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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O75503: Variant p.Asn143Ser

Bis(monoacylglycero)phosphate synthase CLN5
Gene: CLN5
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Variant information Variant position: help 143 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 Asparagine (N) to Serine (S) at position 143 (N143S, p.Asn143Ser). 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 Change from medium size and polar (N) to small size and polar (S) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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
Variant description: help In CLN5; loss of glycosylation; effectively transported to the lysosome; significant loss of bis(monoacylglycero)phosphate synthase activity; no alterations in secondary structure and thermal stability. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 143 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 358 The length of the canonical sequence.
Location on the sequence: help RSTLTGKNYTMEWYELFQLG N CTFPHLRPEMDAPFWCNQGA 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                         RSTLTGKNYTMEWYELFQLGNCTFPHL--RPEMDAPFWCNQGA

                              KSTLTGKNYTMEWYELFQLGNCTFPHL--RPEMNAPFWCNQ

Mouse                         RSTLTGKNYTIEWYELFQLGNCTFPHL--RPDKSAPFWCNQ

Bovine                        RSTLTEKNYTMEWYELFQLGNCTFPHL--RPEMNAPFWCNQ

Sheep                         RSTLTEKNYTMEWYELFQLGNCTFPHL--RPEMNAPFWCNQ

Slime mold                    YDLTTGLNYTAEYDAFFEVGNGTLPNIINVDGKDELLWCNA
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 1 – 358 Bis(monoacylglycero)phosphate synthase CLN5
Chain 44 – 358 Bis(monoacylglycero)phosphate synthase CLN5, secreted form
Topological domain 41 – 358 Lumenal
Glycosylation 130 – 130 N-linked (GlcNAc...) asparagine
Glycosylation 143 – 143 N-linked (GlcNAc...) asparagine
Disulfide bond 70 – 159
Disulfide bond 77 – 165
Mutagenesis 130 – 130 N -> Q. Loss of glycosylation. Retained in the endoplasmic reticulum rather than reaching the lysosome.
Mutagenesis 143 – 143 N -> Q. Loss of glycosylation. Effectively transported to the lysosome.



Literature citations
Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses.
Kousi M.; Lehesjoki A.E.; Mole S.E.;
Hum. Mutat. 33:42-63(2012)
Cited for: VARIANTS CLN5 HIS-63; TYR-77; SER-143; PRO-149; SER-156; ARG-158; SER-158; ASP-209 AND CYS-325; VARIANTS ARG-26 AND LYS-193; The role of N-glycosylation in folding, trafficking, and functionality of lysosomal protein CLN5.
Moharir A.; Peck S.H.; Budden T.; Lee S.Y.;
PLoS ONE 8:E74299-E74299(2013)
Cited for: CHARACTERIZATION OF VARIANTS CLN5 SER-143 AND ASN-230; GLYCOSYLATION AT ASN-130; ASN-143; ASN-178; ASN-203; ASN-255; ASN-271; ASN-281 AND ASN-352; MUTAGENESIS OF ASN-130; ASN-143; ASN-178; ASN-203; ASN-255; ASN-271; ASN-281 AND ASN-352; SUBCELLULAR LOCATION (SECRETED FORM); The Batten disease gene product CLN5 is the lysosomal bis(monoacylglycero)phosphate synthase.
Medoh U.N.; Hims A.; Chen J.Y.; Ghoochani A.; Nyame K.; Dong W.; Abu-Remaileh M.;
Science 381:1182-1189(2023)
Cited for: CHARACTERIZATION OF VARIANT CLN5 SER-143; FUNCTION; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; ACTIVITY REGULATION; SUBCELLULAR LOCATION; SUBUNIT; CIRCULAR DICHROISM; MUTAGENESIS OF CYS-231 AND 318-HIS-LYS-319; SUBSTRATE SPECIFICITY; ACTIVE SITE;
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.