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O15427 (MOT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monocarboxylate transporter 4

Short name=MCT 4
Alternative name(s):
Solute carrier family 16 member 3
Gene names
Name:SLC16A3
Synonyms:MCT4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length465 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Tissue specificity

Highly expressed in skeletal muscle.

Sequence similarities

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

Caution

Was initially assigned as monocarboxylate transporter 3 (MCT3) (Ref.1). However, it was later shown that it corresponds to monocarboxylate transporter 4 (MCT4).

Ontologies

Keywords
   Biological processSymport
Transport
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cellular metabolic process

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

monocarboxylic acid transport

Traceable author statement Ref.1. Source: ProtInc

pyruvate metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

integral component of plasma membrane

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

nuclear membrane

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionmonocarboxylic acid transmembrane transporter activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

secondary active monocarboxylate transmembrane transporter activity

Inferred from electronic annotation. Source: InterPro

symporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 465464Monocarboxylate transporter 4
PRO_0000211394

Regions

Topological domain2 – 1716Cytoplasmic Potential
Transmembrane18 – 3821Helical; Potential
Topological domain39 – 6123Extracellular Potential
Transmembrane62 – 8221Helical; Potential
Topological domain83 – 842Cytoplasmic Potential
Transmembrane85 – 10521Helical; Potential
Topological domain106 – 1094Extracellular Potential
Transmembrane110 – 13021Helical; Potential
Topological domain131 – 14919Cytoplasmic Potential
Transmembrane150 – 17021Helical; Potential
Topological domain171 – 1799Extracellular Potential
Transmembrane180 – 20021Helical; Potential
Topological domain201 – 22727Cytoplasmic Potential
Transmembrane228 – 24821Helical; Potential
Topological domain249 – 26416Extracellular Potential
Transmembrane265 – 28521Helical; Potential
Topological domain286 – 2949Cytoplasmic Potential
Transmembrane295 – 31521Helical; Potential
Topological domain316 – 3172Extracellular Potential
Transmembrane318 – 33821Helical; Potential
Topological domain339 – 35113Cytoplasmic Potential
Transmembrane352 – 37221Helical; Potential
Topological domain373 – 38412Extracellular Potential
Transmembrane385 – 40521Helical; Potential
Topological domain406 – 46560Cytoplasmic Potential

Amino acid modifications

Modified residue4601Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.8
Modified residue4641Phosphoserine Ref.7 Ref.8

Sequences

Sequence LengthMass (Da)Tools
O15427 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7BF6384B0F14D927

FASTA46549,469
        10         20         30         40         50         60 
MGGAVVDEGP TGVKAPDGGW GWAVLFGCFV ITGFSYAFPK AVSVFFKELI QEFGIGYSDT 

        70         80         90        100        110        120 
AWISSILLAM LYGTGPLCSV CVNRFGCRPV MLVGGLFASL GMVAASFCRS IIQVYLTTGV 

       130        140        150        160        170        180 
ITGLGLALNF QPSLIMLNRY FSKRRPMANG LAAAGSPVFL CALSPLGQLL QDRYGWRGGF 

       190        200        210        220        230        240 
LILGGLLLNC CVCAALMRPL VVTAQPGSGP PRPSRRLLDL SVFRDRGFVL YAVAASVMVL 

       250        260        270        280        290        300 
GLFVPPVFVV SYAKDLGVPD TKAAFLLTIL GFIDIFARPA AGFVAGLGKV RPYSVYLFSF 

       310        320        330        340        350        360 
SMFFNGLADL AGSTAGDYGG LVVFCIFFGI SYGMVGALQF EVLMAIVGTH KFSSAIGLVL 

       370        380        390        400        410        420 
LMEAVAVLVG PPSGGKLLDA THVYMYVFIL AGAEVLTSSL ILLLGNFFCI RKKPKEPQPE 

       430        440        450        460 
VAAAEEEKLH KPPADSGVDL REVEHFLKAE PEKNGEVVHT PETSV 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and sequencing of four new mammalian monocarboxylate transporter (MCT) homologues confirms the existence of a transporter family with an ancient past."
Price N.T., Jackson V.N., Halestrap A.P.
Biochem. J. 329:321-328(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[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: Cerebellum.
[4]Bienvenut W.V., Lao L., Ryan K.L.
Submitted (OCT-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-14 AND 429-441, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[6]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-460 AND SER-464, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U81800 mRNA. Translation: AAC52015.1.
AK127319 mRNA. Translation: BAG54480.1.
BC112267 mRNA. Translation: AAI12268.1.
BC112269 mRNA. Translation: AAI12270.1.
CCDSCCDS11804.1.
RefSeqNP_001035887.1. NM_001042422.2.
NP_001035888.1. NM_001042423.2.
NP_001193879.1. NM_001206950.1.
NP_001193880.1. NM_001206951.1.
NP_001193881.1. NM_001206952.1.
NP_004198.1. NM_004207.3.
UniGeneHs.500761.

3D structure databases

ProteinModelPortalO15427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114571. 1 interaction.
IntActO15427. 1 interaction.
MINTMINT-4526381.
STRING9606.ENSP00000376150.

Chemistry

ChEMBLCHEMBL2073663.
DrugBankDB00119. Pyruvic acid.

Protein family/group databases

TCDB2.A.1.13.6. the major facilitator superfamily (mfs).

PTM databases

PhosphoSiteO15427.

Proteomic databases

MaxQBO15427.
PaxDbO15427.
PeptideAtlasO15427.
PRIDEO15427.

Protocols and materials databases

DNASU9123.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392339; ENSP00000376150; ENSG00000141526.
ENST00000392341; ENSP00000376152; ENSG00000141526.
ENST00000581287; ENSP00000463978; ENSG00000141526.
ENST00000582743; ENSP00000462405; ENSG00000141526.
GeneID9123.
KEGGhsa:9123.
UCSCuc002kea.3. human.

Organism-specific databases

CTD9123.
GeneCardsGC17P080186.
HGNCHGNC:10924. SLC16A3.
HPACAB017490.
HPA021451.
MIM603877. gene.
neXtProtNX_O15427.
PharmGKBPA35815.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG321880.
HOGENOMHOG000280688.
HOVERGENHBG006384.
InParanoidO15427.
KOK08180.
OMAGNFFCIR.
PhylomeDBO15427.
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

ArrayExpressO15427.
BgeeO15427.
CleanExHS_SLC16A3.
GenevestigatorO15427.

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

ChiTaRSSLC16A3. human.
GeneWikiSLC16A3.
GenomeRNAi9123.
NextBio34193.
PROO15427.
SOURCESearch...

Entry information

Entry nameMOT4_HUMAN
AccessionPrimary (citable) accession number: O15427
Secondary accession number(s): B3KXG8, Q2M1P8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: July 9, 2014
This is version 119 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 chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM