism-specific databases

CTD

4883.

GeneCards

GC05P032747.

HGNC

HGNC:7945. NPR3.

HPA

HPA031065.

MIM

108962. gene.

neXtProt

NX_P17342.

PharmGKB

PA31737.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG255055.

HOGENOM

HOG000236252.

HOVERGEN

HBG060145.

InParanoid

P17342.

KO

K12325.

OMA

FQVAYED.

OrthoDB

EOG4933HW.

PhylomeDB

P17342.

Gene expression databases

ArrayExpress

P17342.

Bgee

P17342.

CleanEx

HS_NPR3.

Genevestigator

P17342.

GermOnline

ENSG00000113389. Homo sapiens.

Family and domain databases

InterPro

IPR001828. ANF_lig-bd_rcpt.
IPR001170. Ntpep_rcpt.
[Graphical view]

Pfam

PF01094. ANF_receptor. 1 hit.
[Graphical view]

PRINTS

PR00255. NATPEPTIDER.

PROSITE

PS00458. ANF_RECEPTORS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P17342.

ChEMBL

CHEMBL2247.

DrugBank

DB04899. Nesiritide.

EvolutionaryTrace

P17342.

GenomeRNAi

4883.

NextBio

18796.

SOURCE

Search...

Entry information

Entry name

ANPRC_HUMAN

Accession

Primary (citable) accession number: P17342
Secondary accession number(s): A2RRD1, B4DT84, E7EPG9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	January 10, 2003
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 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.