SO1A6_MOUSE
ID SO1A6_MOUSE Reviewed; 670 AA.
AC Q99J94; Q3UQC6; Q9CUP7;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Solute carrier organic anion transporter family member 1A6;
DE AltName: Full=Kidney-specific organic anion-transporting polypeptide 5;
DE Short=OATP-5;
DE AltName: Full=Solute carrier family 21 member 13;
GN Name=Slco1a6; Synonyms=Oatp5, Slc21a13;
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].
RC STRAIN=BALB/cJ; TISSUE=Kidney;
RX PubMed=11162483; DOI=10.1006/bbrc.2000.4072;
RA Choudhuri S., Ogura K., Klaassen C.D.;
RT "Cloning, expression, and ontogeny of mouse organic anion-transporting
RT polypeptide-5, a kidney-specific organic anion transporter.";
RL Biochem. Biophys. Res. Commun. 280:92-98(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Testis;
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]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-632; SER-634 AND SER-635, 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: May mediate the Na(+)-independent transport of organic
CC anions.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Kidney specific.
CC -!- DEVELOPMENTAL STAGE: Not detected at birth and up to day 20.
CC Intermediate levels were detected at day 40 and adult levels were
CC reached at day 60.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AF213260; AAG60350.1; -; mRNA.
DR EMBL; AF203701; AAG60003.1; -; mRNA.
DR EMBL; AK015176; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK142587; BAE25116.1; -; mRNA.
DR CCDS; CCDS39693.1; -.
DR PIR; JC7581; JC7581.
DR RefSeq; NP_076207.1; NM_023718.3.
DR RefSeq; XP_006507028.1; XM_006506965.3.
DR RefSeq; XP_011239889.1; XM_011241587.1.
DR RefSeq; XP_017177101.1; XM_017321612.1.
DR AlphaFoldDB; Q99J94; -.
DR SMR; Q99J94; -.
DR STRING; 10090.ENSMUSP00000107458; -.
DR TCDB; 2.A.60.1.25; the organo anion transporter (oat) family.
DR GlyGen; Q99J94; 5 sites.
DR iPTMnet; Q99J94; -.
DR PhosphoSitePlus; Q99J94; -.
DR jPOST; Q99J94; -.
DR PaxDb; Q99J94; -.
DR PRIDE; Q99J94; -.
DR ProteomicsDB; 261101; -.
DR DNASU; 28254; -.
DR Ensembl; ENSMUST00000111827; ENSMUSP00000107458; ENSMUSG00000079262.
DR GeneID; 28254; -.
DR KEGG; mmu:28254; -.
DR UCSC; uc009eow.2; mouse.
DR CTD; 28254; -.
DR MGI; MGI:1351906; Slco1a6.
DR VEuPathDB; HostDB:ENSMUSG00000079262; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_4_0_1; -.
DR InParanoid; Q99J94; -.
DR OMA; MSECLLS; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q99J94; -.
DR TreeFam; TF317540; -.
DR BioGRID-ORCS; 28254; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Slco1a6; mouse.
DR PRO; PR:Q99J94; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99J94; protein.
DR Bgee; ENSMUSG00000079262; Expressed in right kidney and 63 other tissues.
DR Genevisible; Q99J94; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IBA:GO_Central.
DR GO; GO:0008206; P:bile acid metabolic process; IMP:MGI.
DR GO; GO:0042632; P:cholesterol homeostasis; IMP:MGI.
DR GO; GO:0042168; P:heme metabolic process; IMP:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:MGI.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0070328; P:triglyceride homeostasis; IMP:MGI.
DR GO; GO:0006805; P:xenobiotic metabolic process; IMP:MGI.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..670
FT /note="Solute carrier organic anion transporter family
FT member 1A6"
FT /id="PRO_0000191048"
FT TOPO_DOM 1..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 21..40
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 41..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..86
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 87..111
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..155
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..184
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 185..203
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..242
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 243..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..333
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..353
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..377
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 378..381
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..405
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 406..513
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 514..536
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..545
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 546..571
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 572..605
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 606..623
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 624..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 433..488
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 633..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 636..670
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 632
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 135
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 492
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 439..469
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 445..465
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 454..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 473..479
FT /note="VGTGANM -> QLPGNSQ (in Ref. 2; AK015176)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="Q -> Y (in Ref. 2; AK015176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 670 AA; 74145 MW; 98139F545DF96B1B CRC64;
MGEPGKRVGI HRVRCFAKIK VFLLALIWAY ISKILSGVYM STMLTQLERQ FNISTSIVGL
INGSFEMGNL LVIVFVSYFG TKLHRPIMIG VGCAVMGLGC FIISLPHFLM GRYEYETTIS
PTSNLSSNSF LCVENRSQTL KPTQDPAECV KEIKSLMWIY VLVGNIIRGI GETPIMPLGI
SYIEDFAKSE NSPLYIGILE VGKMIGPILG YLMGPFCANI YVDTGSVNTD DLTITPTDTR
WVGAWWIGFL VCAGVNVLTS IPFFFFPKTL PKEGLQDNGD GTENAKEEKH RDKAKEENQG
IIKEFFLMMK NLFCNPIYML CVLTSVLQVN GVANIVIYKP KYLEHHFGIS TAKAVFLIGL
YTTPSVSAGY LISGFIMKKL KITLKKAAII ALCLFMSECL LSLCNFMLTC DTTPIAGLTT
SYEGIQQSFD MENKFLSDCN TRCNCLTKTW DPVCGNNGLA YMSPCLAGCE KSVGTGANMV
FQNCSCIRSS GNSSAVLGLC KKGPDCANKL QYFLIITVFC CFFYSLATIP GYMVFLRCMK
SEEKSLGIGL QAFFMRLFAG IPAPIYFGAL IDRTCLHWGT LKCGEPGACR TYEVSSFRRL
YLGLPAALRG SIILPSFFIL RLIRKLQIPG DTDSSEIELA ETKPTEKESE CTDMHKSSKV
ENDGELKTKL
