S22AC_MOUSE
ID S22AC_MOUSE Reviewed; 553 AA.
AC Q8CFZ5; O54778;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Solute carrier family 22 member 12;
DE AltName: Full=Renal-specific transporter;
DE Short=RST;
DE AltName: Full=Urate anion exchanger 1;
GN Name=Slc22a12; Synonyms=Urat1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9409754; DOI=10.1016/s0014-5793(97)01325-2;
RA Mori K., Ogawa Y., Ebihara K., Aoki T., Tamura N., Sugawara A.,
RA Kuwahara T., Ozaki S., Mukoyama M., Tashiro K., Tanaka I., Nakao K.;
RT "Kidney-specific expression of a novel mouse organic cation transporter-
RT like protein.";
RL FEBS Lett. 417:371-374(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP FUNCTION, GLYCOSYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=14747372; DOI=10.1097/01.asn.0000107560.80107.19;
RA Hosoyamada M., Ichida K., Enomoto A., Hosoya T., Endou H.;
RT "Function and localization of urate transporter 1 in mouse kidney.";
RL J. Am. Soc. Nephrol. 15:261-268(2004).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-534 AND THR-542, AND
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: Major urate transporter involved in renal reabsorption of
CC urate and helps to maintain blood levels of uric acid
CC (PubMed:14747372). Translocates urate over the apical membrane of
CC proximal tubular cells in exchange for organic anions or chloride ions
CC (PubMed:14747372). {ECO:0000269|PubMed:14747372}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1213 uM for urate {ECO:0000269|PubMed:14747372};
CC -!- SUBUNIT: Interacts with PDZK1. {ECO:0000250|UniProtKB:Q96S37}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14747372};
CC Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC {ECO:0000269|PubMed:14747372}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in kidney (at protein level). Detected in
CC kidney cortex, in proximal tubules. {ECO:0000269|PubMed:14747372,
CC ECO:0000269|PubMed:9409754}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:14747372}.
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; AB005451; BAA23875.1; -; mRNA.
DR EMBL; BC035927; AAH35927.1; -; mRNA.
DR CCDS; CCDS29505.1; -.
DR RefSeq; NP_033229.3; NM_009203.3.
DR AlphaFoldDB; Q8CFZ5; -.
DR SMR; Q8CFZ5; -.
DR STRING; 10090.ENSMUSP00000109078; -.
DR TCDB; 2.A.1.19.14; the major facilitator superfamily (mfs).
DR GlyGen; Q8CFZ5; 1 site.
DR iPTMnet; Q8CFZ5; -.
DR PhosphoSitePlus; Q8CFZ5; -.
DR jPOST; Q8CFZ5; -.
DR MaxQB; Q8CFZ5; -.
DR PaxDb; Q8CFZ5; -.
DR PeptideAtlas; Q8CFZ5; -.
DR PRIDE; Q8CFZ5; -.
DR ProteomicsDB; 260757; -.
DR DNASU; 20521; -.
DR GeneID; 20521; -.
DR KEGG; mmu:20521; -.
DR UCSC; uc012bho.1; mouse.
DR CTD; 116085; -.
DR MGI; MGI:1195269; Slc22a12.
DR eggNOG; KOG0255; Eukaryota.
DR InParanoid; Q8CFZ5; -.
DR OrthoDB; 464838at2759; -.
DR PhylomeDB; Q8CFZ5; -.
DR TreeFam; TF315847; -.
DR Reactome; R-MMU-561048; Organic anion transport.
DR BioGRID-ORCS; 20521; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Slc22a12; mouse.
DR PRO; PR:Q8CFZ5; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CFZ5; protein.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0030165; F:PDZ domain binding; ISS:UniProtKB.
DR GO; GO:0015143; F:urate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015711; P:organic anion transport; IBA:GO_Central.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISS:UniProtKB.
DR GO; GO:0046415; P:urate metabolic process; ISO:MGI.
DR GO; GO:0015747; P:urate transport; IDA:UniProtKB.
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; Phosphoprotein;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..553
FT /note="Solute carrier family 22 member 12"
FT /id="PRO_0000307945"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 232..252
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 351..371
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 412..432
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 466..486
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 407
FT /note="F -> L (in Ref. 1; BAA23875)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 553 AA; 60194 MW; D331583A8D54DBBF CRC64;
MAFPELLDRV GGLGRFQLFQ TVALVTPILW VTTQNMLENF SAAVPHHRCW VPLLDNSTSQ
ASIPGDLGPD VLLAVSIPPG PDQQPHQCLR FRQPQWQLTE SNATATNWSD AATEPCEDGW
VYDHSTFRST IVTTWDLVCN SQALRPMAQS IFLAGILVGA AVCGHASDRF GRRRVLTWSY
LLVSVSGTAA AFMPTFPLYC LFRFLLASAV AGVMMNTASL LMEWTSAQGS PLVMTLNALG
FSFGQVLTGS VAYGVRSWRM LQLAVSAPFF LFFVYSWWLP ESARWLITVG KLDQGLQELQ
RVAAVNRRKA EGDTLTMEVL RSAMEEEPSR DKAGASLGTL LHTPGLRHRT IISMLCWFAF
GFTFYGLALD LQALGSNIFL LQALIGIVDF PVKTGSLLLI SRLGRRFCQV SFLVLPGLCI
LSNILVPHGM GVLRSALAVL GLGCLGGAFT CITIFSSELF PTVIRMTAVG LCQVAARGGA
MLGPLVRLLG VYGSWMPLLV YGVVPVLSGL AALLLPETKN LPLPDTIQDI QKQSVKKVTH
DTPDGSILMS TRL
