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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02788: Variant p.Glu579Asp

Lactotransferrin
Gene: LTF
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Variant information Variant position: help 579 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Glutamate (E) to Aspartate (D) at position 579 (E579D, p.Glu579Asp). 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 acidic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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

Polymorphism: help The sequence shown corresponds to the reference genome sequence and is likely to represent the minor allele, whereas most publications refer to the longer sequence containing variant Arg-22 ins. Insertion of the additional arginine in variant Arg-22 ins creates an N-terminal basic cluster of four arginines, all of which appear to be important for the full functionality of the protein, including bactericidal and antifungal activities as well as binding to glycosaminoglycans, pspA, LPS, lysozyme and DNA. Additional information on the polymorphism described.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 579 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 710 The length of the canonical sequence.
Location on the sequence: help GDVAFVKDVTVLQNTDGNNN E AWAKDLKLADFALLCLDGKR 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                         GDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKR

Mouse                         GNVAFLKDSTVLQNTDGKNTEEWARNLKLKDFELLCLDDTR

Pig                           GDVAFVKDVTVLDNTNGQNTEEWARELRSDDFELLCLDGTR

Bovine                        GDVAFVKNDTVWENTNGESTADWAKNLNREDFRLLCLDGTR

Goat                          GDVAFVKNDTVWENTNGESSADWAKNLNREDFRLLCLDGTT

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 20 – 710 Lactotransferrin
Domain 364 – 695 Transferrin-like 2
Disulfide bond 424 – 705
Disulfide bond 446 – 668
Disulfide bond 502 – 696



Literature citations
cDNA cloning and sequence analysis of human lactoferrin.
Cheng H.; Chen X.Z.; Huan L.D.;
Sheng Wu Gong Cheng Xue Bao 17:385-387(2001)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579; Crystal structure of human seminal diferric lactoferrin at 3.4 Angstrom resolution.
Kumar J.; Weber W.; Munchau S.; Yadav S.; Singh S.B.; Saravanan K.; Paramasivam M.; Sharma S.; Kaur P.; Bhushan A.; Srinivasan A.; Betzel C.; Singh T.P.;
Indian J. Biochem. Biophys. 40:14-21(2003)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 22-710 IN COMPLEX WITH IRON AND CARBONATE; FUNCTION; VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579; Submission
Shi Y.-Q.; Zhang Y.; Zheng Y.-M.;
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS ARG-22 INS; THR-29; ARG-47 AND ASP-579; Submission
McCombie W.R.; Wilson R.; Chen E.; Gibbs R.; Zuo L.; Johnson D.; Nhan M.; Parnell L.; Dedhia N.; Ansari A.; Mardis E.; Schutz K.; Gnoj L.; la Bastide M.; Kaplan N.; Greco T.; Touchman J.; Muzny D.; Chen C.N.; Evans C.; Fitzgerald M.; See L.H.; Tang M.; Porcel B.M.; Dragan Y.; Giacalone J.; Pae A.; Powell E.; Solinsky K.A.; Desilva U.; Diaz-Perez S.; Zhou X.; Yu Y.; Watanabe M.; Doggett N.; Garcia D.; Sagripanti J.L.;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 236-710; VARIANT ASP-579; The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin.
Thomassen E.A.; van Veen H.A.; van Berkel P.H.; Nuijens J.H.; Abrahams J.P.;
Transgenic Res. 14:397-405(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 20-710 IN COMPLEX WITH IRON AND CARBONATE; GLYCOSYLATION AT ASN-156 AND ASN-497; VARIANT ASP-579;
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.