UniProtKB/Swiss-Prot Q03135: Variant p.Pro132Leu

Caveolin-1
Gene: CAV1
Feedback?

Variant information Variant position:

132 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 Proline (P) to Leucine (L) at position 132 (P132L, p.Pro132Leu). 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:

Similar physico-chemical property. Both residues are medium size and hydrophobic. The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

-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:

In breast cancer; seems to form misfolded oligomers that are retained within the Golgi complex and are not targeted to caveolae or the plasma membrane; loss of interaction with VCP. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs1213469537 [ dbSNP | Ensembl ]

Sequence information Variant position:

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

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

ALIWGIYFAILSFLHIWAVV P CIKSFLIEIQCISRVYSIYV 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                         ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Gorilla                       ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

                              ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Chimpanzee                    ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Mouse                         ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Rat                           ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Pig                           ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Bovine                        ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Rabbit                        ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Sheep                         ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Cat                           ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Horse                         ALIWGIYFAILSFLHIWAVVPCIKSFLIEIQCISRVYSIYV

Chicken                       ALIWGIYFAILSFLHIWAVVPCIRSYLIEIQCISRVYSICI

Caenorhabditis elegans        TIIFAIFFGLLASINVFIIVPLGKLLSIPGTLLAKLWNWLI

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	2 – 178	Caveolin-1
Topological domain	126 – 178	Cytoplasmic
Region	131 – 142	Interacts with SPRY1, SPRY2, SPRY3 and SPRY4
Lipidation	133 – 133	S-palmitoyl cysteine
Lipidation	143 – 143	S-palmitoyl cysteine
Helix	130 – 140

Literature citations
Caveolin-1 mutations (P132L and null) and the pathogenesis of breast cancer: caveolin-1 (P132L) behaves in a dominant-negative manner and caveolin-1 (-/-) null mice show mammary epithelial cell hyperplasia.
Lee H.; Park D.S.; Razani B.; Russell R.G.; Pestell R.G.; Lisanti M.P.;
Am. J. Pathol. 161:1357-1369(2002)
Cited for: VARIANT LEU-132; CHARACTERIZATION OF VARIANT LEU-132; Endolysosomal sorting of ubiquitylated caveolin-1 is regulated by VCP and UBXD1 and impaired by VCP disease mutations.
Ritz D.; Vuk M.; Kirchner P.; Bug M.; Schuetz S.; Hayer A.; Bremer S.; Lusk C.; Baloh R.H.; Lee H.; Glatter T.; Gstaiger M.; Aebersold R.; Weihl C.C.; Meyer H.;
Nat. Cell Biol. 13:1116-1123(2011)
Cited for: INTERACTION WITH VCP AND UBXN6; UBIQUITINATION; CHARACTERIZATION OF VARIANT LEU-132;

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.