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O88909 (S22A8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 86. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Solute carrier family 22 member 8
Alternative name(s):
Organic anion transporter 3
Short name=mOat3
Reduced in osteosclerosis transporter
Gene names
Name:Slc22a8
Synonyms:Oat3, Roct
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length537 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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. Ref.5 Ref.6 Ref.7

Subcellular location

Basolateral cell membrane; Multi-pass membrane protein Potential. 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.

Tissue specificity

Highly expressed in kidney. Expressed in developing bone. Weakly expressed in brain and eye. Ref.1 Ref.7

Disruption phenotype

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. Ref.5

Sequence similarities

Belongs to the major facilitator (TC 2.A.1) superfamily. Organic cation transporter (TC 2.A.1.19) family. [View classification]

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 537537Solute carrier family 22 member 8
PRO_0000273441

Regions

Topological domain1 – 1111Cytoplasmic Potential
Transmembrane12 – 3221Helical; Potential
Topological domain33 – 12391Extracellular Potential
Transmembrane124 – 14421Helical; Potential
Topological domain145 – 1506Cytoplasmic Potential
Transmembrane151 – 17121Helical; Potential
Topological domain172 – 1765Extracellular Potential
Transmembrane177 – 19721Helical; Potential
Topological domain198 – 21215Cytoplasmic Potential
Transmembrane213 – 23321Helical; Potential
Topological domain234 – 2363Extracellular Potential
Transmembrane237 – 25721Helical; Potential
Topological domain258 – 32770Cytoplasmic Potential
Transmembrane328 – 34821Helical; Potential
Topological domain349 – 3546Extracellular Potential
Transmembrane355 – 37521Helical; Potential
Topological domain376 – 3838Cytoplasmic Potential
Transmembrane384 – 40421Helical; Potential
Topological domain405 – 4117Extracellular Potential
Transmembrane412 – 43221Helical; Potential
Topological domain433 – 47139Cytoplasmic Potential
Transmembrane472 – 49221Helical; Potential
Topological domain493 – 53745Extracellular Potential

Amino acid modifications

Glycosylation811N-linked (GlcNAc...) Potential

Experimental info

Sequence conflict2711K → R in AAC61265. Ref.1
Sequence conflict4791G → V in BAC27624. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O88909 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: F85FF82002AB26EB

FASTA53759,246
        10         20         30         40         50         60 
MTFSEILDRV GSMGPFQYLH VTLLALPILG IANHNLLQIF TATTPDHHCR PPPNASLEPW 

        70         80         90        100        110        120 
VLPLGPNGKP EKCLRFVHLP NASLPNDTQG ATEPCLDGWI YNSTRDTIVT EWDLVCGSNK 

       130        140        150        160        170        180 
LKEMAQSVFM AGILVGGPVF GELSDRFGRK PILTWSYLLL AASGSSAAFS PSLTVYMIFR 

       190        200        210        220        230        240 
FLCGCSISGI SLSTIILNVE WVPTSTRAIS STTIGYCYTI GQFILPGLAY AVPQWRWLQL 

       250        260        270        280        290        300 
SVSAAFFIFS LLSWWVPESI RWLVLSGKFS KALKTLQRVA TFNGKKEEGE KLTVEELKFN 

       310        320        330        340        350        360 
LQKDITSAKV KYGLSDLFRV SILRRVTFCL SLAWFATGFA YYSLAMGVEE FGVNIYILQI 

       370        380        390        400        410        420 
IFGGVDIPAK FITILSISYL GRRITQGFLL ILAGVAILAL IFVSSEMQLL RTALAVFGKG 

       430        440        450        460        470        480 
CLSGSFSCLF LYTSELYPTV LRQTGMGISN IWARVGSMIA PLVKITGELQ PFIPNVIFGT 

       490        500        510        520        530 
MTLLGGSAAF FLLETLNRPL PETIEDIQDW YQQTKKTKQE PEAEKASQTI PLKTGGP

« Hide

References

« Hide 'large scale' references
[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. 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].
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00387413.
RefSeqNP_001158106.1. NM_001164634.1.
NP_001158107.1. NM_001164635.1.
NP_112471.3. NM_031194.5.
UniGeneMm.285294.

3D structure databases

ProteinModelPortalO88909.
SMRO88909. Positions 117-449.
ModBaseSearch...

Protein family/group databases

TCDB2.A.1.19.9. major facilitator superfamily (MFS).

Proteomic databases

PRIDEO88909.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000010251; ENSMUSP00000010251; ENSMUSG00000063796.
ENSMUST00000170817; ENSMUSP00000131045; ENSMUSG00000063796.
GeneID19879.
KEGGmmu:19879.
UCSCuc008gmc.2. mouse.

Organism-specific databases

CTD9376.
MGIMGI:1336187. Slc22a8.

Phylogenomic databases

eggNOGCOG0477.
GeneTreeENSGT00550000074177.
HOGENOMHOG000234569.
HOVERGENHBG108433.
InParanoidO88909.
KOK08205.
OMAMANHNLL.
OrthoDBEOG418BPG.

Gene expression databases

BgeeO88909.
GenevestigatorO88909.

Family and domain databases

InterProIPR020846. MFS_dom.
IPR016196. MFS_dom_general_subst_transpt.
IPR004749. Orgcat_transp.
IPR005828. Sub_transporter.
[Graphical view]
PfamPF00083. Sugar_tr. 1 hit.
[Graphical view]
SUPFAMSSF103473. MFS_gen_substrate_transporter. 1 hit.
TIGRFAMsTIGR00898. 2A0119. 1 hit.
PROSITEPS50850. MFS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio297374.
SOURCESearch...

Entry information

Entry nameS22A8_MOUSE
AccessionPrimary (citable) accession number: O88909
Secondary accession number(s): Q3TZF9 expand/collapse secondary AC list , Q8CCX3, Q8CFH5, Q91WJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: May 1, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents