UniProtKB/Swiss-Prot Q96RJ0: Variant p.Thr252Ala

Trace amine-associated receptor 1
Gene: TAAR1
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Variant information Variant position:

252 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 Threonine (T) to Alanine (A) at position 252 (T252A, p.Thr252Ala). 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:

Change from medium size and polar (T) to small size and hydrophobic (A) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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:

Reduced activation of G(i) G alpha proteins in response to agonist-binding. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs6926857 [ dbSNP | Ensembl ]

Sequence information Variant position:

252 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

339 The length of the canonical sequence.
Location on the sequence:

QIGLEMKNGISQSKERKAVK T LGIVMGVFLICWCPFFICTV 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:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         QIGLEMKNGISQSKERKAVKTLGIVMGVFLICWCPFFICTV

Rhesus macaque                QIGLEMKNGISQSKERKAVKTLGIVMGVFLICWCPFFVCTV

Chimpanzee                    QIGLEMKNGISQSKERKAVKTLGIVMGVFLICWCPFFICTV

Mouse                         QVGLEGKSQAPQSKETKAAKTLGIMVGVFLVCWCPFFLCTV

Rat                           QVGLEGESRAPQSKETKAAKTLGIMVGVFLLCWCPFFFCMV

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	1 – 339	Trace amine-associated receptor 1
Transmembrane	250 – 273	Helical; Name=6
Mutagenesis	253 – 253	L -> A. Reduced activation of G(i) G alpha proteins in response to agonist-binding.
Mutagenesis	260 – 260	F -> A. Reduced activation of G(s) G alpha proteins in response to agonist-binding.
Mutagenesis	264 – 264	W -> A. Abolished activation of G alpha proteins in response to 3-iodothyronamine-binding.
Mutagenesis	264 – 264	W -> F. Abolished activation of G alpha proteins in response to agonist-binding.
Mutagenesis	267 – 267	F -> A. Abolished activation of G alpha proteins in response to 3-iodothyronamine-binding. Reduced activation of G(q) G alpha proteins in response to agonist-binding. Does not affect activation of G(s) G alpha proteins in response to agonist-binding.
Mutagenesis	268 – 268	F -> A. Abolished activation of G alpha proteins in response to 3-iodothyronamine-binding.
Mutagenesis	271 – 271	T -> AN. Decreased G-protein coupled receptor activity in response to p-tyramine-binding.
Helix	248 – 276

Literature citations
Ligand recognition and G-protein coupling of trace amine receptor TAAR1.
Xu Z.; Guo L.; Yu J.; Shen S.; Wu C.; Zhang W.; Zhao C.; Deng Y.; Tian X.; Feng Y.; Hou H.; Su L.; Wang H.; Guo S.; Wang H.; Wang K.; Chen P.; Zhao J.; Zhang X.; Yong X.; Cheng L.; Liu L.; Yang S.; Yang F.; Wang X.; Yu X.; Xu Y.; Sun J.P.; Yan W.; Shao Z.;
Nature 624:672-681(2023)
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (2.84 ANGSTROMS) IN COMPLEX WITH BETA-PHENYLETHYLAMINE; GNAI1; GNAS; GNB1 AND GNG2; DISULFIDE BOND; FUNCTION; ACTIVITY REGULATION; MUTAGENESIS OF HIS-55; ARG-83; ASP-103; SER-107; LEU-114; PHE-154; SER-183; VAL-184; PHE-185; PHE-186; THR-194; GLN-220; ILE-224; LEU-253; PHE-260; TRP-264; PHE-267; PHE-268; ILE-290; PHE-292; TYR-294; TYR-304 AND PHE-307; CHARACTERIZATION OF VARIANT ALA-252;

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.