Q8BGC3 · MOT12_MOUSE
- ProteinMonocarboxylate transporter 12
- GeneSlc16a12
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids486 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Functions as a transporter for creatine and as well for its precursor guanidinoacetate. Transport of creatine and GAA is independent of resting membrane potential and extracellular Na+, Cl-, or pH. Contributes to the process of creatine biosynthesis and distribution.
Catalytic activity
- creatine(in) = creatine(out)
- guanidinoacetate(in) = guanidinoacetate(out)
Activity regulation
Creatine uptake is inhibited by carbonyl cyanide 3-chlorophenylhydrazone (CCCP) and by valinomycin.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | basolateral plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | creatine transmembrane transporter activity | |
Molecular Function | monocarboxylic acid transmembrane transporter activity | |
Molecular Function | uniporter activity | |
Biological Process | creatine transmembrane transport | |
Biological Process | creatinine metabolic process |
Names & Taxonomy
Protein names
- Recommended nameMonocarboxylate transporter 12
- Short namesMCT 12
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ8BGC3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Multi-pass membrane protein
Basolateral cell membrane ; Multi-pass membrane protein
Note: Interaction with isoform 2 of BSG is required for its localization to the plasma membrane.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MTKITRVSL | ||||||
Transmembrane | 10-30 | Helical | ||||
Sequence: ASPPDGGWGWMIVAGCFLVTI | ||||||
Transmembrane | 58-78 | Helical | ||||
Sequence: AWIHSIVDCMTMLCAPLGSVV | ||||||
Transmembrane | 86-106 | Helical | ||||
Sequence: AGIMLGGLLASTGFILGSFAT | ||||||
Transmembrane | 115-135 | Helical | ||||
Sequence: LGVLTGLGFALCYSPAIAMVG | ||||||
Transmembrane | 148-168 | Helical | ||||
Sequence: IAMSGSGIGTFILAPVVQLLI | ||||||
Transmembrane | 177-197 | Helical | ||||
Sequence: LLILGGFVLNLCVCGALMRPI | ||||||
Transmembrane | 253-273 | Helical | ||||
Sequence: FVVLAVSVLFMAYGCSPLFVY | ||||||
Transmembrane | 289-309 | Helical | ||||
Sequence: AFLMSILGVIDIVGNITFGWL | ||||||
Transmembrane | 320-340 | Helical | ||||
Sequence: YVCYLFAVALDGLCYLCLPML | ||||||
Transmembrane | 353-373 | Helical | ||||
Sequence: FGYFDGAYVTLIPVVTAEIVG | ||||||
Transmembrane | 383-403 | Helical | ||||
Sequence: VVYFLHAVPYLVSPPIAGWLV | ||||||
Transmembrane | 410-430 | Helical | ||||
Sequence: TAAFLLCGFAMIFSSILLGFV | ||||||
Topological domain | 431-486 | Cytoplasmic | ||||
Sequence: RIVKRMKRTQVPFPVKDSDPKLQLWTNGSVAYSVARELDQKDEEPLPKARSGCNLT |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000286676 | 1-486 | Monocarboxylate transporter 12 | |||
Sequence: MTKITRVSLASPPDGGWGWMIVAGCFLVTICTRAVTRCISIFFVEFQTYFAQDYSQTAWIHSIVDCMTMLCAPLGSVVSNQLSCQAGIMLGGLLASTGFILGSFATSLKHLYLSLGVLTGLGFALCYSPAIAMVGKYFSRRKALAYGIAMSGSGIGTFILAPVVQLLIEQFSWRGALLILGGFVLNLCVCGALMRPITLKEDRSVPEKNHNRESQREDCKQASPYSPLTKECTETRLCCSLQQEYGFLLMSDFVVLAVSVLFMAYGCSPLFVYLVPYALSVGVSHHQAAFLMSILGVIDIVGNITFGWLTDRRCLKNYRYVCYLFAVALDGLCYLCLPMLQTFPLLVPFSCTFGYFDGAYVTLIPVVTAEIVGTTSLSSALGVVYFLHAVPYLVSPPIAGWLVDTTGSYTAAFLLCGFAMIFSSILLGFVRIVKRMKRTQVPFPVKDSDPKLQLWTNGSVAYSVARELDQKDEEPLPKARSGCNLT |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in the lung, liver, kidney, and pancreas (PubMed:26376857).
Expressed in eye lens
Expressed in eye lens
Developmental stage
Expressed in lens at P1 and P7 (PubMed:21778275).
The expression levels are higher than in adult lens (PubMed:21778275).
Detected in the basolateral membrane of the lens epithelium, with strong staining at equatorial epithelium, and in differentiating secondary fiber cells at P1 (at protein level) (PubMed:21778275).
The expression levels are higher than in adult lens (PubMed:21778275).
Detected in the basolateral membrane of the lens epithelium, with strong staining at equatorial epithelium, and in differentiating secondary fiber cells at P1 (at protein level) (PubMed:21778275).
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length486
- Mass (Da)53,152
- Last updated2003-03-01 v1
- ChecksumAA3CC9951FB28247
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 234 | in Ref. 2; AAI13804/AAI11903 | ||||
Sequence: E → K | ||||||
Sequence conflict | 293 | in Ref. 2; AAI13804 | ||||
Sequence: S → C |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK028284 EMBL· GenBank· DDBJ | BAC25857.1 EMBL· GenBank· DDBJ | mRNA | ||
AK029076 EMBL· GenBank· DDBJ | BAC26279.1 EMBL· GenBank· DDBJ | mRNA | ||
BC111902 EMBL· GenBank· DDBJ | AAI11903.1 EMBL· GenBank· DDBJ | mRNA | ||
BC113803 EMBL· GenBank· DDBJ | AAI13804.1 EMBL· GenBank· DDBJ | mRNA |