S22AJ_MOUSE
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 03-AUG-2022, entry version 146.
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},
GN Slc22a9 {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=2.0 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 GlyGen; Q8VCA0; 4 sites.
DR iPTMnet; Q8VCA0; -.
DR PhosphoSitePlus; Q8VCA0; -.
DR jPOST; Q8VCA0; -.
DR MaxQB; Q8VCA0; -.
DR PaxDb; Q8VCA0; -.
DR PRIDE; Q8VCA0; -.
DR ProteomicsDB; 253360; -.
DR DNASU; 207151; -.
DR Ensembl; ENSMUST00000025666; ENSMUSP00000025666; ENSMUSG00000024757.
DR GeneID; 207151; -.
DR KEGG; mmu:207151; -.
DR UCSC; uc008glo.2; mouse.
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; WLIMTNK; -.
DR OrthoDB; 464838at2759; -.
DR PhylomeDB; Q8VCA0; -.
DR TreeFam; TF315847; -.
DR BioGRID-ORCS; 207151; 3 hits in 72 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 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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015301; F:anion:anion antiporter activity; 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:0015711; P:organic anion transport; IDA:MGI.
DR GO; GO:0002238; P:response to molecule of fungal origin; IEA:Ensembl.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR005828; MFS_sugar_transport-like.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF00083; Sugar_tr; 1.
DR SUPFAM; SSF103473; SSF103473; 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
