UniProtKB/Swiss-Prot P16860: Variant p.Met93Leu

Natriuretic peptides B
Gene: NPPB
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Variant information Variant position:

93 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 Methionine (M) to Leucine (L) at position 93 (M93L, p.Met93Leu). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

2 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 rs5230 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

PTGVWKSREVATEGIRGHRK M VLYTLRAPRSPKMVQGSGCF 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                         PTGVWKSREVATEGIRGHRKMVLYTLRAPRSPKMVQGSGCF

                              PAEAPEAG-GTPRGVLAPHDSVLQALRRLRSPKMMHKSGCF

Mouse                         LTK------EHPKRVLRSQGSTLRVQQRPQNSKVTHISSCF

Rat                           PTK------ELLKRVLRSQDSAFRIQERLRNSKMAHSSSCF

Pig                           LTEAWEAREAAPTGVLGPRSSIFQVLRGIRSPKTMRDSGCF

Bovine                        LEETWDSPAAAPAGFLGPHHSILRALRG---PKMMRDSGCF

Sheep                         LEETWDSPAAAPAGFLGPHHSLLQALRG---PKMMRDSGCF

Cat                           PAESWEAQEEPPARVLAPHDNVLRALRRLGSSKMMRDSRCF

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	27 – 134	Natriuretic peptides B
Peptide	27 – 102	NT-proBNP
Peptide	29 – 134	proBNP(3-108)
Glycosylation	74 – 74	O-linked (HexNAc...) threonine
Glycosylation	79 – 79	O-linked (HexNAc...) serine
Glycosylation	84 – 84	O-linked (HexNAc...) threonine; Partial
Glycosylation	97 – 97	O-linked (HexNAc...) threonine
Mutagenesis	97 – 97	T -> A. Prevents O-glycosylation at this residue. Decreased extracellular levels of NPPB due to decreased stability after secretion whereas extracellular levels of brain natriuretic peptide 32 is increased. In HEK293 cells, proteolytic processing by CORIN or FURIN is reduced but in HL1 cells proteolytic processing is not affected.
Mutagenesis	99 – 99	R -> A. Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-102 and A-105.
Mutagenesis	102 – 102	R -> A. Loss of FURIN-mediated proteolytic processing in HEK293 cells, however processing in HL1 cells, likely mediated by CORIN, is only slightly reduced. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-105.
Mutagenesis	105 – 105	K -> A. No effect on proteolytic processing in HEK293 or HL1 cells. Loss of CORIN-mediated processing in HL1 cells; when associated with A-99 and A-102.

Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.

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.