SO3A1_MOUSE
ID SO3A1_MOUSE Reviewed; 710 AA.
AC Q8R3L5; Q3TLX2; Q3U7W0; Q505P2; Q544H3; Q9CTV3; Q9JKV0;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Solute carrier organic anion transporter family member 3A1;
DE AltName: Full=MJAM;
DE AltName: Full=Organic anion-transporting polypeptide D;
DE Short=OATP-D;
DE AltName: Full=Sodium-independent organic anion transporter D;
DE AltName: Full=Solute carrier family 21 member 11;
GN Name=Slco3a1; Synonyms=Oatp3a1, Oatpd, Slc21a11;
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] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Kidney;
RA Isern J., Menoyo A., Melia M.J., Meseguer A.;
RT "Mus musculus organic anion transporting polypeptide MJAM.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 14-710 (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Macrophage, Mammary gland, and Thymus;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 7-710 (ISOFORM 2).
RC TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
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: Mediates the Na(+)-independent transport of organic anions.
CC Mediates transport of prostaglandins (PG) E1 and E2, thyroxine (T4),
CC deltorphin II, BQ-123 and vasopressin. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8R3L5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3L5-2; Sequence=VSP_036839, VSP_036840;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- INDUCTION: By androgens in kidney and lung.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF226324; AAF35370.1; -; mRNA.
DR EMBL; AK020010; BAB31965.1; -; mRNA.
DR EMBL; AK037938; BAC29904.1; -; mRNA.
DR EMBL; AK152488; BAE31259.1; -; mRNA.
DR EMBL; AK166266; BAE38670.1; -; mRNA.
DR EMBL; BC025059; AAH25059.1; -; mRNA.
DR EMBL; BC094464; AAH94464.1; -; mRNA.
DR CCDS; CCDS21366.1; -. [Q8R3L5-2]
DR CCDS; CCDS21367.1; -. [Q8R3L5-1]
DR RefSeq; NP_001033732.1; NM_001038643.1. [Q8R3L5-2]
DR RefSeq; NP_076397.2; NM_023908.2. [Q8R3L5-1]
DR AlphaFoldDB; Q8R3L5; -.
DR SMR; Q8R3L5; -.
DR STRING; 10090.ENSMUSP00000026897; -.
DR GlyGen; Q8R3L5; 7 sites.
DR iPTMnet; Q8R3L5; -.
DR PhosphoSitePlus; Q8R3L5; -.
DR SwissPalm; Q8R3L5; -.
DR EPD; Q8R3L5; -.
DR MaxQB; Q8R3L5; -.
DR PaxDb; Q8R3L5; -.
DR PRIDE; Q8R3L5; -.
DR ProteomicsDB; 261311; -. [Q8R3L5-1]
DR ProteomicsDB; 261312; -. [Q8R3L5-2]
DR Antibodypedia; 29012; 77 antibodies from 16 providers.
DR DNASU; 108116; -.
DR Ensembl; ENSMUST00000026897; ENSMUSP00000026897; ENSMUSG00000025790. [Q8R3L5-1]
DR Ensembl; ENSMUST00000098371; ENSMUSP00000095973; ENSMUSG00000025790. [Q8R3L5-2]
DR GeneID; 108116; -.
DR KEGG; mmu:108116; -.
DR UCSC; uc009hwf.1; mouse. [Q8R3L5-2]
DR UCSC; uc009hwg.1; mouse. [Q8R3L5-1]
DR CTD; 28232; -.
DR MGI; MGI:1351867; Slco3a1.
DR VEuPathDB; HostDB:ENSMUSG00000025790; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR HOGENOM; CLU_008954_3_0_1; -.
DR InParanoid; Q8R3L5; -.
DR OMA; CNINCEC; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q8R3L5; -.
DR TreeFam; TF317540; -.
DR Reactome; R-MMU-879518; Transport of organic anions.
DR BioGRID-ORCS; 108116; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Slco3a1; mouse.
DR PRO; PR:Q8R3L5; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8R3L5; protein.
DR Bgee; ENSMUSG00000025790; Expressed in superior cervical ganglion and 249 other tissues.
DR ExpressionAtlas; Q8R3L5; baseline and differential.
DR Genevisible; Q8R3L5; 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:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISO:MGI.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0015732; P:prostaglandin transport; ISO:MGI.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
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.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell membrane; Disulfide bond;
KW Glycoprotein; Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..710
FT /note="Solute carrier organic anion transporter family
FT member 3A1"
FT /id="PRO_0000191065"
FT TOPO_DOM 1..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..79
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..106
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..131
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 132..174
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 175..203
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 204..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..261
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..286
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 287..344
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..366
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 367..386
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..410
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 411..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..438
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..539
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 540..562
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 563..571
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 572..597
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 598..630
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 631..648
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 649..705
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 465..513
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9UIG8"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 169
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 381
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 457
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 502
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 519
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 471..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 475..486
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 477..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT VAR_SEQ 667..692
FT /note="EFFASTLTLDNLGRDPVPAHQTHRTK -> TEYQDIETEKTCPESQSPSEDS
FT FVRS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036839"
FT VAR_SEQ 693..710
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_036840"
FT CONFLICT 7
FT /note="G -> D (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 14
FT /note="R -> G (in Ref. 2; BAE38670)"
FT /evidence="ECO:0000305"
FT CONFLICT 138
FT /note="G -> V (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="G -> E (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="R -> T (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 159..160
FT /note="EG -> DR (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> M (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 428
FT /note="N -> K (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="F -> L (in Ref. 1; AAF35370)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="D -> G (in Ref. 2; BAE31259)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="Q -> L (in Ref. 2; BAE31259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 76763 MW; AC89FB5026441C59 CRC64;
MQGKKPGGSS GGGRSGELQG DEAQRNKKKK KKVSCFSNIK IFLVSECALM LAQGTVGAYL
VSVLTTLERR FNLQSADVGV IASSFEIGNL ALILFVSYFG ARGHRPRLIG CGGIVMALGA
LLSALPEFLT HQYKYEAGEI RWGAEGRDVC ATNGSSSDEG PDPDLICRNR TATNMMYLLL
IGAQVLLGIG ATPVQPLGVS YIDDHVRRKD SSLYIGILFT MLVFGPACGF ILGSFCTKIY
VDAVFIDTSN LDITPDDPRW IGAWWGGFLL CGALLFFSSL LMFGFPQSLP PHSDPGMESE
QAMLPEREYE RPKPSNGVLR HPLEPDSSAS CFQQLRVIPK VTKHLLSNPV FTCIVLAACM
EIAVVAGFAA FLGKYLEQQF NLTTSSANQL LGMTAIPCAC LGIFLGGLLV KKLSLSALGA
IRMAMLVNLV STACYVSFLF LGCDTGPVAG VTVRYGNNSA RGSALDPYSP CNNNCECQTD
SFTPVCGADG ITYLSACFAG CNSTNLTGCA CLTTVPPENA SVVPGKCPSP GCQEAFLTFL
CVMCVCSLIG AMAQTPSVII LIRTVSPELK SYALGVLFLL LRLLGFIPPP LIFGAGIDST
CLFWSTFCGE QGACVLYDNV VYRYLYVSIA IALKSFAFIL YTTTWQCLRK NYKRYIKNHE
GGLSTSEFFA STLTLDNLGR DPVPAHQTHR TKFIYNLEDH EWCENMESVL
