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Protein

Sodium-coupled monocarboxylate transporter 2

Gene

Slc5a12

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an electroneutral and low-affinity sodium (Na+)-dependent sodium-coupled solute transporter. Catalyzes the transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, nicotinate, propionate, butyrate and beta-D-hydroxybutyrate. May be responsible for the first step of reabsorption of monocarboxylates from the lumen of the proximal tubule of the kidney and the small intestine. May play also a role in monocarboxylates transport in the retina. Mediates electroneutral uptake of lactate, with a stoichiometry of 2 Na+ for each lactate.2 Publications

GO - Molecular functioni

  • lactate transmembrane transporter activity Source: CACAO
  • symporter activity Source: UniProtKB-KW

GO - Biological processi

  • lactate transmembrane transport Source: GOC
  • sodium ion transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Ion transport, Sodium transport, Symport, Transport

Keywords - Ligandi

Sodium

Names & Taxonomyi

Protein namesi
Recommended name:
Sodium-coupled monocarboxylate transporter 2
Alternative name(s):
Electroneutral sodium monocarboxylate cotransporter
Low-affinity sodium-lactate cotransporter
Solute carrier family 5 member 12
Gene namesi
Name:Slc5a12
Synonyms:Smct2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2138890. Slc5a12.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99ExtracellularSequence analysis
Transmembranei10 – 3021HelicalSequence analysisAdd
BLAST
Topological domaini31 – 4717CytoplasmicSequence analysisAdd
BLAST
Transmembranei48 – 6821HelicalSequence analysisAdd
BLAST
Topological domaini69 – 8012ExtracellularSequence analysisAdd
BLAST
Transmembranei81 – 10121HelicalSequence analysisAdd
BLAST
Topological domaini102 – 12827CytoplasmicSequence analysisAdd
BLAST
Transmembranei129 – 14921HelicalSequence analysisAdd
BLAST
Topological domaini150 – 1578ExtracellularSequence analysis
Transmembranei158 – 17821HelicalSequence analysisAdd
BLAST
Topological domaini179 – 1802CytoplasmicSequence analysis
Transmembranei181 – 20121HelicalSequence analysisAdd
BLAST
Topological domaini202 – 23534ExtracellularSequence analysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Topological domaini257 – 27519CytoplasmicSequence analysisAdd
BLAST
Transmembranei276 – 29621HelicalSequence analysisAdd
BLAST
Topological domaini297 – 32125ExtracellularSequence analysisAdd
BLAST
Transmembranei322 – 34221HelicalSequence analysisAdd
BLAST
Topological domaini343 – 38543CytoplasmicSequence analysisAdd
BLAST
Transmembranei386 – 40621HelicalSequence analysisAdd
BLAST
Topological domaini407 – 4115ExtracellularSequence analysis
Transmembranei412 – 43221HelicalSequence analysisAdd
BLAST
Topological domaini433 – 4375CytoplasmicSequence analysis
Transmembranei438 – 45821HelicalSequence analysisAdd
BLAST
Topological domaini459 – 50446ExtracellularSequence analysisAdd
BLAST
Transmembranei505 – 52521HelicalSequence analysisAdd
BLAST
Topological domaini526 – 61994CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 619619Sodium-coupled monocarboxylate transporter 2PRO_0000337681Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence analysis
Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ49B93.
PaxDbiQ49B93.
PRIDEiQ49B93.

PTM databases

iPTMnetiQ49B93.
PhosphoSiteiQ49B93.

Expressioni

Tissue specificityi

Expressed in the cortical region of the kidney corresponding to the proximal tubule. Expressed in Mueller cells of the inner retina (at protein level). Isoform 1 is expressed in the retina, kidney, small intestine and skeletal muscle. Isoform 2 is not detected in the kidney, small intestine and skeletal muscle. In the kidney, expressed predominantly in tubular epithelial cells of the cortical region and in the convoluted portions of the proximal tubule (pars convoluta). In the small intestine, its expression is highest in the proximal part and gradually decreased towards the distal end. Expressed in the neural retina. Not detected in the caecum and colon.4 Publications

Inductioni

Up-regulated by CEBPD.1 Publication

Gene expression databases

BgeeiQ49B93.
ExpressionAtlasiQ49B93. baseline and differential.
GenevisibleiQ49B93. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047340.

Structurei

3D structure databases

ProteinModelPortaliQ49B93.
SMRiQ49B93. Positions 53-460.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2349. Eukaryota.
COG0591. LUCA.
GeneTreeiENSGT00760000118955.
HOGENOMiHOG000261662.
HOVERGENiHBG057280.
InParanoidiQ49B93.
KOiK14388.
OMAiAIADTWY.
OrthoDBiEOG70PBX7.
PhylomeDBiQ49B93.
TreeFamiTF316728.

Family and domain databases

InterProiIPR001734. Na/solute_symporter.
[Graphical view]
PANTHERiPTHR11819. PTHR11819. 1 hit.
PfamiPF00474. SSF. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00813. sss. 1 hit.
PROSITEiPS50283. NA_SOLUT_SYMP_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q49B93-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MRVKNFEAWD YVVFAGLFVI SSGIGVFFAI KERKKTTSRE FLVGGRQMSF
60 70 80 90 100
GPVALSLTAS FMSAVTVLGT PAEVYRFGAS FFLFLISYVF VVFFTSELFL
110 120 130 140 150
PVFYRSGITS TYEYLQLRFN KPVRYAATII YIVQTILYTG VVVYAPALAL
160 170 180 190 200
NQVTGFNLWA SVFATGIVCT FYCSLGGLKA VVWTDAFQMV VMIVGFLTVL
210 220 230 240 250
IQGSNHVGGF NNVLEKAGNG SRLHIVDFDV DPLRRHTFWT ITIGGTFTWL
260 270 280 290 300
GVYGVNQSTI QRCISCKTEK HAKLALYFNL LGLWIIVACA VFSGLIMYSH
310 320 330 340 350
FKDCDPWTSG VISAPDQLMP YFVMEIFATM PGLPGLFVAC AFSGTLSTVA
360 370 380 390 400
ASINALATVT FEDFVKSCFP HLSDKLSTWI SKGLCILFGI MCTSMAVVAS
410 420 430 440 450
LMGSVVQAAL SIHGMCGGPM LGLFTLGLVF PFVNWKGALG GLLTGITLSF
460 470 480 490 500
WVAIGSFIYP APESKTLPLP LSTEHCVELN ITTTVAPQIS SRPVLADTWY
510 520 530 540 550
SLSYLYFSAV GCLGCIAAGI IISFLTGKQR GKDIDPLLIR PVCNLFCFWS
560 570 580 590 600
KKYKTLCWCG VQHDRETEQD YLDSGSAWKQ GVESGLQNGL KQDTLAQIPG
610
YNPKEKSYSN SVPEKTTYF
Length:619
Mass (Da):67,951
Last modified:September 13, 2005 - v1
Checksum:iB1C36211590A511A
GO
Isoform 2 (identifier: Q49B93-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     409-436: ALSIHGMCGGPMLGLFTLGLVFPFVNWK → PGIVSQERAITGSFQRNLASVCYGVSIWKLIM

Note: No experimental confirmation available.
Show »
Length:623
Mass (Da):68,470
Checksum:iD4103BC260819E86
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei409 – 43628ALSIH…FVNWK → PGIVSQERAITGSFQRNLAS VCYGVSIWKLIM in isoform 2. 1 PublicationVSP_033996Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY964639 mRNA. Translation: AAY32930.1.
AF529222 mRNA. Translation: AAQ09530.1.
AK144004 mRNA. Translation: BAE25658.1.
AK165419 mRNA. Translation: BAE38174.1.
AL732495, BX005257 Genomic DNA. Translation: CAM26858.1.
AL732495, BX005257 Genomic DNA. Translation: CAM26859.1.
BX005257, AL732495 Genomic DNA. Translation: CAM27818.1.
BX005257, AL732495 Genomic DNA. Translation: CAM27819.1.
BC121791 mRNA. Translation: AAI21792.1.
CCDSiCCDS16512.1. [Q49B93-2]
CCDS50656.1. [Q49B93-1]
RefSeqiNP_001003915.1. NM_001003915.2. [Q49B93-2]
NP_001171095.1. NM_001177624.1. [Q49B93-1]
UniGeneiMm.277148.

Genome annotation databases

EnsembliENSMUST00000045972; ENSMUSP00000047340; ENSMUSG00000041644. [Q49B93-2]
ENSMUST00000111026; ENSMUSP00000106655; ENSMUSG00000041644. [Q49B93-1]
GeneIDi241612.
KEGGimmu:241612.
UCSCiuc008lmw.2. mouse. [Q49B93-2]
uc008lmx.2. mouse. [Q49B93-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY964639 mRNA. Translation: AAY32930.1.
AF529222 mRNA. Translation: AAQ09530.1.
AK144004 mRNA. Translation: BAE25658.1.
AK165419 mRNA. Translation: BAE38174.1.
AL732495, BX005257 Genomic DNA. Translation: CAM26858.1.
AL732495, BX005257 Genomic DNA. Translation: CAM26859.1.
BX005257, AL732495 Genomic DNA. Translation: CAM27818.1.
BX005257, AL732495 Genomic DNA. Translation: CAM27819.1.
BC121791 mRNA. Translation: AAI21792.1.
CCDSiCCDS16512.1. [Q49B93-2]
CCDS50656.1. [Q49B93-1]
RefSeqiNP_001003915.1. NM_001003915.2. [Q49B93-2]
NP_001171095.1. NM_001177624.1. [Q49B93-1]
UniGeneiMm.277148.

3D structure databases

ProteinModelPortaliQ49B93.
SMRiQ49B93. Positions 53-460.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047340.

PTM databases

iPTMnetiQ49B93.
PhosphoSiteiQ49B93.

Proteomic databases

MaxQBiQ49B93.
PaxDbiQ49B93.
PRIDEiQ49B93.

Protocols and materials databases

DNASUi241612.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045972; ENSMUSP00000047340; ENSMUSG00000041644. [Q49B93-2]
ENSMUST00000111026; ENSMUSP00000106655; ENSMUSG00000041644. [Q49B93-1]
GeneIDi241612.
KEGGimmu:241612.
UCSCiuc008lmw.2. mouse. [Q49B93-2]
uc008lmx.2. mouse. [Q49B93-1]

Organism-specific databases

CTDi159963.
MGIiMGI:2138890. Slc5a12.

Phylogenomic databases

eggNOGiKOG2349. Eukaryota.
COG0591. LUCA.
GeneTreeiENSGT00760000118955.
HOGENOMiHOG000261662.
HOVERGENiHBG057280.
InParanoidiQ49B93.
KOiK14388.
OMAiAIADTWY.
OrthoDBiEOG70PBX7.
PhylomeDBiQ49B93.
TreeFamiTF316728.

Miscellaneous databases

ChiTaRSiSlc5a12. mouse.
NextBioi385076.
PROiQ49B93.
SOURCEiSearch...

Gene expression databases

BgeeiQ49B93.
ExpressionAtlasiQ49B93. baseline and differential.
GenevisibleiQ49B93. MM.

Family and domain databases

InterProiIPR001734. Na/solute_symporter.
[Graphical view]
PANTHERiPTHR11819. PTHR11819. 1 hit.
PfamiPF00474. SSF. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00813. sss. 1 hit.
PROSITEiPS50283. NA_SOLUT_SYMP_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and functional identification of slc5a12 as a sodium-coupled low-affinity transporter for monocarboxylates (SMCT2)."
    Srinivas S.R., Gopal E., Zhuang L., Itagaki S., Martin P.M., Fei Y.-J., Ganapathy V., Prasad P.D.
    Biochem. J. 392:655-664(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, STOICHIOMETRY, TISSUE SPECIFICITY.
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "Sequence of a novel sodium solute cotransporter similar to the Na-iodide transporter."
    Mount D.B.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: C57BL/6J.
  3. "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.
    , 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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Kidney.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  5. "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] OF 2-619 (ISOFORM 1).
  6. "c/ebpdelta null mouse as a model for the double knock-out of slc5a8 and slc5a12 in kidney."
    Thangaraju M., Ananth S., Martin P.M., Roon P., Smith S.B., Sterneck E., Prasad P.D., Ganapathy V.
    J. Biol. Chem. 281:26769-26773(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
  7. "Cloning and functional characterization of human SMCT2 (SLC5A12) and expression pattern of the transporter in kidney."
    Gopal E., Umapathy N.S., Martin P.M., Ananth S., Gnana-Prakasam J.P., Becker H., Wagner C.A., Ganapathy V., Prasad P.D.
    Biochim. Biophys. Acta 1768:2690-2697(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Expression of the sodium-coupled monocarboxylate transporters SMCT1 (SLC5A8) and SMCT2 (SLC5A12) in retina."
    Martin P.M., Dun Y., Mysona B., Ananth S., Roon P., Smith S.B., Ganapathy V.
    Invest. Ophthalmol. Vis. Sci. 48:3356-3363(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: POSSIBLE FUNCTION, TISSUE SPECIFICITY.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiSC5AC_MOUSE
AccessioniPrimary (citable) accession number: Q49B93
Secondary accession number(s): Q0D2G1, Q6A4K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 13, 2005
Last modified: February 17, 2016
This is version 98 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.