UniProtKB/Swiss-Prot P02724: Variant p.Ala84Pro

Glycophorin-A
Gene: GYPA
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Variant information Variant position:

84 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 Alanine (A) to Proline (P) at position 84 (A84P, p.Ala84Pro). 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 small size and hydrophobic (A) to medium size and hydrophobic (P) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-1 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
Polymorphism:

Along with GYPB, GYPA is responsible for the MNS blood group system [MIM:111300]. The molecular basis of the GPA M/N bloodgroup antigen is a variation at positions 20 and 24. Ser-20 and Gly-24 correspond to M (shown); 'Leu-20' and 'Glu-24' correspond to N.GYPA polymorphisms are involved in resistance to malaria [MIM:611162]. - Additional information on the polymorphism described.
Variant description:

In ENEP/HAG antigen. Any additional useful information about the variant.

Sequence information Variant position:

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

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

EISVRTVYPPEEETGERVQL A HHFSEPEITLIIFGVMAGVI 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                         EISVRTVY---PPEEET-GERVQLAHHFSEPEITLIIFGVMAGVI

                              SGTMYQHL---PDGGQK--ARQQLVHIFSEPVIIGIIYAVM

Chimpanzee                    EIYVTTVY---PPEEEN-GEGVQLVHRFSEPEITLIIFGVM

Mouse                         PTEVSAAFEEQPVSPHIGGMPSPIQHDFPALVMILIILGVM

Pig                           VMTIKNTT---AVVQKETGVPESYHQDFSHAEITGIIFAVM

Horse                         ------------------GDGLQLAHDFSQPVITVIILGVM

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	20 – 150	Glycophorin-A
Topological domain	20 – 91	Extracellular
Glycosylation	66 – 66	O-linked (GalNAc...) serine
Glycosylation	69 – 69	O-linked (GalNAc...) threonine
Mutagenesis	87 – 87	F -> C. Diminishes dimerization.
Mutagenesis	88 – 88	S -> C. Diminishes dimerization.
Mutagenesis	90 – 90	P -> C. Diminishes dimerization.
Mutagenesis	91 – 91	E -> C. Diminishes dimerization.
Mutagenesis	94 – 94	L -> I. Diminishes dimerization.
Mutagenesis	95 – 95	I -> A. Diminishes dimerization.
Mutagenesis	98 – 98	G -> L. Diminishes dimerization.
Mutagenesis	102 – 102	G -> L. Abolishes dimerization.
Beta strand	84 – 86

Literature citations
Glycophorin A mutation Ala65 --> Pro gives rise to a novel pair of MNS alleles ENEP (MNS39) and HAG (MNS41) and altered Wrb expression: direct evidence for GPA/band 3 interaction necessary for normal Wrb expression.
Poole J.; Banks J.; Bruce L.J.; Ring S.M.; Levene C.; Stern H.; Overbeeke M.A.; Tanner M.J.;
Transfus. Med. 9:167-174(1999)
Cited for: VARIANT ENEP/HAG PRO-84;

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.