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O88909

- S22A8_MOUSE

UniProt

O88909 - S22A8_MOUSE

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Protein

Solute carrier family 22 member 8

Gene

Slc22a8

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

Functioni

Plays an important role in the excretion/detoxification of endogenous and exogenous organic anions, especially from the brain and kidney. Mediates the uptake of p-amino-hippurate (PAH) and estron sulfate (ES). Also mediates uptake of several organic compounds such as prostaglandin E2, prostaglandin F(2-alpha), allopurinol, 6-mercaptopurine (6-MP), 5-fluorouracil (5-FU), and L-carnitine.3 Publications

GO - Molecular functioni

  1. inorganic anion exchanger activity Source: Ensembl
  2. organic anion transmembrane transporter activity Source: Ensembl
  3. quaternary ammonium group transmembrane transporter activity Source: Ensembl

GO - Biological processi

  1. glutathione transport Source: Ensembl
  2. response to methotrexate Source: Ensembl
  3. response to toxic substance Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Detoxification, Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_198604. Organic anion transport.

Protein family/group databases

TCDBi2.A.1.19.9. the major facilitator superfamily (mfs).

Names & Taxonomyi

Protein namesi
Recommended name:
Solute carrier family 22 member 8
Alternative name(s):
Organic anion transporter 3
Short name:
mOat3
Reduced in osteosclerosis transporter
Gene namesi
Name:Slc22a8
Synonyms:Oat3, Roct
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 19

Organism-specific databases

MGIiMGI:1336187. Slc22a8.

Subcellular locationi

Basolateral cell membrane Curated; Multi-pass membrane protein Curated
Note: Localizes on the brush border membrane of the choroid epithelial cells. Localizes to the basolateral membrane of the proximal tubular cells. Localizes on the abluminal and possibly, luminal membrane of the brain capillary endothelial cells (BCEC) (By similarity).By similarity

GO - Cellular componenti

  1. basolateral plasma membrane Source: Ensembl
  2. extracellular vesicular exosome Source: Ensembl
  3. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice appear healthly and are fertile. Exhibit a loss of taurocholate, estrone sulfate and para-aminohippurate transport in kidney and of fluorescein (FL) transport in choroid plexus.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 537537Solute carrier family 22 member 8PRO_0000273441Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi81 – 811N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiO88909.

Expressioni

Tissue specificityi

Highly expressed in kidney. Expressed in developing bone. Weakly expressed in brain and eye.2 Publications

Gene expression databases

BgeeiO88909.
GenevestigatoriO88909.

Structurei

3D structure databases

ProteinModelPortaliO88909.
SMRiO88909. Positions 117-449.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 1111CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini33 – 12391ExtracellularSequence AnalysisAdd
BLAST
Topological domaini145 – 1506CytoplasmicSequence Analysis
Topological domaini172 – 1765ExtracellularSequence Analysis
Topological domaini198 – 21215CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini234 – 2363ExtracellularSequence Analysis
Topological domaini258 – 32770CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini349 – 3546ExtracellularSequence Analysis
Topological domaini376 – 3838CytoplasmicSequence Analysis
Topological domaini405 – 4117ExtracellularSequence Analysis
Topological domaini433 – 47139CytoplasmicSequence AnalysisAdd
BLAST
Topological domaini493 – 53745ExtracellularSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei12 – 3221HelicalSequence AnalysisAdd
BLAST
Transmembranei124 – 14421HelicalSequence AnalysisAdd
BLAST
Transmembranei151 – 17121HelicalSequence AnalysisAdd
BLAST
Transmembranei177 – 19721HelicalSequence AnalysisAdd
BLAST
Transmembranei213 – 23321HelicalSequence AnalysisAdd
BLAST
Transmembranei237 – 25721HelicalSequence AnalysisAdd
BLAST
Transmembranei328 – 34821HelicalSequence AnalysisAdd
BLAST
Transmembranei355 – 37521HelicalSequence AnalysisAdd
BLAST
Transmembranei384 – 40421HelicalSequence AnalysisAdd
BLAST
Transmembranei412 – 43221HelicalSequence AnalysisAdd
BLAST
Transmembranei472 – 49221HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG0477.
GeneTreeiENSGT00760000118852.
HOGENOMiHOG000234569.
HOVERGENiHBG108433.
InParanoidiO88909.
KOiK08205.
OMAiDGWVYNS.
OrthoDBiEOG7C8GH9.
PhylomeDBiO88909.
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.

O88909-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTFSEILDRV GSMGPFQYLH VTLLALPILG IANHNLLQIF TATTPDHHCR
60 70 80 90 100
PPPNASLEPW VLPLGPNGKP EKCLRFVHLP NASLPNDTQG ATEPCLDGWI
110 120 130 140 150
YNSTRDTIVT EWDLVCGSNK LKEMAQSVFM AGILVGGPVF GELSDRFGRK
160 170 180 190 200
PILTWSYLLL AASGSSAAFS PSLTVYMIFR FLCGCSISGI SLSTIILNVE
210 220 230 240 250
WVPTSTRAIS STTIGYCYTI GQFILPGLAY AVPQWRWLQL SVSAAFFIFS
260 270 280 290 300
LLSWWVPESI RWLVLSGKFS KALKTLQRVA TFNGKKEEGE KLTVEELKFN
310 320 330 340 350
LQKDITSAKV KYGLSDLFRV SILRRVTFCL SLAWFATGFA YYSLAMGVEE
360 370 380 390 400
FGVNIYILQI IFGGVDIPAK FITILSISYL GRRITQGFLL ILAGVAILAL
410 420 430 440 450
IFVSSEMQLL RTALAVFGKG CLSGSFSCLF LYTSELYPTV LRQTGMGISN
460 470 480 490 500
IWARVGSMIA PLVKITGELQ PFIPNVIFGT MTLLGGSAAF FLLETLNRPL
510 520 530
PETIEDIQDW YQQTKKTKQE PEAEKASQTI PLKTGGP
Length:537
Mass (Da):59,246
Last modified:January 23, 2007 - v2
Checksum:iF85FF82002AB26EB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti271 – 2711K → R in AAC61265. (PubMed:10087192)Curated
Sequence conflicti479 – 4791G → V in BAC27624. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078869 mRNA. Translation: AAC61265.1.
AK031962 mRNA. Translation: BAC27624.1.
AK044336 mRNA. Translation: BAC31873.1.
AK157891 mRNA. Translation: BAE34249.1.
BC014762 mRNA. Translation: AAH14762.1.
AB079895 mRNA. Translation: BAC53618.1.
CCDSiCCDS29537.1.
RefSeqiNP_001158106.1. NM_001164634.1.
NP_001158107.1. NM_001164635.1.
NP_112471.3. NM_031194.5.
UniGeneiMm.285294.

Genome annotation databases

EnsembliENSMUST00000010251; ENSMUSP00000010251; ENSMUSG00000063796.
ENSMUST00000170817; ENSMUSP00000131045; ENSMUSG00000063796.
GeneIDi19879.
KEGGimmu:19879.
UCSCiuc008gmc.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF078869 mRNA. Translation: AAC61265.1 .
AK031962 mRNA. Translation: BAC27624.1 .
AK044336 mRNA. Translation: BAC31873.1 .
AK157891 mRNA. Translation: BAE34249.1 .
BC014762 mRNA. Translation: AAH14762.1 .
AB079895 mRNA. Translation: BAC53618.1 .
CCDSi CCDS29537.1.
RefSeqi NP_001158106.1. NM_001164634.1.
NP_001158107.1. NM_001164635.1.
NP_112471.3. NM_031194.5.
UniGenei Mm.285294.

3D structure databases

ProteinModelPortali O88909.
SMRi O88909. Positions 117-449.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2073672.

Protein family/group databases

TCDBi 2.A.1.19.9. the major facilitator superfamily (mfs).

Proteomic databases

PRIDEi O88909.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000010251 ; ENSMUSP00000010251 ; ENSMUSG00000063796 .
ENSMUST00000170817 ; ENSMUSP00000131045 ; ENSMUSG00000063796 .
GeneIDi 19879.
KEGGi mmu:19879.
UCSCi uc008gmc.2. mouse.

Organism-specific databases

CTDi 9376.
MGIi MGI:1336187. Slc22a8.

Phylogenomic databases

eggNOGi COG0477.
GeneTreei ENSGT00760000118852.
HOGENOMi HOG000234569.
HOVERGENi HBG108433.
InParanoidi O88909.
KOi K08205.
OMAi DGWVYNS.
OrthoDBi EOG7C8GH9.
PhylomeDBi O88909.
TreeFami TF315847.

Enzyme and pathway databases

Reactomei REACT_198604. Organic anion transport.

Miscellaneous databases

NextBioi 297374.
PROi O88909.
SOURCEi Search...

Gene expression databases

Bgeei O88909.
Genevestigatori O88909.

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. "A novel putative transporter maps to the osteosclerosis (oc) mutation and is not expressed in the oc mutant mouse."
    Brady K.P., Dushkin H., Foernzler D., Koike T., Magner F., Her H., Gullans S., Segre G.V., Green R.M., Beier D.R.
    Genomics 56:254-261(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    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: Inner ear, Medulla oblongata and Retina.
  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: Kidney.
  4. "Cloning and functional characterization of mOAT3 (Roct)."
    Kobayashi Y., Shibusawa A., Ohshiro N., Sasaki T., Tokuyama S., Yamamoto T.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 13-537.
    Tissue: Kidney.
  5. "Impaired organic anion transport in kidney and choroid plexus of organic anion transporter 3 (Oat3 (Slc22a8)) knockout mice."
    Sweet D.H., Miller D.S., Pritchard J.B., Fujiwara Y., Beier D.R., Nigam S.K.
    J. Biol. Chem. 277:26934-26943(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  6. "Organic anion transport in choroid plexus from wild-type and organic anion transporter 3 (Slc22a8)-null mice."
    Sykes D., Sweet D.H., Lowes S., Nigam S.K., Pritchard J.B., Miller D.S.
    Am. J. Physiol. 286:F972-F978(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Renal transport of organic compounds mediated by mouse organic anion transporter 3 (mOat3): further substrate specificity of mOat3."
    Kobayashi Y., Ohshiro N., Tsuchiya A., Kohyama N., Ohbayashi M., Yamamoto T.
    Drug Metab. Dispos. 32:479-483(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiS22A8_MOUSE
AccessioniPrimary (citable) accession number: O88909
Secondary accession number(s): Q3TZF9
, Q8CCX3, Q8CFH5, Q91WJ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 100 of the entry and version 2 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