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Solute carrier family 22 member 6 (Kidney-specific transport protein) (Novel kidney transcript) (mNKT) (Organic anion transporter 1) (Renal organic anion transporter 1) (mROAT1)

 S22A6_MOUSE             Reviewed;         545 AA.
Q8VC69; Q61185;
18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
01-MAR-2002, sequence version 1.
20-JUN-2018, entry version 135.
RecName: Full=Solute carrier family 22 member 6;
AltName: Full=Kidney-specific transport protein;
AltName: Full=Novel kidney transcript;
Short=mNKT;
AltName: Full=Organic anion transporter 1;
AltName: Full=Renal organic anion transporter 1;
Short=mROAT1;
Name=Slc22a6; Synonyms=Nkt, Oat1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
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, AND SUBCELLULAR LOCATION.
STRAIN=BALB/cJ; TISSUE=Kidney;
PubMed=9045672; DOI=10.1074/jbc.272.10.6471;
Lopez-Nieto C.E., You G., Bush K.T., Barros E.J., Beier D.R.,
Nigam S.K.;
"Molecular cloning and characterization of NKT, a gene product related
to the organic cation transporter family that is almost exclusively
expressed in the kidney.";
J. Biol. Chem. 272:6471-6478(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Liver;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
PubMed=9880528; DOI=10.1074/jbc.274.3.1519;
Kuze K., Graves P., Leahy A., Wilson P., Stuhlmann H., You G.;
"Heterologous expression and functional characterization of a mouse
renal organic anion transporter in mammalian cells.";
J. Biol. Chem. 274:1519-1524(1999).
[5]
FUNCTION.
PubMed=10744714; DOI=10.1074/jbc.275.14.10278;
You G., Kuze K., Kohanski R.A., Amsler K., Henderson S.;
"Regulation of mOAT-mediated organic anion transport by okadaic acid
and protein kinase C in LLC-PK(1) cells.";
J. Biol. Chem. 275:10278-10284(2000).
[6]
FUNCTION.
PubMed=14979872; DOI=10.1042/BJ20031724;
Tanaka K., Zhou F., Kuze K., You G.;
"Cysteine residues in the organic anion transporter mOAT1.";
Biochem. J. 380:283-287(2004).
[7]
MUTAGENESIS OF ASN-39, AND GLYCOSYLATION AT ASN-56; ASN-86; ASN-91 AND
ASN-107.
PubMed=14749323; DOI=10.1074/jbc.M400197200;
Tanaka K., Xu W., Zhou F., You G.;
"Role of glycosylation in the organic anion transporter OAT1.";
J. Biol. Chem. 279:14961-14966(2004).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: 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. {ECO:0000250,
ECO:0000269|PubMed:10744714, ECO:0000269|PubMed:14979872,
ECO:0000269|PubMed:9880528}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=37.3 uM for PAH {ECO:0000269|PubMed:9880528};
Vmax=210 pmol/min/mg enzyme for PAH uptake
{ECO:0000269|PubMed:9880528};
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9045672};
Multi-pass membrane protein {ECO:0000269|PubMed:9045672}.
Note=Localized to the plasma membrane.
-!- TISSUE SPECIFICITY: Expressed in kidney; in the basolateral
membrane and at much lower levels in brain.
{ECO:0000269|PubMed:9045672, ECO:0000269|PubMed:9880528}.
-!- DEVELOPMENTAL STAGE: Developmentally regulated with significant
expression beginning at E18 and rising just before birth.
-!- DOMAIN: Multiple cysteine residues are necessary for proper
targeting to the plasma membrane.
-!- PTM: Glycosylated. Glycosylation is necessary for proper targeting
of the transporter to the plasma membrane.
{ECO:0000269|PubMed:14749323}.
-!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1)
superfamily. Organic cation transporter (TC 2.A.1.19) family.
{ECO:0000305}.
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EMBL; U52842; AAC53112.1; -; mRNA.
EMBL; AK035971; BAC29261.1; -; mRNA.
EMBL; BC021647; AAH21647.1; -; mRNA.
CCDS; CCDS29538.1; -.
RefSeq; NP_032792.2; NM_008766.3.
UniGene; Mm.30090; -.
ProteinModelPortal; Q8VC69; -.
STRING; 10090.ENSMUSP00000010250; -.
BindingDB; Q8VC69; -.
ChEMBL; CHEMBL5653; -.
iPTMnet; Q8VC69; -.
PhosphoSitePlus; Q8VC69; -.
MaxQB; Q8VC69; -.
PaxDb; Q8VC69; -.
PRIDE; Q8VC69; -.
Ensembl; ENSMUST00000010250; ENSMUSP00000010250; ENSMUSG00000024650.
GeneID; 18399; -.
KEGG; mmu:18399; -.
UCSC; uc008gme.2; mouse.
CTD; 9356; -.
MGI; MGI:892001; Slc22a6.
eggNOG; KOG0255; Eukaryota.
eggNOG; COG0477; LUCA.
GeneTree; ENSGT00760000118852; -.
HOGENOM; HOG000234569; -.
HOVERGEN; HBG108433; -.
InParanoid; Q8VC69; -.
KO; K08203; -.
OMA; RWYSSSG; -.
OrthoDB; EOG091G07CO; -.
PhylomeDB; Q8VC69; -.
TreeFam; TF315847; -.
Reactome; R-MMU-561048; Organic anion transport.
ChiTaRS; Slc22a6; mouse.
PRO; PR:Q8VC69; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000024650; -.
Genevisible; Q8VC69; MM.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0005901; C:caveola; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0015301; F:anion:anion antiporter activity; ISO:MGI.
GO; GO:0031404; F:chloride ion binding; ISO:MGI.
GO; GO:0005452; F:inorganic anion exchanger activity; ISS:UniProtKB.
GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:MGI.
GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISO:MGI.
GO; GO:0015143; F:urate transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
GO; GO:0006820; P:anion transport; IDA:MGI.
GO; GO:0015711; P:organic anion transport; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISO:MGI.
GO; GO:0097254; P:renal tubular secretion; IMP:UniProtKB.
GO; GO:0031427; P:response to methotrexate; IEA:Ensembl.
GO; GO:0043252; P:sodium-independent organic anion transport; ISO:MGI.
GO; GO:0015747; P:urate transport; IBA:GO_Central.
CDD; cd06174; MFS; 1.
InterPro; IPR020846; MFS_dom.
InterPro; IPR005828; MFS_sugar_transport-like.
InterPro; IPR036259; MFS_trans_sf.
InterPro; IPR004749; Orgcat_transp/SVOP.
Pfam; PF00083; Sugar_tr; 1.
SUPFAM; SSF103473; SSF103473; 1.
TIGRFAMs; TIGR00898; 2A0119; 1.
PROSITE; PS50850; MFS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycoprotein; Membrane;
Reference proteome; Transmembrane; Transmembrane helix.
CHAIN 1 545 Solute carrier family 22 member 6.
/FTId=PRO_0000324168.
TOPO_DOM 1 9 Cytoplasmic. {ECO:0000255}.
TRANSMEM 10 30 Helical. {ECO:0000255}.
TOPO_DOM 31 129 Extracellular. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TOPO_DOM 151 157 Cytoplasmic. {ECO:0000255}.
TRANSMEM 158 177 Helical. {ECO:0000255}.
TOPO_DOM 178 180 Extracellular. {ECO:0000255}.
TRANSMEM 181 201 Helical. {ECO:0000255}.
TOPO_DOM 202 218 Cytoplasmic. {ECO:0000255}.
TRANSMEM 219 239 Helical. {ECO:0000255}.
TOPO_DOM 240 242 Extracellular. {ECO:0000255}.
TRANSMEM 243 263 Helical. {ECO:0000255}.
TOPO_DOM 264 331 Cytoplasmic. {ECO:0000255}.
TRANSMEM 332 352 Helical. {ECO:0000255}.
TOPO_DOM 353 362 Extracellular. {ECO:0000255}.
TRANSMEM 363 383 Helical. {ECO:0000255}.
TOPO_DOM 384 389 Cytoplasmic. {ECO:0000255}.
TRANSMEM 390 410 Helical. {ECO:0000255}.
TOPO_DOM 411 419 Extracellular. {ECO:0000255}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TOPO_DOM 441 450 Cytoplasmic. {ECO:0000255}.
TRANSMEM 451 471 Helical. {ECO:0000255}.
TOPO_DOM 472 478 Extracellular. {ECO:0000255}.
TRANSMEM 479 499 Helical. {ECO:0000255}.
TOPO_DOM 500 545 Cytoplasmic. {ECO:0000255}.
CARBOHYD 39 39 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 56 56 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14749323}.
CARBOHYD 86 86 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14749323}.
CARBOHYD 91 91 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14749323}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14749323}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 39 39 N->Q: Complete loss of PAH transport
activity. {ECO:0000269|PubMed:14749323}.
MUTAGEN 49 49 C->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.
{ECO:0000269|PubMed:9045672}.
MUTAGEN 122 122 C->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.
{ECO:0000269|PubMed:9045672}.
MUTAGEN 183 183 C->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.
{ECO:0000269|PubMed:9045672}.
MUTAGEN 434 434 C->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. {ECO:0000269|PubMed:9045672}.
CONFLICT 66 66 W -> R (in Ref. 1; AAC53112).
{ECO:0000305}.
SEQUENCE 545 AA; 60013 MW; 827782E115705C77 CRC64;
MAFNDLLKQV GGVGRFQLIQ VTMVVAPLLL MASHNTLQNF TAAIPAHHCR PPANANLSKD
GGLEAWLPLD KQGRPESCLR FPFPHNGTEA NGTGVTEPCL DGWVYDNSTF PSTIVTEWNL
VCSHRAFRQL AQSLFMVGVL LGAMMFGYLA DRLGRRKVLI LNYLQTAVSG TCAAYAPNYT
VYCIFRLLSG MSLASIAINC MTLNMEWMPI HTRAYVGTLI GYVYSLGQFL LAGIAYAVPH
WRHLQLAVSV PFFVAFIYSW FFIESARWYS SSGRLDLTLR ALQRVARING KQEEGAKLSI
EVLQTSLQKE LTLNKGQASA MELLRCPTLR RLFLCLSMLW FATSFAYYGL VMDLQGFGVS
MYLIQVIFGA VDLPAKFVCF LVINSMGRRP AQLASLLLAG ICILVNGIIP RGHTIIRTSL
AVLGKGCLAS SFNCIFLYTG ELYPTMIRQT GLGMGSTMAR VGSIVSPLIS MTAEFYPSIP
LFIFGAVPVA ASAVTALLPE TLGQPLPDTV QDLKSRSRGK QKQQQLEQQK QMIPLQVSTQ
EKNGL


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