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Protein

Monocarboxylate transporter 2

Gene

Slc16a7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Proton-coupled 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. Functions as high-affinity pyruvate transporter.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Symport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Monocarboxylate transporter 2
Short name:
MCT 2
Alternative name(s):
Solute carrier family 16 member 7
Gene namesi
Name:Slc16a7
Synonyms:Mct2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3691. Slc16a7.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 2121CytoplasmicSequence analysisAdd
BLAST
Transmembranei22 – 4221HelicalSequence analysisAdd
BLAST
Topological domaini43 – 6523ExtracellularSequence analysisAdd
BLAST
Transmembranei66 – 8621HelicalSequence analysisAdd
BLAST
Topological domaini87 – 959CytoplasmicSequence analysis
Transmembranei96 – 11621HelicalSequence analysisAdd
BLAST
Topological domaini117 – 1215ExtracellularSequence analysis
Transmembranei122 – 14221HelicalSequence analysisAdd
BLAST
Topological domaini143 – 15412CytoplasmicSequence analysisAdd
BLAST
Transmembranei155 – 17521HelicalSequence analysisAdd
BLAST
Topological domaini176 – 1794ExtracellularSequence analysis
Transmembranei180 – 20021HelicalSequence analysisAdd
BLAST
Topological domaini201 – 25050CytoplasmicSequence analysisAdd
BLAST
Transmembranei251 – 27121HelicalSequence analysisAdd
BLAST
Topological domaini272 – 28615ExtracellularSequence analysisAdd
BLAST
Transmembranei287 – 30721HelicalSequence analysisAdd
BLAST
Topological domaini308 – 3169CytoplasmicSequence analysis
Transmembranei317 – 33721HelicalSequence analysisAdd
BLAST
Topological domaini338 – 3425ExtracellularSequence analysis
Transmembranei343 – 36321HelicalSequence analysisAdd
BLAST
Topological domaini364 – 37714CytoplasmicSequence analysisAdd
BLAST
Transmembranei378 – 39821HelicalSequence analysisAdd
BLAST
Topological domaini399 – 41012ExtracellularSequence analysisAdd
BLAST
Transmembranei411 – 43121HelicalSequence analysisAdd
BLAST
Topological domaini432 – 48958CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • cytoplasm Source: RGD
  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 489489Monocarboxylate transporter 2PRO_0000211389Add
BLAST

Proteomic databases

PaxDbiQ63344.
PRIDEiQ63344.

PTM databases

PhosphoSiteiQ63344.

Expressioni

Tissue specificityi

Detected in brain and kidney (at protein level).1 Publication

Interactioni

Subunit structurei

Interacts with GRID2IP (By similarity). Interacts with EMB.By similarity2 Publications

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054845.

Structurei

3D structure databases

ProteinModelPortaliQ63344.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2504. Eukaryota.
COG0477. LUCA.
HOGENOMiHOG000280688.
HOVERGENiHBG006384.
InParanoidiQ63344.
PhylomeDBiQ63344.

Family and domain databases

InterProiIPR004743. MCT.
IPR027178. MCT2.
IPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PANTHERiPTHR11360:SF25. PTHR11360:SF25. 1 hit.
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00892. 2A0113. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q63344-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSESSVKAT AAPPPFPLPP DGGWGWVVVC ASFISIGFSY AFPKAVTVFF
60 70 80 90 100
NDIKDIFKTT SSQIAWISSI MLAVMYAGGP ISSVLVNNYG SRPVLIVGGL
110 120 130 140 150
LCCTGMILAS FSSSVIELYL TVGFIGGLGL AFNLQPALTI IGKYFYRKRP
160 170 180 190 200
LANGFAMAGS PVFLSTLAPF NQFLFNSYGW KGSFLILGAI FLHSCVAGCL
210 220 230 240 250
MRPVGPSPRA AKSKSKVGSR QDSSTKRLSK VSTAEKINRF LDFGLFTHRG
260 270 280 290 300
FLIYLSGNVV LFLGMFAPII FLAPYAKDKG VDDYNSAFLL SVMAFTDMFA
310 320 330 340 350
RPSVGLIANT SLIRPRIQYL FSVAIMFTGI CHLLCPLAHS YTALVVYVIF
360 370 380 390 400
FGIGFGSISS LLFECLMDQV GASRFSSAVG LVTIVECCPV LFGPPLAGKL
410 420 430 440 450
LDITGQYKYL YIASGIVVLS SGIYLLICNA INYRLLEKER KREKARRKKS
460 470 480
ASQASKEMEA LSRSKQDDVT VKVSNTHNPP SDRDKESSI
Length:489
Mass (Da):53,057
Last modified:November 1, 1996 - v1
Checksum:i447E1CE2D707044B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951L → V in AAB04023 (PubMed:9482213).Curated
Sequence conflicti392 – 3921F → P in AAB04023 (PubMed:9482213).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97445 mRNA. Translation: CAA66074.1.
U62316 mRNA. Translation: AAB04023.1.
UniGeneiRn.10524.
Rn.217495.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97445 mRNA. Translation: CAA66074.1.
U62316 mRNA. Translation: AAB04023.1.
UniGeneiRn.10524.
Rn.217495.

3D structure databases

ProteinModelPortaliQ63344.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000054845.

PTM databases

PhosphoSiteiQ63344.

Proteomic databases

PaxDbiQ63344.
PRIDEiQ63344.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

RGDi3691. Slc16a7.

Phylogenomic databases

eggNOGiKOG2504. Eukaryota.
COG0477. LUCA.
HOGENOMiHOG000280688.
HOVERGENiHBG006384.
InParanoidiQ63344.
PhylomeDBiQ63344.

Miscellaneous databases

PROiQ63344.

Family and domain databases

InterProiIPR004743. MCT.
IPR027178. MCT2.
IPR011701. MFS.
IPR020846. MFS_dom.
[Graphical view]
PANTHERiPTHR11360:SF25. PTHR11360:SF25. 1 hit.
PfamiPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00892. 2A0113. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the monocarboxylate transporter isoform MCT2 from rat testis provides evidence that expression in tissues is species-specific and may involve post-transcriptional regulation."
    Jackson V.N., Price N.T., Carpenter L., Halestrap A.P.
    Biochem. J. 324:447-453(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
    Strain: Sprague-Dawley.
    Tissue: Testis.
  2. "Expression of the monocarboxylate transporter MCT2 by rat brain glia."
    Gerhart D.Z., Enerson B.E., Zhdankina O.Y., Leino R.L., Drewes L.R.
    Glia 22:272-281(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Wistar.
    Tissue: Brain.
  3. "Basigin (CD147) is the target for organomercurial inhibition of monocarboxylate transporter isoforms 1 and 4: the ancillary protein for the insensitive MCT2 is EMBIGIN (gp70)."
    Wilson M.C., Meredith D., Fox J.E., Manoharan C., Davies A.J., Halestrap A.P.
    J. Biol. Chem. 280:27213-27221(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMB, SUBCELLULAR LOCATION.
  4. "The inhibition of monocarboxylate transporter 2 (MCT2) by AR-C155858 is modulated by the associated ancillary protein."
    Ovens M.J., Manoharan C., Wilson M.C., Murray C.M., Halestrap A.P.
    Biochem. J. 431:217-225(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMB, SUBCELLULAR LOCATION, FUNCTION.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMOT2_RAT
AccessioniPrimary (citable) accession number: Q63344
Secondary accession number(s): Q63649
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 11, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.