Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8R0M8 (MOT5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Monocarboxylate transporter 5

Short name=MCT 5
Gene names
Name:Slc16a4
Synonyms:Mct5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length500 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 By similarity.

Sequence similarities

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

Ontologies

Keywords
   Biological processSymport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionsymporter activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8R0M8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8R0M8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     451-500: GWIYDYTQTYTGSFYFSGTCYILSSVSLFFVPLAERWKRKQSDLLRTTIK → DVTHGWTTYLMHMKPLKT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q8R0M8-3)

The sequence of this isoform differs from the canonical sequence as follows:
     350-500: ITETVSQLIS...QSDLLRTTIK → KKNELSLIKVY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Monocarboxylate transporter 5
PRO_0000416125

Regions

Topological domain1 – 1616Cytoplasmic Potential
Transmembrane17 – 3721Helical; Potential
Topological domain38 – 5821Extracellular Potential
Transmembrane59 – 7921Helical; Potential
Topological domain80 – 878Cytoplasmic Potential
Transmembrane88 – 10821Helical; Potential
Topological domain1091Extracellular Potential
Transmembrane110 – 12920Helical; Potential
Topological domain130 – 15324Cytoplasmic Potential
Transmembrane154 – 17421Helical; Potential
Topological domain1751Extracellular Potential
Transmembrane176 – 19520Helical; Potential
Topological domain196 – 304109Cytoplasmic Potential
Transmembrane305 – 32521Helical; Potential
Topological domain326 – 34217Extracellular Potential
Transmembrane343 – 36321Helical; Potential
Topological domain364 – 37411Cytoplasmic Potential
Transmembrane375 – 39521Helical; Potential
Topological domain3961Extracellular Potential
Transmembrane397 – 41620Helical; Potential
Topological domain417 – 43014Cytoplasmic Potential
Transmembrane431 – 45121Helical; Potential
Topological domain452 – 46312Extracellular Potential
Transmembrane464 – 48421Helical; Potential
Topological domain485 – 50016Cytoplasmic Potential

Natural variations

Alternative sequence350 – 500151ITETV…RTTIK → KKNELSLIKVY in isoform 3.
VSP_042510
Alternative sequence451 – 50050GWIYD…RTTIK → DVTHGWTTYLMHMKPLKT in isoform 2.
VSP_042511

Experimental info

Sequence conflict3661N → D in BAC32495. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 80B0FFF7D0C652E7

FASTA50055,678
        10         20         30         40         50         60 
MVKKEKTPSP YTKPLDGGWG WMVVLHFFLV NVFVMGMTKT FAIFFVVFQE EFEGTSEQIG 

        70         80         90        100        110        120 
WIGSIMSSLR FSAGPLAAII CDVLGEKATS ILGTFLVSGG YVISSWATGI PFLCVTMGLL 

       130        140        150        160        170        180 
PGLGSAFLYQ VAAVVITKYF KKRLGLSTAI ARSGMGLTFL LAPFTKFLID LYDWTGALIL 

       190        200        210        220        230        240 
FGAIILNLVP SSMLLRPIHS QSNNNSDIEN KGSILSATEP EASYKTETSK CKETQEPFIK 

       250        260        270        280        290        300 
DSTMKKSEQP TTTLTVLGNQ SEEFSNRPHR NRPLLMSNGK SHKKKFVSWN CKQKLLDISL 

       310        320        330        340        350        360 
FRNPFFYIFT WSFLLSQLAY FIPTFHLVAR AKTLGIDVMD ASYLVSVAGI TETVSQLISG 

       370        380        390        400        410        420 
WIADQNWIKK YQYHKSYLIL CGVTNLLAPL ATTFPLLMAY TILFAIFAGG YLALILPVLV 

       430        440        450        460        470        480 
DLSKNSRVHK FLGYASFFAG IAVLSGPPIA GWIYDYTQTY TGSFYFSGTC YILSSVSLFF 

       490        500 
VPLAERWKRK QSDLLRTTIK 

« Hide

Isoform 2 [UniParc].

Checksum: 7FF2E4895F05836F
Show »

FASTA46851,899
Isoform 3 [UniParc].

Checksum: 423DCF37A5728068
Show »

FASTA36040,028

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
Strain: C57BL/6J.
Tissue: Corpora quadrigemina, Diencephalon, Hippocampus and Kidney.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[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] (ISOFORMS 1 AND 2).
Strain: FVB/N.
Tissue: Kidney.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK045797 mRNA. Translation: BAC32495.1.
AK049873 mRNA. Translation: BAC33967.1.
AK052779 mRNA. Translation: BAC35143.1.
AK085492 mRNA. Translation: BAC39456.1.
AK136837 mRNA. Translation: BAE23142.1.
AC132405 Genomic DNA. No translation available.
CH466607 Genomic DNA. Translation: EDL01900.1.
BC025441 mRNA. Translation: AAH25441.1.
BC026596 mRNA. Translation: AAH26596.1.
RefSeqNP_666248.1. NM_146136.1.
UniGeneMm.38384.

3D structure databases

ProteinModelPortalQ8R0M8.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ8R0M8.

Proteomic databases

PRIDEQ8R0M8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029502; ENSMUSP00000029502; ENSMUSG00000027896. [Q8R0M8-1]
ENSMUST00000106723; ENSMUSP00000102334; ENSMUSG00000027896. [Q8R0M8-2]
GeneID229699.
KEGGmmu:229699.
UCSCuc008qwx.1. mouse. [Q8R0M8-3]
uc008qwy.2. mouse. [Q8R0M8-1]

Organism-specific databases

CTD9122.
MGIMGI:2385183. Slc16a4.

Phylogenomic databases

GeneTreeENSGT00740000114926.
HOGENOMHOG000059591.
HOVERGENHBG006385.
InParanoidQ8R0M8.
KOK08181.
OMAAVVITKY.
OrthoDBEOG7NGQBB.
PhylomeDBQ8R0M8.
TreeFamTF313792.

Gene expression databases

BgeeQ8R0M8.
GenevestigatorQ8R0M8.

Family and domain databases

InterProIPR011701. MFS.
IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
[Graphical view]
PfamPF07690. MFS_1. 1 hit.
[Graphical view]
SUPFAMSSF103473. SSF103473. 2 hits.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio379615.
PROQ8R0M8.
SOURCESearch...

Entry information

Entry nameMOT5_MOUSE
AccessionPrimary (citable) accession number: Q8R0M8
Secondary accession number(s): Q8BLA5, Q8BWE3, Q8R157
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: June 1, 2002
Last modified: April 16, 2014
This is version 88 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot