UniProtKB/Swiss-Prot P15812: Variant p.Leu194Pro

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 194 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 Leucine (L) to Proline (P) at position 194 (L194P, p.Leu194Pro). 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: -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
Polymorphism: Six alleles of CD1E are known. CD1E*01 has His-102/Gln-106/Ser-149/Arg-164/Leu-194, CD1E*02 has His-102/Arg-106/Ser-149/Arg-164/Leu-194, CD1E*03 (9L) has His-102/Gln-106/Ser-149/Trp-164/Leu-194, CD1E*04 (15L) has His-102/Gln-106/Ser-149/Arg-164/Pro-194, CD1E*05 has Arg-102/Arg-106/Ser-149/Arg-164/Leu-194 and CD1E*06 has His-102/Arg-106/Asn-149/Arg-164/Leu-194 (PubMed:11019917, PubMed:12144626, PubMed:18325888). The sequence shown is that of allele CD1E*01. Additional information on the polymorphism described.
Variant description: In allele CD1E*04; impairs localization to late endosomal compartments and lipid antigen presentation. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs200741122 [ dbSNP | Ensembl ]

Sequence information

Variant position: 194 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 388 The length of the canonical sequence.
Location on the sequence: RYLDIKEILQSLLGHTCPRF L AGLMEAGESELKRKVKPEAW 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.
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 – 388	T-cell surface glycoprotein CD1e, membrane-associated
Chain	32 – 388	T-cell surface glycoprotein CD1e, soluble
Domain	191 – 301	Ig-like
Alternative sequence	20 – 208	Missing. In isoform 8, isoform 9, isoform 10, isoform 11 and isoform 12.
Alternative sequence	119 – 209	YPFEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTCPRFLAGLMEAGESELKRKV -> L. In isoform 5, isoform 6 and isoform 7.
Helix	176 – 201

Literature citations

Identification of two novel human CD1E alleles.
Mirones I.; Oteo M.; Parra-Cuadrado J.F.; Martinez-Naves E.;
Tissue Antigens 56:159-161(2000)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 120-208 (ALLELES CD1E*03 AND CD1E*04); POLYMORPHISM; VARIANTS TRP-164 AND PRO-194; A naturally occurring mutation in CD1e impairs lipid antigen presentation.
Tourne S.; Maitre B.; Collmann A.; Layre E.; Mariotti S.; Signorino-Gelo F.; Loch C.; Salamero J.; Gilleron M.; Angenieux C.; Cazenave J.P.; Mori L.; Hanau D.; Puzo G.; De Libero G.; de la Salle H.;
J. Immunol. 180:3642-3646(2008)
Cited for: POLYMORPHISM; VARIANT PRO-194;