S22AM_MOUSE
ID S22AM_MOUSE Reviewed; 554 AA.
AC Q8R0S9;
DT 05-JUL-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Solute carrier family 22 member 22 {ECO:0000312|MGI:MGI:2446114};
DE AltName: Full=Prostaglandin-specific organic anion transporter {ECO:0000303|PubMed:20448048};
GN Name=Slc22a22 {ECO:0000312|MGI:MGI:2446114};
GN Synonyms=Oat-pg {ECO:0000303|PubMed:20448048};
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|Proteomes:UP000000589};
RN [1] {ECO:0000312|EMBL:BAJ11740.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20448048; DOI=10.1074/jbc.m109.084426;
RA Shiraya K., Hirata T., Hatano R., Nagamori S., Wiriyasermkul P.,
RA Jutabha P., Matsubara M., Muto S., Tanaka H., Asano S., Anzai N., Endou H.,
RA Yamada A., Sakurai H., Kanai Y.;
RT "A novel transporter of SLC22 family specifically transports prostaglandins
RT and co-localizes with 15-hydroxyprostaglandin dehydrogenase in renal
RT proximal tubules.";
RL J. Biol. Chem. 285:22141-22151(2010).
RN [2] {ECO:0000312|EMBL:BAC26852.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC26852.1};
RC TISSUE=Testis {ECO:0000312|EMBL:BAC26852.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3] {ECO:0000312|Proteomes:UP000000589}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
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 [4] {ECO:0000312|EMBL:EDL29281.1}
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 [5] {ECO:0000312|EMBL:AAH26439.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N {ECO:0000312|EMBL:AAH26439.1};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH26439.1};
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 [6]
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 exhibits
CC high specificity for a subset of prostaglandins including prostaglandin
CC E2 (PGE2), prostaglandin E1 (PGE1), prostaglandin F2-alpha (PGF2-alpha)
CC and prostaglandin D2 (PGD2). {ECO:0000269|PubMed:20448048}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=118.3 nM for prostaglandin E2 {ECO:0000269|PubMed:20448048};
CC KM=158.2 nM for prostaglandin F2-alpha {ECO:0000269|PubMed:20448048};
CC KM=156.8 nM for prostaglandin E1 {ECO:0000269|PubMed:20448048};
CC KM=371.6 nM for prostaglandin D2 {ECO:0000269|PubMed:20448048};
CC Vmax=6.32 pmol/min/mg enzyme toward prostaglandin E2
CC {ECO:0000269|PubMed:20448048};
CC Vmax=4.61 pmol/min/mg enzyme toward prostaglandin F2-alpha
CC {ECO:0000269|PubMed:20448048};
CC Vmax=2.71 pmol/min/mg enzyme toward prostaglandin E1
CC {ECO:0000269|PubMed:20448048};
CC Vmax=8.95 pmol/min/mg enzyme toward prostaglandin D2
CC {ECO:0000269|PubMed:20448048};
CC Temperature dependence:
CC High activity at 37 degrees Celsius. Little or no activity at 0
CC degrees Celsius. {ECO:0000269|PubMed:20448048};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:20448048}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in kidney where it is found
CC in proximal convoluted tubules (at protein level). Colocalizes with the
CC prostaglandin-inactivating enzyme HPGD in kidney (at protein level).
CC Not detected in other tissues tested. {ECO:0000269|PubMed:20448048}.
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; AB520670; BAJ11740.1; -; mRNA.
DR EMBL; AK030222; BAC26852.1; -; mRNA.
DR EMBL; AC123692; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124678; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC161480; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466545; EDL29281.1; -; Genomic_DNA.
DR EMBL; BC026439; AAH26439.1; -; mRNA.
DR CCDS; CCDS27481.1; -.
DR RefSeq; NP_759010.1; NM_172378.2.
DR RefSeq; XP_006520759.1; XM_006520696.1.
DR AlphaFoldDB; Q8R0S9; -.
DR SMR; Q8R0S9; -.
DR STRING; 10090.ENSMUSP00000022995; -.
DR TCDB; 2.A.1.19.20; the major facilitator superfamily (mfs).
DR GlyGen; Q8R0S9; 2 sites.
DR iPTMnet; Q8R0S9; -.
DR PhosphoSitePlus; Q8R0S9; -.
DR jPOST; Q8R0S9; -.
DR PaxDb; Q8R0S9; -.
DR PRIDE; Q8R0S9; -.
DR ProteomicsDB; 253362; -.
DR DNASU; 210463; -.
DR Ensembl; ENSMUST00000022995; ENSMUSP00000022995; ENSMUSG00000022366.
DR Ensembl; ENSMUST00000110196; ENSMUSP00000105825; ENSMUSG00000022366.
DR GeneID; 210463; -.
DR KEGG; mmu:210463; -.
DR UCSC; uc007vsn.1; mouse.
DR CTD; 210463; -.
DR MGI; MGI:2446114; Slc22a22.
DR VEuPathDB; HostDB:ENSMUSG00000022366; -.
DR eggNOG; KOG0255; Eukaryota.
DR GeneTree; ENSGT00940000157004; -.
DR HOGENOM; CLU_001265_33_3_1; -.
DR InParanoid; Q8R0S9; -.
DR OMA; CHRFRQT; -.
DR OrthoDB; 464838at2759; -.
DR PhylomeDB; Q8R0S9; -.
DR TreeFam; TF315847; -.
DR BioGRID-ORCS; 210463; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Slc22a22; mouse.
DR PRO; PR:Q8R0S9; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8R0S9; protein.
DR Bgee; ENSMUSG00000022366; Expressed in right kidney and 9 other tissues.
DR ExpressionAtlas; Q8R0S9; baseline and differential.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004955; F:prostaglandin receptor activity; IDA:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015711; P:organic anion transport; IBA:GO_Central.
DR GO; GO:0071720; P:sodium-independent prostaglandin transport; IDA:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR005829; Sugar_transporter_CS.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
DR PROSITE; PS00216; SUGAR_TRANSPORT_1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..554
FT /note="Solute carrier family 22 member 22"
FT /id="PRO_0000440989"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 16..36
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..144
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 145..165
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 166..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 173..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..199
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..231
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 232..252
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 253..258
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 280..347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 348..368
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 369..376
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 377..397
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 398..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 406..426
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..434
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 435..455
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 456..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 467..487
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 488..491
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 492..512
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 513..554
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 194
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 554 AA; 62424 MW; 65C850DEC9CF00E7 CRC64;
MDFDEILHHV GDSGRFQICM IILLNILSLV LSPHDVLENF TAAIPAHHCS INLDNSRSEV
STDMNLTTED LMKVSIPMGP NQKPEQCRRF RYTQWQFLDS NISTFNSTEL ETEPCLDGWT
YDHSVFTSTI VTEWDLVCDF QSFKYYAQAT SLAGHLVSCP LSGIISDRFG RKPLLMYCSL
AYGAVGTYCA FAPNFSVYCV LRFLLSAFQS TILINSLILV LEEASVQWHP TIIVLSGLFN
SIGQGVLGGL AYVISDWHLL QLAYALPFFI FFVLFCWVPE SVRWLIITGK TDQAWKELQR
IASINGKKGI AQNLTTEDLR SKLKKDVNST GKLFRIKDIF INPLIRKIVL SNSSLLFAEL
FSFVGLLLDV QLLGKNMFLT QIFLGAIDVP SKSLTYFTIR NVSRRPLIAF LLLTTGSCIT
ITIFISEEMY VLRTIIFILG KGCFAAFTCI STTYINELSP VELRSTLNGV FLAVVRLAGV
LSALTLATRK YFVYLPMILY GVLPIVATIS ILFLPETFNL PHTDIIKDME KRKRLMSKNI
SKKEGQDFLE TTEC
