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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9BXJ0: Variant p.Ser163Arg

Complement C1q tumor necrosis factor-related protein 5
Gene: C1QTNF5
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Variant information Variant position: help 163 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 Serine (S) to Arginine (R) at position 163 (S163R, p.Ser163Arg). 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 large size and basic (R) 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 LORD; decreased down-regulation of ADIPOR1-dependent signal transduction and constitutive AMPK phosphorylation in retinal pigment epithelium from patient-derived induced pluripotent stem cells; severely decreased mutant protein secretion. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 243 The length of the canonical sequence.
Location on the sequence: help FTCQVPGVYYFAVHATVYRA S LQFDLVKNGESIASFFQFFG 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                         FTCQVPGVYYFAVHATVYRASLQFDLVKNGESIASFFQFFG

Mouse                         FTCQVPGVYYFAVHATVYRASLQFDLVKNGQSIASFFQYFG

Rat                           FTCQVPGVYYFAVHATVYRASLQFDLVKNGQSIASFFQFFG
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 16 – 243 Complement C1q tumor necrosis factor-related protein 5
Domain 99 – 238 C1q
Beta strand 149 – 170



Literature citations
CTRP5 is a membrane-associated and secretory protein in the RPE and ciliary body and the S163R mutation of CTRP5 impairs its secretion.
Mandal M.N.; Vasireddy V.; Reddy G.B.; Wang X.; Moroi S.E.; Pattnaik B.R.; Hughes B.A.; Heckenlively J.R.; Hitchcock P.F.; Jablonski M.M.; Ayyagari R.;
Invest. Ophthalmol. Vis. Sci. 47:5505-5513(2006)
Cited for: SUBCELLULAR LOCATION; CHARACTERIZATION OF VARIANT LORD ARG-163;
Mutation in a short-chain collagen gene, CTRP5, results in extracellular deposit formation in late-onset retinal degeneration: a genetic model for age-related macular degeneration.
Hayward C.; Shu X.; Cideciyan A.V.; Lennon A.; Barran P.; Zareparsi S.; Sawyer L.; Hendry G.; Dhillon B.; Milam A.H.; Luthert P.J.; Swaroop A.; Hastie N.D.; Jacobson S.G.; Wright A.F.;
Hum. Mol. Genet. 12:2657-2667(2003)
Cited for: VARIANT LORD ARG-163; INVOLVEMENT IN LORD;
Novel pathogenic mutations in C1QTNF5 support a dominant negative disease mechanism in late-onset retinal degeneration.
Stanton C.M.; Borooah S.; Drake C.; Marsh J.A.; Campbell S.; Lennon A.; Soares D.C.; Vallabh N.A.; Sahni J.; Cideciyan A.V.; Dhillon B.; Vitart V.; Jacobson S.G.; Wright A.F.; Hayward C.;
Sci. Rep. 7:12147-12147(2017)
Cited for: VARIANTS LORD ARG-163; THR-188 AND CYS-216; CHARACTERIZATION OF VARIANTS LORD ARG-163 AND CYS-216; INVOLVEMENT IN LORD;
AMPK modulation ameliorates dominant disease phenotypes of CTRP5 variant in retinal degeneration.
Miyagishima K.J.; Sharma R.; Nimmagadda M.; Clore-Gronenborn K.; Qureshy Z.; Ortolan D.; Bose D.; Farnoodian M.; Zhang C.; Fausey A.; Sergeev Y.V.; Abu-Asab M.; Jun B.; Do K.V.; Kautzman Guerin M.A.; Calandria J.; George A.; Guan B.; Wan Q.; Sharp R.C.; Cukras C.; Sieving P.A.; Hufnagel R.B.; Bazan N.G.; Boesze-Battaglia K.; Miller S.; Bharti K.;
Commun. Biol. 4:1360-1360(2021)
Cited for: VARIANT LORD ARG-163; CHARACTERIZATION OF VARIANT LORD ARG-163; SUBCELLULAR LOCATION; INTERACTION WITH ADIPOR1; FUNCTION; INVOLVEMENT IN LORD;
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.