Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q12884: Variant p.Ser363Leu

Prolyl endopeptidase FAP
Gene: FAP
Feedback?
Variant information Variant position: help 363 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 Serine (S) to Leucine (L) at position 363 (S363L, p.Ser363Leu). 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 small size and polar (S) to medium size and hydrophobic (L) 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

Variant description: help Decreased plasma membrane expression; loss of homodimerization and dipeptidyl peptidase activity; mislocalized with the calnexin in the endoplasmic reticulum; causes induction of the unfolded protein response (UPR). Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 363 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 760 The length of the canonical sequence.
Location on the sequence: help RTGWAGGFFVSTPVFSYDAI S YYKIFSDKDGYKHIHYIKDT 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                         RTGWAGGFFVSTPVFSYDAISYYKIFSDKDGYKHIHYIKDT

Mouse                         RTGWAGGFFVSTPAFSQDATSYYKIFSDKDGYKHIHYIKDT

Bovine                        RTGWAGGFFVSTPVFSHDTISYYKIFSDKDGYKHIHYIRDT

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 – 760 Prolyl endopeptidase FAP
Chain 24 – 760 Antiplasmin-cleaving enzyme FAP, soluble form
Topological domain 26 – 760 Extracellular
Alternative sequence 1 – 521 Missing. In isoform 2.



Literature citations
Quantitation of fibroblast activation protein (FAP)-specific protease activity in mouse, baboon and human fluids and organs.
Keane F.M.; Yao T.W.; Seelk S.; Gall M.G.; Chowdhury S.; Poplawski S.E.; Lai J.H.; Li Y.; Wu W.; Farrell P.; Vieira de Ribeiro A.J.; Osborne B.; Yu D.M.; Seth D.; Rahman K.; Haber P.; Topaloglu A.K.; Wang C.; Thomson S.; Hennessy A.; Prins J.; Twigg S.M.; McLennan S.V.; McCaughan G.W.; Bachovchin W.W.; Gorrell M.D.;
FEBS Open Bio 4:43-54(2013)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; TISSUE SPECIFICITY; CHARACTERIZATION OF VARIANT LEU-363; A rare variant in human fibroblast activation protein associated with ER stress, loss of enzymatic function and loss of cell surface localisation.
Osborne B.; Yao T.W.; Wang X.M.; Chen Y.; Kotan L.D.; Nadvi N.A.; Herdem M.; McCaughan G.W.; Allen J.D.; Yu D.M.; Topaloglu A.K.; Gorrell M.D.;
Biochim. Biophys. Acta 1844:1248-1259(2014)
Cited for: FUNCTION; CATALYTIC ACTIVITY; SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT LEU-363;
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.