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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02766: Variant p.Leu75Pro

Transthyretin
Gene: TTR
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Variant information Variant position: help 75 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Leucine (L) to Proline (P) at position 75 (L75P, p.Leu75Pro). 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: help 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: help -3 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
Variant description: help In AMYLD1; amyloid polyneuropathy. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 75 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 147 The length of the canonical sequence.
Location on the sequence: help KAADDTWEPFASGKTSESGE L HGLTTEEEFVEGIYKVEIDT 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         KAADDTWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDT

Chimpanzee                    KAADETWEPFASGKTSESGELHGLTTEEEFVEGIYKVEIDT

Mouse                         KTSEGSWEPFASGKTAESGELHGLTTDEKFVEGVYRVELDT

Rat                           KTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDT

Pig                           KAADGTWEPFALGKTSEFGELHGLTTDEKFVEGIYKVELDT

Bovine                        KAADETWEPFASGKTSESGELHGLTTEDKFVEGLYKVELDT

Rabbit                        KAADETWEPFASGKTSKTGELHGLTTSEKFVEGVYKVELDT

Sheep                         KAADETWEPFASGKTSDSGELHGLTTEDKFVEGLYKVELDT

Chicken                       KAADGTWQDFATGKTTEFGEIHELTTEEQFVEGVYRVEFDT

Xenopus laevis                QTESGKWEQITSGKTTELGEIHNLTTDEQFTEGVYKIEFAT

Xenopus tropicalis            NT-EGNWELISSGKTTELGEIHNIITDEQFTEGVYKIEFAT
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 21 – 147 Transthyretin
Binding site 74 – 74
Modified residue 62 – 62 4-carboxyglutamate; in a patient with Moyamoya disease
Modified residue 72 – 72 Phosphoserine
Beta strand 73 – 75



Literature citations
The crystal structure of amyloidogenic Leu55 --> Pro transthyretin variant reveals a possible pathway for transthyretin polymerization into amyloid fibrils.
Sebastiao M.P.; Saraiva M.J.; Damas A.M.;
J. Biol. Chem. 273:24715-24722(1998)
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 21-147 OF VARIANT AMYLD1 PRO-75; The binding of 2,4-dinitrophenol to wild-type and amyloidogenic transthyretin.
Morais-de-Sa E.; Neto-Silva R.M.; Pereira P.J.B.; Saraiva M.J.; Damas A.M.;
Acta Crystallogr. D 62:512-519(2006)
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF WILD-TYPE AND VARIANTS AMYLD1 PRO-75 AND PHE-98; Transthyretin Pro55, a variant associated with early-onset, aggressive, diffuse amyloidosis with cardiac and neurologic involvement.
Jacobson D.R.; McFarlin D.E.; Kane I.; Buxbaum J.N.;
Hum. Genet. 89:353-356(1992)
Cited for: VARIANT AMYLD1 PRO-75; Familial amyloid polyneuropathy in Taiwan: identification of transthyretin variant (Leu55-->Pro).
Yamamoto K.; Hsu S.P.; Yoshida K.; Ikeda S.; Nakazato M.; Shiomi K.; Cheng S.Y.; Furihata K.; Ueno I.; Yanagisawa N.;
Muscle Nerve 17:637-641(1994)
Cited for: VARIANT AMYLD1 PRO-75;
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.