SO1C1_MACFA
ID SO1C1_MACFA Reviewed; 602 AA.
AC Q9GMU6;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Solute carrier organic anion transporter family member 1C1;
DE AltName: Full=Solute carrier family 21 member 14;
DE AltName: Full=Thyroxine transporter;
GN Name=SLCO1C1; Synonyms=OATP1C1, SLC21A14; ORFNames=QnpA-13170;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Parietal cortex;
RA Osada N., Hida M., Kusuda J., Tanuma R., Iseki K., Hirai M., Terao K.,
RA Suzuki Y., Sugano S., Hashimoto K.;
RT "Isolation of full-length cDNA clones from macaque brain cDNA libraries.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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. May play a significant role
CC in regulating T4 flux into and out of the brain (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
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 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000305}.
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DR EMBL; AB047629; BAB12153.1; -; mRNA.
DR AlphaFoldDB; Q9GMU6; -.
DR SMR; Q9GMU6; -.
DR eggNOG; KOG3626; Eukaryota.
DR Proteomes; UP000233100; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IEA:InterPro.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004156; OATP.
DR InterPro; IPR030764; OATP1C1.
DR PANTHER; PTHR11388; PTHR11388; 2.
DR PANTHER; PTHR11388:SF99; PTHR11388:SF99; 2.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF03137; OATP; 2.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF103473; SSF103473; 2.
DR TIGRFAMs; TIGR00805; oat; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..602
FT /note="Solute carrier organic anion transporter family
FT member 1C1"
FT /id="PRO_0000191055"
FT TOPO_DOM 1..43
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 44..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..82
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 104..109
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 110..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..139
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..156
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 157..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 239..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 261..280
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..308
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 309..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 333..444
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..467
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 468..476
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 477..502
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 503..536
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 537..554
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 555..602
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 360..415
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 190..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 400
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 410
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 366..396
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 372..392
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 381..413
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 602 AA; 66739 MW; 1E02E84170F6C31D CRC64;
MDTSSKENIQ LFCKTSVQPV GRPSFKTEYP SSEEKQPCCG ELKVFLGALS FVYFAKALAE
GYLKSTITQI ERRFDIPSSL VGVIDGSFEI GNLLVITFVS YFGAKLHRPK IIGAGCLIMG
VGTLLIAMPQ FFMEQYKYEI YSPSSNSTLS ISPCLLESSS QLPVSVMEKS KSKISLLAAV
PFWYLPKSLP RSQSREDSNS SSEKSKFIRD DHTDYQTPQG ENVKIMEMAR DFLPSLKYLF
GNPVYFLYLC TSTVQFNSLF GMVTYKPKYI EQQYGQSSSR ANFVIGLINI PAVALGIFSG
GIAMKKFRIS VCGAAKLYLG SSVFGYLLFL SLFALGCENS DVAGLTVSYQ GTKPVSYHER
ALFSDCNPRC KCSETKWEPM CGENGITYVS ACPAGCQTSN RSGKNIIFYN CTCVGIAASK
SGNSSGIVGR CQKDNGCPQM FLYFLVISVI TSYTLSLGGI PGYILLLRCI KPQLKSFALG
IYTLSIRVLA GIPAPVYFGV LIDTSCLKWG FKRCGSRGSC RLYDSNVFRH IYLGLTVILG
TVSIFLSIAV LFILKKNYVS KHRNFITKRE RTMVSTRFQK ENCTTSDHLL QPKYWPGKET
QL
