ID   S22AJ_MOUSE             Reviewed;         551 AA.
AC   Q8VCA0; Q6A4K9;
DT   30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Solute carrier family 22 member 19 {ECO:0000303|PubMed:15068970};
DE   AltName: Full=Organic anion transporter 5 {ECO:0000312|EMBL:AAQ09529.1};
GN   Name=Slc22a19 {ECO:0000303|PubMed:15068970};
GN   Synonyms=Oat5 {ECO:0000312|EMBL:AAQ09529.1}, Slc22a9
GN   {ECO:0000312|MGI:MGI:2442751};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090 {ECO:0000312|EMBL:AAH21384.1};
RN   [1] {ECO:0000312|EMBL:AAQ09529.1}
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:AAQ09529.1};
RA   Mount D.B.;
RT   "Sequence of murine organic anion transporter 5 (OAT-5).";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000312|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000312|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3] {ECO:0000312|EMBL:EDL33322.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000312|EMBL:AAH21384.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N {ECO:0000312|EMBL:AAH21384.1};
RC   TISSUE=Kidney {ECO:0000312|EMBL:AAH21384.1};
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5] {ECO:0000305}
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=15068970; DOI=10.1152/ajprenal.00012.2004;
RA   Youngblood G.L., Sweet D.H.;
RT   "Identification and functional assessment of the novel murine organic anion
RT   transporter Oat5 (Slc22a19) expressed in kidney.";
RL   Am. J. Physiol. 287:F236-F244(2004).
RN   [6] {ECO:0000305}
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=16150593; DOI=10.1016/j.jsbmb.2005.06.028;
RA   Kwak J.O., Kim H.W., Oh K.J., Ko C.B., Park H., Cha S.H.;
RT   "Characterization of mouse organic anion transporter 5 as a renal steroid
RT   sulfate transporter.";
RL   J. Steroid Biochem. Mol. Biol. 97:369-375(2005).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Sodium-independent organic anion transporter which shows high
CC       specificity for estrone sulfate, dehydroepiandrosterone sulfate, and
CC       the mycotoxin ochratoxin A (OTA) (PubMed:15068970, PubMed:16150593).
CC       Transport of OTA is strongly inhibited by estrone sulfate and
CC       probenecid, and to a lesser extent by 2,4-dichlorophenoxyacetic acid
CC       (2,4-D) and salicylate (PubMed:15068970). Transport of estrone sulfate
CC       is inhibited by various steroid sulfate conjugates including
CC       dehydroepiandrosterone sulfate, alpha-naphthyl sulfate, beta-estradiol
CC       sulfate, 4-methylumbelliferyl sulfate and p-nitrophenyl sulfate (but
CC       not minoxidil sulfate) (PubMed:16150593). {ECO:0000269|PubMed:15068970,
CC       ECO:0000269|PubMed:16150593}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2 uM for ochratoxin A {ECO:0000269|PubMed:15068970};
CC         KM=2.2 uM for estrone sulfate {ECO:0000269|PubMed:16150593};
CC         KM=3.8 uM for dehydroepiandrosterone sulfate
CC         {ECO:0000269|PubMed:16150593};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:15068970, ECO:0000269|PubMed:16150593}; Multi-pass
CC       membrane protein {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Specifically expressed in kidney, where it
CC       localizes to proximal tubules of the outer medulla (at protein level)
CC       (PubMed:15068970, PubMed:16150593). Not detected in other tissues
CC       tested (PubMed:15068970). {ECO:0000269|PubMed:15068970,
CC       ECO:0000269|PubMed:16150593}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; AF529221; AAQ09529.1; -; mRNA.
DR   EMBL; AC109225; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC130693; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC021384; AAH21384.1; -; mRNA.
DR   EMBL; CH466612; EDL33322.1; -; Genomic_DNA.
DR   CCDS; CCDS29532.1; -.
DR   RefSeq; NP_659034.1; NM_144785.2.
DR   AlphaFoldDB; Q8VCA0; -.
DR   SMR; Q8VCA0; -.
DR   STRING; 10090.ENSMUSP00000025666; -.
DR   ChEMBL; CHEMBL2073675; -.
DR   GlyCosmos; Q8VCA0; 4 sites, No reported glycans.
DR   GlyGen; Q8VCA0; 4 sites.
DR   iPTMnet; Q8VCA0; -.
DR   PhosphoSitePlus; Q8VCA0; -.
DR   jPOST; Q8VCA0; -.
DR   MaxQB; Q8VCA0; -.
DR   PaxDb; 10090-ENSMUSP00000025666; -.
DR   ProteomicsDB; 253360; -.
DR   DNASU; 207151; -.
DR   Ensembl; ENSMUST00000025666.8; ENSMUSP00000025666.8; ENSMUSG00000024757.8.
DR   GeneID; 207151; -.
DR   KEGG; mmu:207151; -.
DR   UCSC; uc008glo.2; mouse.
DR   AGR; MGI:2442751; -.
DR   CTD; 207151; -.
DR   MGI; MGI:2442751; Slc22a19.
DR   VEuPathDB; HostDB:ENSMUSG00000024757; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000161239; -.
DR   HOGENOM; CLU_001265_33_3_1; -.
DR   InParanoid; Q8VCA0; -.
DR   OMA; CTSGIAF; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; Q8VCA0; -.
DR   TreeFam; TF315847; -.
DR   BioGRID-ORCS; 207151; 3 hits in 77 CRISPR screens.
DR   PRO; PR:Q8VCA0; -.
DR   Proteomes; UP000000589; Chromosome 19.
DR   RNAct; Q8VCA0; Protein.
DR   Bgee; ENSMUSG00000024757; Expressed in right kidney and 18 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0015636; F:short-chain fatty acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0019534; F:toxin transmembrane transporter activity; IDA:MGI.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0015711; P:organic anion transport; IDA:MGI.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:Ensembl.
DR   CDD; cd17374; MFS_OAT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR24064:SF670; SOLUTE CARRIER FAMILY 22 (ORGANIC CATION TRANSPORTER), MEMBER 26-RELATED; 1.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..551
FT                   /note="Solute carrier family 22 member 19"
FT                   /id="PRO_0000441094"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..145
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..188
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..234
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        235..255
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        256..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..349
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        350..370
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        371..377
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        399..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        407..427
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        428..434
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        435..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        456..468
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        469..489
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        490..495
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        517..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REGION          524..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..545
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        538..540
FT                   /note="KEA -> EET (in Ref. 1; AAQ09529)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   551 AA;  60864 MW;  018589BC68C4DC20 CRC64;
     MAFQDLIIQI GSLGRFQILH MIFVLICHAL SAPHTLLENF TAAIPSHRCW VPILDNDTAS
     DNGSRILSQD DLLRISIPLD SNLRPDKCRR YIQPQWHLLH LNGTFPTVTE PDTEPCVDGW
     VYDQSTFLST TVTQWDLVCG SQALNSVAKF IYMTGIFIGY IMGGHLSDKF GRKLIFTCSL
     LKMAITETCV AFAPSFLIYC SLRFLSGIFS STLRTNSALL ILEWTSPKFQ ALVMALIFIA
     SGVGQTLLGG LAFAFRNWHH LQLALSVPMF LLLIPTRWLS ESARWLIMAN KPQKSLKELK
     KAACVNRIKN SGDALTLEVV KTIMKEELEA AQTKPSPLDL FRTPNLRKRI CLLSFVRFVS
     VMSLLGLLIN IQYLSNNVFL LQCLYGVVCI PANVLGNFSM NYMGRRMTQL IFMSVLGISI
     LAVVFLPQEM QILRVFLSTL GGAISSASIT STLVHANELV PTIIRATALG VVGIAGSAGG
     ALSPLLMILT TYSASLPWII YGILPFLGGL VALLLPETKN QPLPDSIQDI ENKRKSSKEA
     KKDVVAKVTP L
//