SO1C1_RAT
ID SO1C1_RAT Reviewed; 716 AA.
AC Q9EPZ7;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Solute carrier organic anion transporter family member 1C1;
DE AltName: Full=BBB-specific anion transporter type 1;
DE AltName: Full=Blood-brain barrier-specific anion transporter 1;
DE AltName: Full=Solute carrier family 21 member 14;
DE AltName: Full=Thyroxine transporter;
GN Name=Slco1c1; Synonyms=Bsat1, Oatp1c1, Oatpf, Slc21a14;
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].
RC STRAIN=Sprague-Dawley; TISSUE=Brain capillary;
RX PubMed=11149669; DOI=10.1097/00004647-200101000-00008;
RA Li J.Y., Boado R.J., Pardridge W.M.;
RT "Blood-brain barrier genomics.";
RL J. Cereb. Blood Flow Metab. 21:61-68(2001).
RN [2]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=18687783; DOI=10.1210/en.2008-0378;
RA Roberts L.M., Woodford K., Zhou M., Black D.S., Haggerty J.E., Tate E.H.,
RA Grindstaff K.K., Mengesha W., Raman C., Zerangue N.;
RT "Expression of the thyroid hormone transporters monocarboxylate
RT transporter-8 (SLC16A2) and organic ion transporter-14 (SLCO1C1) at the
RT blood-brain barrier.";
RL Endocrinology 149:6251-6261(2008).
CC -!- FUNCTION: Mediates the Na(+)-independent high affinity transport of
CC organic anions such as the thyroid hormones thyroxine (T4) and rT3.
CC Other potential substrates, such as triiodothyronine (T3), 17-beta-
CC glucuronosyl estradiol, estrone-3-sulfate and sulfobromophthalein (BSP)
CC are transported with much lower efficiency (By similarity). May play a
CC significant role in regulating T4 flux into and out of the brain.
CC {ECO:0000250, ECO:0000269|PubMed:18687783}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18687783}.
CC Note=Expressed in both luminal and abluminal membranes of brain
CC capillary endothelial cells. Localized to the apical membrane and basal
CC surfaces of choroid plexus.
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebral microvessels (at
CC protein level). Brain-specific. Not detected in glioma cells, kidney,
CC heart, lung or liver. Highly expressed in cerebral microvessels
CC throughout the brain and in tanycytes of the third ventricle.
CC {ECO:0000269|PubMed:18687783}.
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; AF306546; AAG37066.1; -; mRNA.
DR RefSeq; NP_445893.1; NM_053441.1.
DR AlphaFoldDB; Q9EPZ7; -.
DR SMR; Q9EPZ7; -.
DR BioGRID; 250000; 1.
DR STRING; 10116.ENSRNOP00000013230; -.
DR TCDB; 2.A.60.1.10; the organo anion transporter (oat) family.
DR GlyGen; Q9EPZ7; 3 sites, 2 N-linked glycans (1 site).
DR PhosphoSitePlus; Q9EPZ7; -.
DR PaxDb; Q9EPZ7; -.
DR GeneID; 84511; -.
DR KEGG; rno:84511; -.
DR UCSC; RGD:628660; rat.
DR CTD; 53919; -.
DR RGD; 628660; Slco1c1.
DR eggNOG; KOG3626; Eukaryota.
DR InParanoid; Q9EPZ7; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9EPZ7; -.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR PRO; PR:Q9EPZ7; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; IDA:RGD.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:RGD.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISO:RGD.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0070327; P:thyroid hormone transport; ISO:RGD.
DR GO; GO:0055085; P:transmembrane transport; ISO:RGD.
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 InterPro; IPR030764; OATP1C1.
DR PANTHER; PTHR11388; PTHR11388; 1.
DR PANTHER; PTHR11388:SF99; PTHR11388:SF99; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..716
FT /note="Solute carrier organic anion transporter family
FT member 1C1"
FT /id="PRO_0000191057"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..63
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..134
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..187
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..216
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 217..235
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 257..274
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..299
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..352
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 353..374
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..394
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..418
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..422
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..446
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..558
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 559..581
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 582..590
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 591..616
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..650
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 651..668
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 669..716
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 474..529
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 524
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 537
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 480..510
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 486..506
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 495..527
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 716 AA; 78627 MW; 487734B82A50A6EA CRC64;
MDTSSKENAH LFHKNSAQPA GGPSFKAGYP STEEARPCCG KLKVFLGALS FVYFAKALTE
GYLKSTITQI ERRFDIPSSL VGIIDGSFEI GNLLVITFVS YFGAKLHRPK IIGAGCLVMG
FGTMLIAVPQ FFMEKYSYEK YERYSPSSNL TPNISPCYLE SSSPSPRSIV GKSQNKINDE
CEVDTSSSMW VYVFLGNLLR GLGETPIQPL GIAYLDDFAS EDNAAFYIGC VQTVAIIGPI
FGFLLGSLCA KLYVDIGFVN LDHITITPKD PQWVGAWWLG YLIAGFLSLL AAVPFWCLPK
TLPRSQSRED SGSSSEKSKF ITDDPVNYQM APREESMKIM EMARDFLPSL KSLFRNPVYI
LYLCASTVQF NSLFGMVTYK PKYIEQQYGQ SSSKANFVIG LINIPAVALG IFSGGIVMKK
FRLGICEATK LYLGSSVFGY LLFLSLFALG CENSSVAGLT VSYQGTKPVS YHERALFSDC
NSRCKCSDSK WEPMCGDNGI TYASACLAGC QSSSRSGKNI IFSNCTCVGF AAPKSGNWSG
MMGRCQKDNG CSQMFLYFLV ISVITSYTLS LGGIPGYILL LRCIQPQLKS FALGIYTLAV
RVLAGIPAPV YFGVLIDTSC LKWGFKKCGS RGSCRLYDSH AFRHIYLGLT TLLGTVSVFL
STAVLLVLKK KYVSKRSSFI TAREKIVMSS SVKKETCAAR DHGLQPKYWP GKETRL
