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P53987 (MOT1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Monocarboxylate transporter 1

Short name=MCT 1
Alternative name(s):
Solute carrier family 16 member 1
Gene names
Name:Slc16a1
Synonyms:Mct1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proton-linked monocarboxylate transporter. Catalyzes the rapid transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, branched-chain oxo acids derived from leucine, valine and isoleucine, and the ketone bodies acetoacetate, beta-hydroxybutyrate and acetate By similarity.

Subcellular location

Cell membrane; Multi-pass membrane protein By similarity.

Sequence similarities

Belongs to the major facilitator superfamily. Monocarboxylate porter (TC 2.A.1.13) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 494494Monocarboxylate transporter 1
PRO_0000211384

Regions

Topological domain1 – 1515Cytoplasmic Potential
Transmembrane16 – 3621Helical; Potential
Topological domain37 – 5923Extracellular Potential
Transmembrane60 – 8021Helical; Potential
Topological domain81 – 866Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 1114Extracellular Potential
Transmembrane112 – 13221Helical; Potential
Topological domain133 – 14311Cytoplasmic Potential
Transmembrane144 – 16421Helical; Potential
Topological domain165 – 1662Extracellular Potential
Transmembrane167 – 18721Helical; Potential
Topological domain188 – 25568Cytoplasmic Potential
Transmembrane256 – 27621Helical; Potential
Topological domain277 – 29115Extracellular Potential
Transmembrane292 – 31221Helical; Potential
Topological domain313 – 3219Cytoplasmic Potential
Transmembrane322 – 34221Helical; Potential
Topological domain343 – 3464Extracellular Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 38215Cytoplasmic Potential
Transmembrane383 – 40321Helical; Potential
Topological domain404 – 41512Extracellular Potential
Transmembrane416 – 43621Helical; Potential
Topological domain437 – 49458Cytoplasmic Potential

Amino acid modifications

Modified residue2101Phosphoserine Ref.5
Modified residue2131Phosphoserine Ref.5
Modified residue2301Phosphoserine By similarity
Modified residue4591Phosphothreonine By similarity
Modified residue4601Phosphoserine By similarity
Modified residue4611Phosphothreonine By similarity
Modified residue4761Phosphoserine By similarity
Modified residue4921Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
P53987 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: CF82F8794CDBF057

FASTA49453,238
        10         20         30         40         50         60 
MPPAIGGPVG YTPPDGGWGW AVVVGAFISI GFSYAFPKSI TVFFKEIEII FSATTSEVSW 

        70         80         90        100        110        120 
ISSIMLAVMY AGGPISSILV NKYGSRPVMI AGGCLSGCGL IAASFCNTVQ ELYFCIGVIG 

       130        140        150        160        170        180 
GLGLAFNLNP ALTMIGKYFY KKRPLANGLA MAGSPVFLST LAPLNQAFFG IFGWRGSFLI 

       190        200        210        220        230        240 
LGGLLLNCCV AGSLMRPIGP QQGKVEKLKS KESLQEAGKS DANTDLIGGS PKGEKLSVFQ 

       250        260        270        280        290        300 
TVNKFLDLSL FTHRGFLLYL SGNVVMFFGL FTPLVFLSNY GKSKHFSSEK SAFLLSILAF 

       310        320        330        340        350        360 
VDMVARPSMG LAANTRWIRP RVQYFFAASV VANGVCHLLA PLSTTYVGFC IYAGVFGFAF 

       370        380        390        400        410        420 
GWLSSVLFET LMDLVGPQRF SSAVGLVTIV ECCPVLLGPP LLGRLNDMYG DYKYTYWACG 

       430        440        450        460        470        480 
VILIIAGLYL FIGMGINYRL VAKEQKAEEK KRDGKEDETS TDVDEKPKKT MKETQSPAPL 

       490 
QNSSGDPAEE ESPV 

« Hide

References

« Hide 'large scale' references
[1]"cDNA cloning and functional characterization of rat intestinal monocarboxylate transporter."
Takanaga H., Tamai I., Inaba S., Sai Y., Higashida H., Yamamoto H., Tsuji A.
Biochem. Biophys. Res. Commun. 217:370-377(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Small intestine.
[2]"cDNA cloning of MCT1, a monocarboxylate transporter from rat skeletal muscle."
Jackson V.N., Price N.T., Halestrap A.P.
Biochim. Biophys. Acta 1238:193-196(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Wistar.
Tissue: Skeletal muscle.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[4]"A monocarboxylate transporter MCT1 is located at the basolateral pole of rat jejunum."
Orsenigo M.N., Tosco M., Bazzini C., Laforenza U., Faelli A.
Exp. Physiol. 84:1033-1042(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 264-472.
Tissue: Jejunal epithelium.
[5]"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS."
Moser K., White F.M.
J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210 AND SER-213, MASS SPECTROMETRY.
Strain: Fischer.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63834 mRNA. Translation: BAA09894.1.
X86216 mRNA. Translation: CAA60116.1.
BC078877 mRNA. Translation: AAH78877.1.
AJ236865 mRNA. Translation: CAB37948.1.
IPIIPI00214787.
PIRJC4399.
RefSeqNP_036848.1. NM_012716.2.
UniGeneRn.6085.

3D structure databases

ProteinModelPortalP53987.
ModBaseSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000027234.

PTM databases

PhosphoSiteP53987.

Proteomic databases

PaxDbP53987.
PRIDEP53987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000027234; ENSRNOP00000027234; ENSRNOG00000019996.
GeneID25027.
KEGGrno:25027.
UCSCRGD:3690. rat.

Organism-specific databases

CTD6566.
RGD3690. Slc16a1.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00670000097675.
HOGENOMHOG000280688.
HOVERGENHBG006384.
InParanoidP53987.
KOK08179.
OMAQYFFAIS.
OrthoDBEOG41G341.

Enzyme and pathway databases

SABIO-RKP53987.

Gene expression databases

GenevestigatorP53987.
GermOnlineENSRNOG00000019996. Rattus norvegicus.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004743. Monocarb_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMsTIGR00892. 2A0113. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio605163.

Entry information

Entry nameMOT1_RAT
AccessionPrimary (citable) accession number: P53987
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: April 3, 2013
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families