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Q8VC69

- S22A6_MOUSE

UniProt

Q8VC69 - S22A6_MOUSE

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Protein

Solute carrier family 22 member 6

Gene

Slc22a6

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

Functioni

Involved in the renal elimination of endogenous and exogenous organic anions. Functions as organic anion exchanger when the uptake of one molecule of organic anion is coupled with an efflux of one molecule of endogenous dicarboxylic acid (glutarate, ketoglutarate, etc). Mediates the sodium-independent uptake of 2,3-dimercapto-1-propanesulfonic acid (DMPS), cidofovir, adefovir, 9-(2-phosphonylmethoxyethyl) guanine (PMEG), 9-(2-phosphonylmethoxyethyl) diaminopurine (PMEDAP), ochratoxin (OTA), acyclovir (ACV), 3'-azido-3-'deoxythymidine (AZT), cimetidine (CMD), 2,4-dichloro-phenoxyacetate (2,4-D), hippurate (HA), indoleacetate (IA), indoxyl sulfate (IS) and 3-carboxy-4-methyl-5-propyl-2-furanpropionate (CMPF) and edaravone sulfate By similarity. Mediates the sodium-independent uptake of p-aminohippurate (PAH). PAH uptake is inhibited by benzothiazolylcysteine (BTC), S-chlorotrifluoroethylcysteine (CTFC), cysteine S-conjugates S-dichlorovinylcysteine (DCVC), furosemide, steviol, phorbol 12-myristate 13-acetate (PMA), calcium ionophore A23187, benzylpenicillin, bumetamide, losartan, probenecid, phenol red, urate, glutarate and alpha-ketoglutarate By similarity. PAH uptake is inhibited by p-chloromercuribenzenesulphonate (PCMBS), diethyl pyrocarbonate (DEPC), indomethacin, sulindac, diclofenac, carprofen, okadaic acid and PKC activators.By similarity3 Publications

Kineticsi

  1. KM=37.3 µM for PAH1 Publication

Vmax=210 pmol/min/mg enzyme for PAH uptake1 Publication

GO - Molecular functioni

  1. chloride ion binding Source: Ensembl
  2. inorganic anion exchanger activity Source: UniProtKB
  3. organic anion transmembrane transporter activity Source: UniProtKB
  4. sodium-independent organic anion transmembrane transporter activity Source: Ensembl

GO - Biological processi

  1. alpha-ketoglutarate transport Source: UniProtKB
  2. anion transport Source: MGI
  3. organic anion transport Source: UniProtKB
  4. protein homooligomerization Source: Ensembl
  5. renal tubular secretion Source: UniProtKB
  6. response to methotrexate Source: Ensembl
  7. sodium-independent organic anion transport Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_198604. Organic anion transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 22 member 6
Alternative name(s):
Kidney-specific transport protein
Novel kidney transcript
Short name:
mNKT
Organic anion transporter 1
Renal organic anion transporter 1
Short name:
mROAT1
Gene namesi
Name:Slc22a6
Synonyms:Nkt, Oat1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:892001. Slc22a6.

Subcellular locationi

Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication
Note: Localized to the plasma membrane.

GO - Cellular componenti

  1. basolateral plasma membrane Source: UniProtKB
  2. caveola Source: Ensembl
  3. extracellular vesicular exosome Source: Ensembl
  4. integral component of plasma membrane Source: UniProtKB
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi39 – 391N → Q: Complete loss of PAH transport activity. 1 Publication
Mutagenesisi49 – 491C → A: Decrease in the level of cell surface expression and transport function. Complete loss of transport function; when associated with A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434. 1 Publication
Mutagenesisi122 – 1221C → A: Decrease in the level of cell surface expression and transport function. Complete loss of transport function; when associated with A-49; A-78; A-99; A-172; A-183; A-200; A-362; A-335; A-379; A-402; A-427 and A-434. 1 Publication
Mutagenesisi183 – 1831C → A: Decrease in the level of cell surface expression and transport function. Complete loss of transport function; when associated with A-49; A-78; A-99; A-122; A-172; A-200; A-362; A-335; A-379; A-402; A-427 and A-434. 1 Publication
Mutagenesisi434 – 4341C → A: Decrease in the level of cell surface expression and transport function. 80% decrease in the level of transport activity; when associated with A-49; A-122 and A-183. Complete loss of transport function; when associated with A-49; A-78; A-99; A-122; A-172; A-183; A-200; A-362; A-335; A-379; A-402 and A-427. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 545545Solute carrier family 22 member 6PRO_0000324168Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi56 – 561N-linked (GlcNAc...)1 Publication
Glycosylationi86 – 861N-linked (GlcNAc...)1 Publication
Glycosylationi91 – 911N-linked (GlcNAc...)1 Publication
Glycosylationi107 – 1071N-linked (GlcNAc...)1 Publication
Glycosylationi178 – 1781N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Glycosylated. Glycosylation is necessary for proper targeting of the transporter to the plasma membrane.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8VC69.
PaxDbiQ8VC69.
PRIDEiQ8VC69.

Expressioni

Tissue specificityi

Expressed in kidney; in the basolateral membrane and at much lower levels in brain.2 Publications

Developmental stagei

Developmentally regulated with significant expression beginning at E18 and rising just before birth.

Gene expression databases

BgeeiQ8VC69.
GenevestigatoriQ8VC69.

Interactioni

Structurei

3D structure databases

ProteinModelPortaliQ8VC69.
SMRiQ8VC69. Positions 133-503.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 99CytoplasmicSequence Analysis
Topological domaini31 – 12999ExtracellularSequence AnalysisAdd
BLAST
Topological domaini151 – 1577CytoplasmicSequence Analysis
Topological domaini178 – 1803ExtracellularSequence Analysis
Topological domaini202 – 21817CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini240 – 2423ExtracellularSequence Analysis
Topological domaini264 – 33168CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini353 – 36210ExtracellularSequence Analysis
Topological domaini384 – 3896CytoplasmicSequence Analysis
Topological domaini411 – 4199ExtracellularSequence Analysis
Topological domaini441 – 45010CytoplasmicSequence Analysis
Topological domaini472 – 4787ExtracellularSequence Analysis
Topological domaini500 – 54546CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei10 – 3021HelicalSequence AnalysisAdd
BLAST
Transmembranei130 – 15021HelicalSequence AnalysisAdd
BLAST
Transmembranei158 – 17720HelicalSequence AnalysisAdd
BLAST
Transmembranei181 – 20121HelicalSequence AnalysisAdd
BLAST
Transmembranei219 – 23921HelicalSequence AnalysisAdd
BLAST
Transmembranei243 – 26321HelicalSequence AnalysisAdd
BLAST
Transmembranei332 – 35221HelicalSequence AnalysisAdd
BLAST
Transmembranei363 – 38321HelicalSequence AnalysisAdd
BLAST
Transmembranei390 – 41021HelicalSequence AnalysisAdd
BLAST
Transmembranei420 – 44021HelicalSequence AnalysisAdd
BLAST
Transmembranei451 – 47121HelicalSequence AnalysisAdd
BLAST
Transmembranei479 – 49921HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domaini

Multiple cysteine residues are necessary for proper targeting to the plasma membrane.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000118852.
HOGENOMiHOG000234569.
HOVERGENiHBG108433.
InParanoidiQ8VC69.
KOiK08203.
OMAiMIRQTGM.
OrthoDBiEOG7C8GH9.
PhylomeDBiQ8VC69.
TreeFamiTF315847.

Family and domain databases

InterProiIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005828. Sub_transporter.
[Graphical view]
PfamiPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMiSSF103473. SSF103473. 1 hit.
TIGRFAMsiTIGR00898. 2A0119. 1 hit.
PROSITEiPS50850. MFS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8VC69-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAFNDLLKQV GGVGRFQLIQ VTMVVAPLLL MASHNTLQNF TAAIPAHHCR
60 70 80 90 100
PPANANLSKD GGLEAWLPLD KQGRPESCLR FPFPHNGTEA NGTGVTEPCL
110 120 130 140 150
DGWVYDNSTF PSTIVTEWNL VCSHRAFRQL AQSLFMVGVL LGAMMFGYLA
160 170 180 190 200
DRLGRRKVLI LNYLQTAVSG TCAAYAPNYT VYCIFRLLSG MSLASIAINC
210 220 230 240 250
MTLNMEWMPI HTRAYVGTLI GYVYSLGQFL LAGIAYAVPH WRHLQLAVSV
260 270 280 290 300
PFFVAFIYSW FFIESARWYS SSGRLDLTLR ALQRVARING KQEEGAKLSI
310 320 330 340 350
EVLQTSLQKE LTLNKGQASA MELLRCPTLR RLFLCLSMLW FATSFAYYGL
360 370 380 390 400
VMDLQGFGVS MYLIQVIFGA VDLPAKFVCF LVINSMGRRP AQLASLLLAG
410 420 430 440 450
ICILVNGIIP RGHTIIRTSL AVLGKGCLAS SFNCIFLYTG ELYPTMIRQT
460 470 480 490 500
GLGMGSTMAR VGSIVSPLIS MTAEFYPSIP LFIFGAVPVA ASAVTALLPE
510 520 530 540
TLGQPLPDTV QDLKSRSRGK QKQQQLEQQK QMIPLQVSTQ EKNGL
Length:545
Mass (Da):60,013
Last modified:March 1, 2002 - v1
Checksum:i827782E115705C77
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti66 – 661W → R in AAC53112. (PubMed:9045672)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52842 mRNA. Translation: AAC53112.1.
AK035971 mRNA. Translation: BAC29261.1.
BC021647 mRNA. Translation: AAH21647.1.
CCDSiCCDS29538.1.
RefSeqiNP_032792.2. NM_008766.3.
UniGeneiMm.30090.

Genome annotation databases

EnsembliENSMUST00000010250; ENSMUSP00000010250; ENSMUSG00000024650.
GeneIDi18399.
KEGGimmu:18399.
UCSCiuc008gme.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U52842 mRNA. Translation: AAC53112.1 .
AK035971 mRNA. Translation: BAC29261.1 .
BC021647 mRNA. Translation: AAH21647.1 .
CCDSi CCDS29538.1.
RefSeqi NP_032792.2. NM_008766.3.
UniGenei Mm.30090.

3D structure databases

ProteinModelPortali Q8VC69.
SMRi Q8VC69. Positions 133-503.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi Q8VC69.
ChEMBLi CHEMBL5653.

Proteomic databases

MaxQBi Q8VC69.
PaxDbi Q8VC69.
PRIDEi Q8VC69.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000010250 ; ENSMUSP00000010250 ; ENSMUSG00000024650 .
GeneIDi 18399.
KEGGi mmu:18399.
UCSCi uc008gme.2. mouse.

Organism-specific databases

CTDi 9356.
MGIi MGI:892001. Slc22a6.

Phylogenomic databases

eggNOGi COG0477.
GeneTreei ENSGT00760000118852.
HOGENOMi HOG000234569.
HOVERGENi HBG108433.
InParanoidi Q8VC69.
KOi K08203.
OMAi MIRQTGM.
OrthoDBi EOG7C8GH9.
PhylomeDBi Q8VC69.
TreeFami TF315847.

Enzyme and pathway databases

Reactomei REACT_198604. Organic anion transport.

Miscellaneous databases

ChiTaRSi SLC22A6. mouse.
NextBioi 294008.
PROi Q8VC69.
SOURCEi Search...

Gene expression databases

Bgeei Q8VC69.
Genevestigatori Q8VC69.

Family and domain databases

InterProi IPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005828. Sub_transporter.
[Graphical view ]
Pfami PF00083. Sugar_tr. 1 hit.
[Graphical view ]
SUPFAMi SSF103473. SSF103473. 1 hit.
TIGRFAMsi TIGR00898. 2A0119. 1 hit.
PROSITEi PS50850. MFS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of NKT, a gene product related to the organic cation transporter family that is almost exclusively expressed in the kidney."
    Lopez-Nieto C.E., You G., Bush K.T., Barros E.J., Beier D.R., Nigam S.K.
    J. Biol. Chem. 272:6471-6478(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, MUTAGENESIS OF CYS-49; CYS-78; CYS-99; CYS-122; CYS-172; CYS-183; CYS-200; CYS-326; CYS-335; CYS-379; CYS-402; CYS-427 AND CYS-434, SUBCELLULAR LOCATION.
    Strain: BALB/c.
    Tissue: Kidney.
  2. "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].
    Strain: C57BL/6J.
    Tissue: Cerebellum.
  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].
    Strain: FVB/N.
    Tissue: Liver.
  4. "Heterologous expression and functional characterization of a mouse renal organic anion transporter in mammalian cells."
    Kuze K., Graves P., Leahy A., Wilson P., Stuhlmann H., You G.
    J. Biol. Chem. 274:1519-1524(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
  5. "Regulation of mOAT-mediated organic anion transport by okadaic acid and protein kinase C in LLC-PK(1) cells."
    You G., Kuze K., Kohanski R.A., Amsler K., Henderson S.
    J. Biol. Chem. 275:10278-10284(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Cysteine residues in the organic anion transporter mOAT1."
    Tanaka K., Zhou F., Kuze K., You G.
    Biochem. J. 380:283-287(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Role of glycosylation in the organic anion transporter OAT1."
    Tanaka K., Xu W., Zhou F., You G.
    J. Biol. Chem. 279:14961-14966(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASN-39, GLYCOSYLATION AT ASN-56; ASN-86; ASN-91 AND ASN-107.

Entry informationi

Entry nameiS22A6_MOUSE
AccessioniPrimary (citable) accession number: Q8VC69
Secondary accession number(s): Q61185
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: March 1, 2002
Last modified: October 29, 2014
This is version 107 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

External Data

Dasty 3