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O95907 (MOT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monocarboxylate transporter 3

Short name=MCT 3
Alternative name(s):
Solute carrier family 16 member 8
Gene names
Name:SLC16A8
Synonyms:MCT3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length504 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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.

Tissue specificity

Retinal pigment epithelium.

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 – 504504Monocarboxylate transporter 3
PRO_0000211390

Regions

Topological domain1 – 1414Cytoplasmic Potential
Transmembrane15 – 3521Helical; Potential
Topological domain36 – 5823Extracellular Potential
Transmembrane59 – 7921Helical; Potential
Topological domain80 – 856Cytoplasmic Potential
Transmembrane86 – 10621Helical; Potential
Topological domain107 – 1159Extracellular Potential
Transmembrane116 – 13621Helical; Potential
Topological domain137 – 1437Cytoplasmic Potential
Transmembrane144 – 16421Helical; Potential
Topological domain165 – 1728Extracellular Potential
Transmembrane173 – 19321Helical; Potential
Topological domain194 – 25461Cytoplasmic Potential
Transmembrane255 – 27521Helical; Potential
Topological domain276 – 28914Extracellular Potential
Transmembrane290 – 31021Helical; Potential
Topological domain311 – 3188Cytoplasmic Potential
Transmembrane319 – 33517Helical; Potential
Topological domain336 – 3427Extracellular Potential
Transmembrane343 – 36321Helical; Potential
Topological domain364 – 37613Cytoplasmic Potential
Transmembrane377 – 39721Helical; Potential
Topological domain398 – 41013Extracellular Potential
Transmembrane411 – 43121Helical; Potential
Topological domain432 – 50473Cytoplasmic Potential

Natural variations

Natural variant2351R → W. Ref.1
Corresponds to variant rs4289289 [ dbSNP | Ensembl ].
VAR_060107
Natural variant4051V → A. Ref.1
Corresponds to variant rs2076371 [ dbSNP | Ensembl ].
VAR_053654

Sequences

Sequence LengthMass (Da)Tools
O95907 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: E924D4FC31340398

FASTA50452,319
        10         20         30         40         50         60 
MGAGGPRRGE GPPDGGWGWV VLGACFVVTG FAYGFPKAVS VFFRALMRDF DAGYSDTAWV 

        70         80         90        100        110        120 
SSIMLAMLYG TGPVSSILVT RFGCRPVMLA GGLLASAGMI LASFATRLLE LYLTAGVLTG 

       130        140        150        160        170        180 
LGLALNFQPS LIMLGLYFER RRPLANGLAA AGSPVFLSAL SPLGQQLLER FGWRGGFLLL 

       190        200        210        220        230        240 
GGLLLHCCAC GAVMRPPPGP GPRPRRDSAG DRAGDAPGEA EADGAGLQLR EASPRVRPRR 

       250        260        270        280        290        300 
RLLDLAVCTD RAFAVYAVTK FLMALGLFVP AILLVNYAKD AGVPDTDAAF LLSIVGFVDI 

       310        320        330        340        350        360 
VARPACGALA GLARLRPHVP YLFSLALLAN GLTDLSSARA RSYGALVAFC VAFGLSYGMV 

       370        380        390        400        410        420 
GALQFEVLMA AVGAPRFPSA LGLVLLVEAA AVLIGPPSAG RLVDVLKNYE IIFYLAGSEV 

       430        440        450        460        470        480 
ALAGVFMAVA TNCCLRCAKA APSGPGTEGG ASDTEDAEAE GDSEPLPVVA EEPGNLEALE 

       490        500 
VLSARGEPTE PEIEARPRLA AESV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning of the human monocarboxylate transporter MCT3 gene: localization to chromosome 22q12.3-q13.2."
Yoon H., Donoso L.A., Philp N.J.
Genomics 60:366-370(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS TRP-235 AND ALA-405.
[2]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF132610 mRNA. Translation: AAF03565.1.
AF132611 Genomic DNA. Translation: AAF03489.1.
AL031587 Genomic DNA. Translation: CAB37479.1.
CCDSCCDS13966.1.
RefSeqNP_037488.2. NM_013356.2.
UniGeneHs.745256.

3D structure databases

ProteinModelPortalO95907.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117083. 2 interactions.
IntActO95907. 2 interactions.
MINTMINT-1429542.
STRING9606.ENSP00000321735.

Chemistry

DrugBankDB00119. Pyruvic acid.

Protein family/group databases

TCDB2.A.1.13.9. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteO95907.

Proteomic databases

PaxDbO95907.
PRIDEO95907.

Protocols and materials databases

DNASU23539.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320521; ENSP00000321735; ENSG00000100156.
GeneID23539.
KEGGhsa:23539.
UCSCuc003auu.3. human.

Organism-specific databases

CTD23539.
GeneCardsGC22M038474.
H-InvDBHIX0041123.
HGNCHGNC:16270. SLC16A8.
MIM610409. gene.
neXtProtNX_O95907.
PharmGKBPA38106.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG297999.
HOGENOMHOG000280688.
HOVERGENHBG006384.
InParanoidO95907.
KOK08185.
OMAVCTDRAF.
PhylomeDBO95907.
TreeFamTF313792.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.
REACT_20633. Bile salt and organic anion SLC transporters.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressO95907.
BgeeO95907.
CleanExHS_SLC16A8.
GenevestigatorO95907.

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. SSF103473. 1 hit.
TIGRFAMsTIGR00892. 2A0113. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi23539.
NextBio46042.
PROO95907.
SOURCESearch...

Entry information

Entry nameMOT3_HUMAN
AccessionPrimary (citable) accession number: O95907
Secondary accession number(s): Q9UBE2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: May 1, 1999
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM