Variant position: 37 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 353 The length of the canonical sequence.
Location on the sequence:
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 RQRVCTLFIIGFKFTFFVSI MIYWHVVGEPKEKGQLYNLPA
Chimpanzee RQRVCTLFIIGFKFTFFVSI MIYWHVVGEPKEKGQLYNLPA
Mouse RQRVFTFFIISFKFMFLISI LIYWHTVGAPKDQRE-YSLPV
Rat RQRVFTLFIISFKFTFLVSI LIYWHTVGAPKDQRRQYSLPV
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
1 – 353 Lactosylceramide 4-alpha-galactosyltransferase
23 – 43 Helical; Signal-anchor for type II membrane protein
Cloning and expression of the histo-blood group Pk UDP-galactose:Galbeta1-4Glcbeta1-Cer alpha1,4-galactosyltransferase. Molecular genetic basis of the p phenotype.
Steffensen R.; Carlier K.; Wiels J.; Levery S.B.; Stroud M.; Cedergren B.; Nilsson Sojka B.; Bennett E.P.; Jersild C.; Clausen H.;
J. Biol. Chem. 275:16723-16729(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA]; FUNCTION; VARIANTS VAL-37 AND LYS-183;
SeattleSNPs variation discovery resource;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS VAL-37 AND ARG-163;
Molecular basis for the p phenotype. Identification of distinct and multiple mutations in the alpha 1,4-galactosyltransferase gene in Swedish and Japanese individuals.
Furukawa K.; Iwamura K.; Uchikawa M.; Sojka B.N.; Wiels J.; Okajima T.; Urano T.; Furukawa K.;
J. Biol. Chem. 275:37752-37756(2000)
Cited for: VARIANTS VAL-37; LYS-183; ASP-187 AND LEU-251; POLYMORPHISM;
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.