SO3A1_RAT
ID SO3A1_RAT Reviewed; 710 AA.
AC Q99N02;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Solute carrier organic anion transporter family member 3A1;
DE AltName: Full=Organic anion-transporting polypeptide D;
DE Short=OATP-D;
DE AltName: Full=Prostaglandin transporter subtype 2;
DE AltName: Full=Sodium-independent organic anion transporter D;
DE AltName: Full=Solute carrier family 21 member 11;
GN Name=Slco3a1; Synonyms=Oatp3a1, Oatpd, Pgt2, Slc21a11;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Adachi H., Abe T.;
RT "Molecular identification of a novel human prostaglandin transporter
RT PGT2.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=16971491; DOI=10.1152/ajpcell.00597.2005;
RA Huber R.D., Gao B., Sidler Pfaendler M.-A., Zhang-Fu W., Leuthold S.,
RA Hagenbuch B., Folkers G., Meier P.J., Stieger B.;
RT "Characterization of two splice variants of human organic anion
RT transporting polypeptide 3A1 isolated from human brain.";
RL Am. J. Physiol. 292:C795-C806(2007).
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 -!- TISSUE SPECIFICITY: Expressed in many brain regions, including frontal
CC cortex, brain stem and cerebellum. Associated with neuronal bodies in a
CC punctated matter. Little expression, if any, in oligodendrocytes.
CC {ECO:0000269|PubMed:16971491}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AF239219; AAK15063.1; -; mRNA.
DR RefSeq; NP_803434.1; NM_177481.1.
DR AlphaFoldDB; Q99N02; -.
DR SMR; Q99N02; -.
DR STRING; 10116.ENSRNOP00000049659; -.
DR ChEMBL; CHEMBL2073689; -.
DR GlyGen; Q99N02; 7 sites.
DR jPOST; Q99N02; -.
DR PaxDb; Q99N02; -.
DR GeneID; 140915; -.
DR KEGG; rno:140915; -.
DR UCSC; RGD:620227; rat.
DR CTD; 28232; -.
DR RGD; 620227; Slco3a1.
DR eggNOG; KOG3626; Eukaryota.
DR InParanoid; Q99N02; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q99N02; -.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR PRO; PR:Q99N02; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
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:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0015732; P:prostaglandin transport; IDA:RGD.
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 2: Evidence at transcript level;
KW Acetylation; Cell membrane; Disulfide bond; Glycoprotein; Ion transport;
KW Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..710
FT /note="Solute carrier organic anion transporter family
FT member 3A1"
FT /id="PRO_0000191066"
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..501
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 477..497
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 486..511
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 710 AA; 76825 MW; 9E0CE36087E6BD17 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 PHSEPGMESE
QAMLPEREYE RPKPSNGVLR HPLEPDSSAS CFQQLRVIPK VTKHLLSNPV FTCIVLAACM
EIAVVAGFAA FLGKYLEQQF NLTTSSANQL LGMTAIPCAC LGIFLGGLLV KKLSLSALGA
IRMAMLVNLV STACYVSFLF LGCDTVPVAG VTVRYGNNSA RGSPLDPYSP CNNNCECQTD
SFTPVCGADG ITYLSACFAG CNSTNLTGCA CLTTVPPENA TVVPGKCPSP GCQEAFLTFL
CVMCVCSLIG AMAQTPSVII LIRTVSPELK SYALGVLFLL LRLLGFIPPP LIFGAGIDST
CLFWSTFCGE QGACVLYDNV VYRYLYVSIA IALKSFAFIL YTTTWQCLRK NYKRYIKNHE
GGLSTSEFLA STLTLDNLGR DPVPAHQTHR TKFIYNLEDH EWCENMESVL
