O95907 (MOT3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Monocarboxylate transporter 3
Short name=MCT 3

Alternative name(s):
Solute carrier family 16 member 8

Gene names

Name:	SLC16A8
Synonyms:	MCT3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	504 AA.
Sequence status	Complete.
Protein existence	Evidence 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]

Ontologies

Keywords
Biological process	Symport Transport
Cellular component	Cell membrane Membrane
Coding sequence diversity	Polymorphism
Domain	Transmembrane Transmembrane helix
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Traceable author statement. Source: Reactome leukocyte migration Traceable author statement. Source: Reactome pyruvate metabolic process Traceable author statement. Source: Reactome
Cellular_component	integral to plasma membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	lactate transmembrane transporter activity Traceable author statement Ref.1. Source: ProtInc 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 504	504	Monocarboxylate transporter 3		PRO_0000211390
Regions
	Topological domain	1 – 14	14	Cytoplasmic Potential
	Transmembrane	15 – 35	21	Helical; Potential
	Topological domain	36 – 58	23	Extracellular Potential
	Transmembrane	59 – 79	21	Helical; Potential
	Topological domain	80 – 85	6	Cytoplasmic Potential
	Transmembrane	86 – 106	21	Helical; Potential
	Topological domain	107 – 115	9	Extracellular Potential
	Transmembrane	116 – 136	21	Helical; Potential
	Topological domain	137 – 143	7	Cytoplasmic Potential
	Transmembrane	144 – 164	21	Helical; Potential
	Topological domain	165 – 172	8	Extracellular Potential
	Transmembrane	173 – 193	21	Helical; Potential
	Topological domain	194 – 254	61	Cytoplasmic Potential
	Transmembrane	255 – 275	21	Helical; Potential
	Topological domain	276 – 289	14	Extracellular Potential
	Transmembrane	290 – 310	21	Helical; Potential
	Topological domain	311 – 318	8	Cytoplasmic Potential
	Transmembrane	319 – 335	17	Helical; Potential
	Topological domain	336 – 342	7	Extracellular Potential
	Transmembrane	343 – 363	21	Helical; Potential
	Topological domain	364 – 376	13	Cytoplasmic Potential
	Transmembrane	377 – 397	21	Helical; Potential
	Topological domain	398 – 410	13	Extracellular Potential
	Transmembrane	411 – 431	21	Helical; Potential
	Topological domain	432 – 504	73	Cytoplasmic Potential
Natural variations
	Natural variant	235	1	R → W. Ref.1 Corresponds to variant rs4289289 [ dbSNP | Ensembl ].		VAR_060107
	Natural variant	405	1	V → A. Ref.1 Corresponds to variant rs2076371 [ dbSNP | Ensembl ].		VAR_053654

Sequences

	Sequence		Length	Mass (Da)
	O95907 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: E924D4FC31340398	FASTA	504	52,319
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00296004.
RefSeq	NP_037488.2. NM_013356.2.
UniGene	Hs.270285.
3D structure databases
ProteinModelPortal	O95907.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95907. 2 interactions.
MINT	MINT-1429542.
STRING	9606.ENSP00000321735.
Protein family/group databases
TCDB	2.A.1.13.9. major facilitator superfamily (MFS).
PTM databases
PhosphoSite	O95907.
Proteomic databases
PaxDb	O95907.
PRIDE	O95907.
Protocols and materials databases
DNASU	23539.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000320521; ENSP00000321735; ENSG00000100156.
GeneID	23539.
KEGG	hsa:23539.
UCSC	uc003auu.3. human.
Organism-specific databases
CTD	23539.
GeneCards	GC22M038474.
H-InvDB	HIX0041123.
HGNC	HGNC:16270. SLC16A8.
MIM	610409. gene.
neXtProt	NX_O95907.
PharmGKB	PA38106.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG297999.
HOGENOM	HOG000280688.
HOVERGEN	HBG006384.
InParanoid	O95907.
KO	K08185.
OMA	CAKAAPS.
OrthoDB	EOG4CVG77.
PhylomeDB	O95907.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15518. Transmembrane transport of small molecules. REACT_20633. Bile salt and organic anion SLC transporters. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	O95907.
Bgee	O95907.
CleanEx	HS_SLC16A8.
Genevestigator	O95907.
GermOnline	ENSG00000100156. Homo sapiens.
Family and domain databases
InterPro	IPR011701. MFS. IPR020846. MFS_dom. IPR016196. MFS_dom_general_subst_transpt. IPR004743. Monocarb_transpt. [Graphical view]
Pfam	PF07690. MFS_1. 1 hit. [Graphical view]
SUPFAM	SSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMs	TIGR00892. 2A0113. 1 hit.
PROSITE	PS50850. MFS. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00119. Pyruvic acid.
GenomeRNAi	23539.
NextBio	46042.
SOURCE	Search...

Entry information

Entry name

MOT3_HUMAN

Accession

Primary (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:	April 3, 2013
This is version 100 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.