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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O76082: Variant p.Arg399Trp

Organic cation/carnitine transporter 2
Gene: SLC22A5
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Variant information Variant position: help 399 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 Arginine (R) to Tryptophan (W) at position 399 (R399W, p.Arg399Trp). 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 large size and basic (R) to large size and aromatic (W) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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

Variant description: help In CDSP; reduces carnitine transport to less than 5% of wild-type activity. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 399 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 557 The length of the canonical sequence.
Location on the sequence: help SAMVEVPAYVLAWLLLQYLP R RYSMATALFLGGSVLLFMQL 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                         SAMVEVPAYVLAWLLLQYLPRRYSMATALFLGGSVLLFMQL

Mouse                         LAAVEVPAYVLAWLLLQYLPRRYSISAALFLGGSVLLFMQL

Rat                           LAAVEVPAYVLAWLLLQHLPRRYSISAALFLGGSVLLFIQL

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 – 557 Organic cation/carnitine transporter 2
Topological domain 395 – 406 Cytoplasmic



Literature citations
Maternal systemic primary carnitine deficiency uncovered by newborn screening: clinical, biochemical, and molecular aspects.
El-Hattab A.W.; Li F.-Y.; Shen J.; Powell B.R.; Bawle E.V.; Adams D.J.; Wahl E.; Kobori J.A.; Graham B.; Scaglia F.; Wong L.-J.;
Genet. Med. 12:19-24(2010)
Cited for: VARIANTS CDSP TRP-15; SER-46; LEU-83; SER-142; VAL-214; MET-232; TRP-399 AND ILE-442; Molecular spectrum of SLC22A5 (OCTN2) gene mutations detected in 143 subjects evaluated for systemic carnitine deficiency.
Li F.-Y.; El-Hattab A.W.; Bawle E.V.; Boles R.G.; Schmitt E.S.; Scaglia F.; Wong L.-J.;
Hum. Mutat. 31:E1632-E1651(2010)
Cited for: VARIANTS CDSP SER-12; TRP-15; LEU-17; SER-32; SER-46; LEU-83; TYR-122; SER-142; TRP-169; GLN-169; PRO-186; VAL-214; HIS-227; MET-232; TRP-257; ARG-264; GLN-282; LEU-355; LEU-398; TRP-399; MET-440; ILE-442; VAL-443; ASP-449; LYS-452; ARG-455; CYS-467; CYS-488 AND SER-507; VARIANTS PRO-66; PRO-75; ALA-96; GLY-123; LEU-143; VAL-177; LEU-230; THR-240; VAL-312; ASN-358 AND SER-549; Functional and molecular studies in primary carnitine deficiency.
Frigeni M.; Balakrishnan B.; Yin X.; Calderon F.R.O.; Mao R.; Pasquali M.; Longo N.;
Hum. Mutat. 38:1684-1699(2017)
Cited for: VARIANTS CDSP 4-TYR--PHE-557 DEL; SER-12; TRP-15; LEU-16; LEU-17; PRO-19; HIS-20; PHE-22 DEL; ASN-26; ILE-28; SER-32; VAL-44; LEU-46; SER-46; TYR-50; PRO-66; PRO-75; LEU-83; TRP-93; VAL-95; ALA-96; GLY-115; 117-TRP--PHE-557 DEL; GLY-123; ASP-131; 132-TRP--PHE-557 DEL; 140-TRP--PHE-557 DEL; SER-142; LEU-143; MET-151; GLN-169; PRO-169; TRP-169; MET-175; VAL-177; LEU-179; PRO-186; ARG-205; SER-210; CYS-211; VAL-214; LYS-219; LEU-225; HIS-227; LEU-230; PHE-231; MET-232; THR-240; VAL-242; ARG-247; 254-ARG--PHE-557 DEL; GLN-254; 256-TRP--PHE-557 DEL; TRP-257; ARG-264; MET-264; PRO-269; 275-TRP--PHE-557 DEL; PHE-280; 282-ARG--PHE-557 DEL; GLN-282; ARG-283; CYS-283; 289-ARG--PHE-557 DEL; 295-VAL--PHE-557 DEL; ASP-301; VAL-312; LYS-317; 319-GLN--PHE-557 DEL; THR-348; ARG-351; LEU-355; ASN-358; PRO-363; 387-TYR--PHE-557 DEL; LEU-394 DEL; LEU-398; GLN-399; TRP-399; GLY-412; GLY-439; MET-440; ILE-442; VAL-443; PHE-446; CYS-447; LEU-448; ASP-449; LYS-452; ARG-455; VAL-462; CYS-467; ARG-468; PHE-470; HIS-471; PRO-471; ARG-476; LEU-478; CYS-488; HIS-488 AND SER-507; VARIANTS PHE-481 AND SER-549; CHARACTERIZATION OF VARIANTS CDSP SER-12; TRP-15; LEU-16; LEU-17; PRO-19; HIS-20; PHE-23 DEL; ASN-26; ILE-28; SER-32; VAL-44; LEU-46; SER-46; TYR-50; PRO-66; PRO-75; LEU-83; TRP-93; VAL-95; ALA-96; GLY-115; GLY-123; ASP-131; SER-142; LEU-143; MET-151; GLN-169; PRO-169; TRP-169; MET-175; VAL-177; LEU-179; PRO-186; ARG-205; SER-210; CYS-211; VAL-214; LYS-219; LEU-225; HIS-227; LEU-230; PHE-231; MET-232; THR-240; VAL-242; ARG-247; GLN-254; TRP-257; ARG-264; MET-264; PRO-269; PHE-280; GLN-282; ARG-283; CYS-283; ASP-301; VAL-312; LYS-317; THR-348; ARG-351; LEU-355; ASN-358; PRO-363; LEU-394 DEL; LEU-398; GLN-399; TRP-399; GLY-412; GLY-439; MET-440; ILE-442; VAL-443; PHE-446; CYS-447; LEU-448; ASP-449; LYS-452; ARG-455; VAL-462; CYS-467; ARG-468; PHE-470; HIS-471; PRO-471; ARG-476; LEU-478; CYS-488; HIS-488 AND SER-507; CHARACTERIZATION OF VARIANTS PHE-481 AND SER-549;
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.