SO4C1_RAT
ID SO4C1_RAT Reviewed; 724 AA.
AC Q71MB6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 117.
DE RecName: Full=Solute carrier organic anion transporter family member 4C1;
DE AltName: Full=Solute carrier family 21 member 20;
GN Name=Slco4c1 {ECO:0000312|RGD:1303048};
GN Synonyms=Oatp4c1 {ECO:0000303|PubMed:14993604},
GN Slc21a20 {ECO:0000250|UniProtKB:Q6ZQN7};
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] {ECO:0000305, ECO:0000312|EMBL:AAQ04697.1}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RC TISSUE=Kidney {ECO:0000269|PubMed:14993604};
RX PubMed=14993604; DOI=10.1073/pnas.0304987101;
RA Mikkaichi T., Suzuki T., Onogawa T., Tanemoto M., Mizutamari H., Okada M.,
RA Chaki T., Masuda S., Tokui T., Eto N., Abe M., Satoh F., Unno M.,
RA Hishinuma T., Inui K., Ito S., Goto J., Abe T.;
RT "Isolation and characterization of a digoxin transporter and its rat
RT homologue expressed in the kidney.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:3569-3574(2004).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-15 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Organic anion transporter, capable of transporting
CC pharmacological substances such as digoxin, ouabain, thyroxine,
CC methotrexate and cAMP. May participate in the regulation of membrane
CC transport of ouabain. Involved in the uptake of the dipeptidyl
CC peptidase-4 inhibitor sitagliptin and hence may play a role in its
CC transport into and out of renal proximal tubule cells. May be involved
CC in the first step of the transport pathway of digoxin and various
CC compounds into the urine in the kidney. May be involved in sperm
CC maturation by enabling directed movement of organic anions and
CC compounds within or between cells. This ion-transporting process is
CC important to maintain the strict epididymal homeostasis necessary for
CC sperm maturation. May have a role in secretory functions since seminal
CC vesicle epithelial cells are assumed to secrete proteins involved in
CC decapacitation by modifying surface proteins to facilitate the
CC acquisition of the ability to fertilize the egg.
CC {ECO:0000250|UniProtKB:Q6ZQN7, ECO:0000250|UniProtKB:Q8BGD4,
CC ECO:0000269|PubMed:14993604}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8.0 uM for digoxin {ECO:0000269|PubMed:14993604};
CC KM=1.9 uM for thyroxine {ECO:0000269|PubMed:14993604};
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:14993604}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:14993604}. Note=Detected at the basolateral
CC membrane of the proximal tubule cell in the kidney.
CC {ECO:0000269|PubMed:14993604}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in kidney and lung but also
CC weakly expressed in brain. {ECO:0000269|PubMed:14993604}.
CC -!- INDUCTION: Expression is significantly decreased in renal failure.
CC {ECO:0000269|PubMed:14993604}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000255}.
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DR EMBL; AF454761; AAQ04697.1; -; mRNA.
DR RefSeq; NP_001002024.1; NM_001002024.1.
DR STRING; 10116.ENSRNOP00000037089; -.
DR ChEMBL; CHEMBL2073710; -.
DR iPTMnet; Q71MB6; -.
DR PhosphoSitePlus; Q71MB6; -.
DR PaxDb; Q71MB6; -.
DR GeneID; 432363; -.
DR KEGG; rno:432363; -.
DR UCSC; RGD:1303048; rat.
DR CTD; 353189; -.
DR RGD; 1303048; Slco4c1.
DR eggNOG; KOG3626; Eukaryota.
DR InParanoid; Q71MB6; -.
DR OrthoDB; 228564at2759; -.
DR PhylomeDB; Q71MB6; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-879518; Transport of organic anions.
DR SABIO-RK; Q71MB6; -.
DR PRO; PR:Q71MB6; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IDA:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0015711; P:organic anion transport; IDA:RGD.
DR GO; GO:0043252; P:sodium-independent organic anion transport; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 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.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Differentiation; Disulfide bond;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Spermatogenesis; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..724
FT /note="Solute carrier organic anion transporter family
FT member 4C1"
FT /id="PRO_0000337154"
FT TOPO_DOM 1..101
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..162
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..193
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 194..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..249
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..269
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..306
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 307..331
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..376
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 377..398
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..418
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 419..442
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..446
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 447..470
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..580
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 581..603
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 604..612
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 613..638
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 639..672
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 673..690
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 691..724
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 494..549
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD4"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD4"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD4"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BGD4"
FT DISULFID 500..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 506..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 515..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 724 AA; 78648 MW; 656E3A02D95A931F CRC64;
MQGSKGVENP AFVPSSPDTP RRASASPSQV EVSAVASRNQ NGGSQPRESE DPQKSTEPSP
PSSTLPASDE PPGSQLSELE EGPCGWRNFH PQCLQRCNNP KGFLLHYCLL ALTQGIVVNG
LVNISISTIE KRYEMKSSLT GLISSSYDIS FCVLSLFVSF FGERGHKPRW LAFASFMIGL
GALVFSLPHF FSGRYELGTI FEDTCLTRNS TRCASSTSLL SNYFYVFVLG QLLLGTGGTP
LYTLGTAFID DSVPTHKSSL YIGIGYSMSI LGPAIGYVLG GQLLTMYIDV AMGQSSDLTE
DDPRWLGAWW IGFLLAWLFA WSLIMPFSCF PKHLPGTAKI QAGKTSQTHQ NNSTSFQHMD
ENFGKSIKDF PTAVKNLMRN TVFICLVLST TSEALVTTGF ATFLPKFIEN QFGLTSSFAA
TLGGAVLIPG AALGQILGGV LVSKFKMKCK NTMKFALCTS GVALMLSFVF IYAKCENGPF
AGVSESYNGT GEMGNLTAPC NANCNCLRSY YYPLCGSDGV QYFSPCFAGC LNSVSNRKPK
AYYNCSCIER KVDITSTAXS PDFEARAGKC KTQCSNLPIF LGIFFITVIF TFMAGTPITV
SILRCVNHRQ RSLALGVQFM LLRLLGTIPG PIIFGVTIDS TCVLWDINEC GTKGACWIYD
NIRMAHMLVA ISVTCKVITI FFNGLAIVLY KPPPPGTEVS FQSQNVVVST ITVEEDLNKI
ENEG
