Gene Ontology annotation through association of InterPro records with GO terms

Use of the ND evidence code for Gene Ontology (GO) terms

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

PMID:11536335

The putative monocarboxylate permeases of the yeast Saccharomyces cerevisiae do not transport monocarboxylic acids across the plasma membrane.

A yeast mch1-5 quintuple deletion showed no growth defect on monocarboxylic acids and wild-type-like monocarboxylate uptake/secretion; the yeast Mch proteins do not transport monocarboxylic acids and perform other functions than their mammalian counterparts. Some Mch proteins reside in intracellular membranes; the mch1-5 mutant had reduced chemostat biomass but pyruvate uptake into isolated mitochondria was unaffected.

PMID:16204239

The monocarboxylate transporter homolog Mch5p catalyzes riboflavin (vitamin B2) uptake in Saccharomyces cerevisiae.

Mch5p is a plasma-membrane riboflavin (vitamin B2) transporter (facilitated diffusion, Km ~17 uM); the other members of the MCH gene family appear to have unrelated functions, so MCH2's substrate is not expected to be riboflavin.

PMID:16847258

A global topology map of the Saccharomyces cerevisiae membrane proteome.

Genome-scale study presenting experimentally constrained topology models for 546 yeast membrane proteins, supporting the multi-pass membrane topology of MCH2.

PMID:8091865

Sequencing of a 13.2 kb segment next to the left telomere of yeast chromosome XI revealed five open reading frames and recent recombination events with the right arms of chromosomes III and V.

Original chromosome-XI sequencing paper; the ORF (later MCH2/YKL221W) is similar to the mammalian putative mevalonate transporter and has the structure of membrane transporters.

file:yeast/MCH2/MCH2-bioinformatics/RESULTS.md

MCH2 (YKL221W / P36032) bioinformatics analysis

Reproducible comparative/structural analysis confirming MCH2 is a 12-TMS MFS monocarboxylate-porter (SLC16/MCT-like) protein, but showing it lacks the conserved TM1 lysine and MFS motif A of transporting MCTs and is distant (<=23% identity) from all characterized transporters, so no substrate can be inferred from homology.