SO1C1_MOUSE
ID SO1C1_MOUSE Reviewed; 715 AA.
AC Q9ERB5; Q8BX54;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Solute carrier organic anion transporter family member 1C1;
DE AltName: Full=Organic anion transporter 2;
DE Short=OATP2;
DE AltName: Full=Organic anion transporter F;
DE Short=OATP-F;
DE AltName: Full=Organic anion-transporting polypeptide 14;
DE Short=OATP-14;
DE AltName: Full=Solute carrier family 21 member 14;
DE AltName: Full=Thyroxine transporter;
GN Name=Slco1c1; Synonyms=Oatp1c1, Oatpf, Slc21a14;
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=Cochlea;
RA Hampton L.L., Lattig M.C., Battey J.F.;
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
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 TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
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), estradiol-
CC 17-beta-glucuronide, 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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18687783};
CC Multi-pass membrane protein {ECO:0000269|PubMed:18687783}.
CC -!- TISSUE SPECIFICITY: Highly expressed in cerebral microvessels (at
CC protein level). Highly expressed in cerebral microvessels throughout
CC 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}.
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DR EMBL; AY007379; AAG09622.1; -; mRNA.
DR EMBL; AK048926; BAC33495.1; -; mRNA.
DR CCDS; CCDS20677.1; -.
DR RefSeq; NP_001171243.1; NM_001177772.1.
DR RefSeq; NP_067446.1; NM_021471.2.
DR AlphaFoldDB; Q9ERB5; -.
DR SMR; Q9ERB5; -.
DR BioGRID; 208444; 1.
DR STRING; 10090.ENSMUSP00000032362; -.
DR BindingDB; Q9ERB5; -.
DR ChEMBL; CHEMBL2073688; -.
DR GlyGen; Q9ERB5; 3 sites.
DR PhosphoSitePlus; Q9ERB5; -.
DR SwissPalm; Q9ERB5; -.
DR PaxDb; Q9ERB5; -.
DR PRIDE; Q9ERB5; -.
DR ProteomicsDB; 261102; -.
DR Antibodypedia; 23947; 115 antibodies from 21 providers.
DR DNASU; 58807; -.
DR Ensembl; ENSMUST00000032362; ENSMUSP00000032362; ENSMUSG00000030235.
DR GeneID; 58807; -.
DR KEGG; mmu:58807; -.
DR UCSC; uc009eop.2; mouse.
DR CTD; 53919; -.
DR MGI; MGI:1889679; Slco1c1.
DR VEuPathDB; HostDB:ENSMUSG00000030235; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244856; -.
DR InParanoid; Q9ERB5; -.
DR OMA; NAGCEKE; -.
DR OrthoDB; 1029129at2759; -.
DR PhylomeDB; Q9ERB5; -.
DR Reactome; R-MMU-879518; Transport of organic anions.
DR BioGRID-ORCS; 58807; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Slco1c1; mouse.
DR PRO; PR:Q9ERB5; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q9ERB5; protein.
DR Bgee; ENSMUSG00000030235; Expressed in brain blood vessel and 101 other tissues.
DR ExpressionAtlas; Q9ERB5; baseline and differential.
DR Genevisible; Q9ERB5; MM.
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; ISO:MGI.
DR GO; GO:0015125; F:bile acid transmembrane transporter activity; ISO:MGI.
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:MGI.
DR GO; GO:0015721; P:bile acid and bile salt transport; ISO:MGI.
DR GO; GO:2000611; P:positive regulation of thyroid hormone generation; ISO:MGI.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0070327; P:thyroid hormone transport; ISO:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO: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 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..715
FT /note="Solute carrier organic anion transporter family
FT member 1C1"
FT /id="PRO_0000191056"
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..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 352..373
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 374..393
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..417
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 418..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..445
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 446..557
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..580
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 581..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 590..615
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 616..649
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 650..667
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 668..715
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 473..528
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CARBOHYD 452
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 536
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 479..509
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 485..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 494..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 603
FT /note="Missing (in Ref. 2; BAC33495)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 78320 MW; 8659472884FAD7FE CRC64;
MDTSSKENAH LFHKNSAQPA GGPSFTVGYP STEEARPCCG KLKVFLGALS FVYFAKALAE
GYLKSTVTQI ERRFEIPSSL VGIIDGSFEI GNLLVITFVS YFGAKLHRPK IIGAGCLVMG
FGTMLIAVPQ FFMEKYSYEK YERYSPSSNV TPSISPCYLE SSSPSPSSIL GKSQNKISHE
CVGDSSSSMW VYVFLGNLLR GLGETPIQPL GIAYLDDFAS EDNAAFYIGC VQTVAIIGPI
FGFLLGSLCA KLYVDIGFVN LDHITITPKD PQWVGAWWLG YLIAGFLSLL AAVPFWCLPK
TLPRSQSREN SGSTSEKSKF IDDPIHYQMA PGDDKMKIME MAKDFLPSLK TLFRNPVYIL
YLCASTVQFN SLFGMVTYKP KYIEQQYGQS SSKANFVIGL INIPAVALGI FSGGIVMKKF
RLGICEATKL YLGSSVFGYL LFLSLFALGC ENSSVAGLTV SYQGTKPVSY HERALFSDCN
SRCKCSDSKW EPMCGDNGIT YVSACLAGCQ SSSRSGKNII FSNCTCVGFA APKSGNWSGM
MGRCQKDNGC SQMFLYFLVI SVITSYTLSL GGIPGYILLL RCIQPQLKSF ALGIYTLAVR
VLAGIPAPVY FGVLIDTSCL KWGFKKCGSR GSCRLYDSHA FRHIYLGLTT LLGTVSVFLS
MAVLFVLKKK YVSKHSSLIT TREKIGMSSS IKKETCAARD RGLQPKYWPG KETRL
