UniProtKB/Swiss-Prot Q9Y5Q5: Variant p.His525Arg

Atrial natriuretic peptide-converting enzyme
Gene: CORIN
Feedback?

Variant information Variant position:

525 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Histidine (H) to Arginine (R) at position 525 (H525R, p.His525Arg). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from medium size and polar (H) to large size and basic (R) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs11934749 [ dbSNP | Ensembl ]

Sequence information Variant position:

525 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

1042 The length of the canonical sequence.
Location on the sequence:

YLMFFSCTILVPKCDVNTGE H IPPCRALCEHSKERCESVLG The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         YLMFFSCTILVPKCDVNTGEHIPPCRALCEHSKERCESVLG

Mouse                         YLMFFACTILVPKCDVNTGQRIPPCRLLCEHSKERCESVLG

Rat                           YLMFFACTILVPKCDVNTGQRVPPCRLLCEHSKERCESVLG

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 1042	Atrial natriuretic peptide-converting enzyme
Chain	1 – 801	Atrial natriuretic peptide-converting enzyme, N-terminal propeptide
Chain	165 – 801	Atrial natriuretic peptide-converting enzyme, 160 kDa soluble fragment
Chain	428 – 801	Atrial natriuretic peptide-converting enzyme, 100 kDa soluble fragment
Topological domain	67 – 1042	Extracellular
Domain	450 – 573	FZ 2
Disulfide bond	502 – 540

Literature citations
Corin, a mosaic transmembrane serine protease encoded by a novel cDNA from human heart.
Yan W.; Sheng N.; Seto M.; Morser J.; Wu Q.;
J. Biol. Chem. 274:14926-14935(1999)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); TISSUE SPECIFICITY; VARIANTS TYR-13 AND ARG-525; 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)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1); VARIANTS TYR-13 AND ARG-525; An integrated genetic and functional analysis of the role of type II transmembrane serine proteases (TMPRSSs) in hearing loss.
Guipponi M.; Toh M.-Y.; Tan J.; Park D.; Hanson K.; Ballana E.; Kwong D.; Cannon P.Z.F.; Wu Q.; Gout A.; Delorenzi M.; Speed T.P.; Smith R.J.H.; Dahl H.-H.M.; Petersen M.; Teasdale R.D.; Estivill X.; Park W.J.; Scott H.S.;
Hum. Mutat. 29:130-141(2008)
Cited for: VARIANT ARG-525;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.