| General information | | DisProt: | DP00747_C002 | | Name: | Atrial natriuretic factor | | Synonym(s): | ANF_HUMAN
ANF
Atrial natriuretic peptide
ANP
cleavage product 2 of Natriuretic peptides A (aa 124-151)
| | First appeared in release: | Release 6.02 (05/24/2013) | | UniProt: | P01160 | | UniGene: | Hs.75640 | | SwissProt: | ANF_HUMAN | | TrEMBL: | | | NCBI (GI): | | | Source organism: | Homo sapiens (Human) | | Sequence length: | 28 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
| | | | | |
SLRRSSCFGG RMDRIGAQSG LGCNSFRY
|
| Functional narrative |
Characterization of disorder is found on Atrial natriuretic factor which is cleavage product 2 of full-length Natriuretic peptides A (DP00747).
------------------------------------------------------------------------------------------------------------------
Hormone playing a key role in cardiovascular homeostasis through regulation of natriuresis, diuresis, and vasodilation. Also plays a role in female pregnancy by promoting trophoblast invasion and spiral artery remodeling in uterus. Specifically binds and stimulates the cGMP production of the NPR1 receptor. Binds the clearance receptor NPR3. Belongs to the natriuretic peptide family.
------------------------------------------------------------------------------------------------------------------
Copyright The UniProt Consortium, http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
------------------------------------------------------------------------------------------------------------------
|
| Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|
| Region 1 | | Type: | Disordered | | Name: | 'activity-conferring' loop | | Location: | 1 - 28 | | Length: | 28 | | Region sequence: |
SLRRSSCFGGRMDRIGAQSGLGCNSFRY | | Modification type: | Complex
Native
| | PDB: | 1ANP:A, 1YK0:E, 3N57:C | | Structural/functional type: | Function arises from the disordered state
| | Functional classes: | Molecular recognition effectors
Molecular assembly
| | Functional subclasses: | Intraprotein interaction
Protein-protein binding
| Detection methods:
- Nuclear magnetic resonance (NMR) (297 K; pH: 3.5; 90% H2O/ 10% D2O (or 99% D2O); ANP (PDB 1ANP) 1.3 mM)
- X-ray crystallography (293 K; pH: 7.5; NPR-C/ANP complex (PDB 1YK0); sodium citrate)
- X-ray crystallography (291 K; pH: 7; Dioxane (10%); Insulin-degrading enzyme/ANP complex (PDB 3N57); Na-HEPES 100 mM; PEGMME-5000 (13%); Tacsimate (10%))
| References:
- Fairbrother WJ, McDowell RS, Cunningham BC. "Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor." Biochemistry. 1994; 33(30): 8897-904. PubMed: 8043577
- Feller SM, Lewitzky M. "What is in a loop?" Cell Commun. Signal. 2012; 10(1): 31. PubMed: 23110718
- He XL, Dukkipati A, Garcia KC. "Structural determinants of natriuretic peptide receptor specificity and degeneracy." J. Mol. Biol.. 2006; 361(4): 698-714. PubMed: 16870210
- Ralat LA, Funke T, Ren M, Guo Q, Dickey DM, Potter LR, Tang W-J. "Crystal Structure of human Insulin-degrading enzyme (IDE) in complex with human atrial natriuretic peptide (ANP)." PDB Primary Citation. 2010.
| Comments:NMR structure 1ANP is from Fairbrother et al (1994), X-ray crystal structure 1YK0 is from He et al (2006), X-ray crystal structure 3N57 is from Ralat et al (2010).
Feller and Lewitzky (2012) discuss important loop formation via disulfide bond between C7 and C23.
|
| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
Disprot-footer
|
