SO4C1_MOUSE
ID SO4C1_MOUSE Reviewed; 722 AA.
AC Q8BGD4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Solute carrier organic anion transporter family member 4C1;
DE AltName: Full=Oatp-R;
DE AltName: Full=Solute carrier family 21 member 20;
GN Name=Slco4c1 {ECO:0000312|MGI:MGI:2442784};
GN Synonyms=Oatp4c1 {ECO:0000250|UniProtKB:Q6ZQN7},
GN Slc21a20 {ECO:0000250|UniProtKB:Q6ZQN7};
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] {ECO:0000312|EMBL:AAT73731.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ {ECO:0000312|EMBL:AAT73731.1};
RA Ishiyama K., Suzuki T., Mikkaichi T., Tanemoto M., Abe T.;
RT "Mouse organic anion transporter oatp-R.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:BAC33637.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33637.1};
RC TISSUE=Embryonic stem cell {ECO:0000269|PubMed:16141072}, and
RC Hippocampus {ECO:0000312|EMBL:BAC33997.1};
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] {ECO:0000312|EMBL:AAI19023.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:AAI19023.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4] {ECO:0000305}
RP FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=16641146; DOI=10.1095/biolreprod.105.047811;
RA Sipila P., Pujianto D.A., Shariatmadari R., Nikkila J., Lehtoranta M.,
RA Huhtaniemi I.T., Poutanen M.;
RT "Differential endocrine regulation of genes enriched in initial segment and
RT distal caput of the mouse epididymis as revealed by genome-wide expression
RT profiling.";
RL Biol. Reprod. 75:240-251(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-19; SER-24; SER-26
RP AND SER-28, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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:0000269|PubMed:16641146}.
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q71MB6}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q71MB6}. Note=Detected at the basolateral
CC membrane of the proximal tubule cell in the kidney.
CC {ECO:0000250|UniProtKB:Q71MB6}.
CC -!- TISSUE SPECIFICITY: Strongly expressed in initial segment of epididymis
CC and seminal vesicles. {ECO:0000269|PubMed:16641146}.
CC -!- INDUCTION: Dramatically down-regulated 1 day after gonadectomy.
CC {ECO:0000269|PubMed:16641146}.
CC -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000255}.
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DR EMBL; AY654588; AAT73731.1; -; mRNA.
DR EMBL; AK049253; BAC33637.1; -; mRNA.
DR EMBL; AK049944; BAC33997.1; -; mRNA.
DR EMBL; BC119022; AAI19023.1; -; mRNA.
DR CCDS; CCDS35675.1; -.
DR RefSeq; NP_766246.1; NM_172658.3.
DR AlphaFoldDB; Q8BGD4; -.
DR SMR; Q8BGD4; -.
DR STRING; 10090.ENSMUSP00000071875; -.
DR iPTMnet; Q8BGD4; -.
DR PhosphoSitePlus; Q8BGD4; -.
DR jPOST; Q8BGD4; -.
DR MaxQB; Q8BGD4; -.
DR PaxDb; Q8BGD4; -.
DR PRIDE; Q8BGD4; -.
DR ProteomicsDB; 261473; -.
DR Antibodypedia; 48357; 66 antibodies from 16 providers.
DR DNASU; 227394; -.
DR Ensembl; ENSMUST00000071985; ENSMUSP00000071875; ENSMUSG00000040693.
DR GeneID; 227394; -.
DR KEGG; mmu:227394; -.
DR UCSC; uc007cfc.1; mouse.
DR CTD; 353189; -.
DR MGI; MGI:2442784; Slco4c1.
DR VEuPathDB; HostDB:ENSMUSG00000040693; -.
DR eggNOG; KOG3626; Eukaryota.
DR GeneTree; ENSGT01050000244906; -.
DR HOGENOM; CLU_008954_1_2_1; -.
DR InParanoid; Q8BGD4; -.
DR OMA; VTCKVIT; -.
DR OrthoDB; 228564at2759; -.
DR PhylomeDB; Q8BGD4; -.
DR TreeFam; TF317540; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-879518; Transport of organic anions.
DR BioGRID-ORCS; 227394; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Slco4c1; mouse.
DR PRO; PR:Q8BGD4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BGD4; protein.
DR Bgee; ENSMUSG00000040693; Expressed in seminal vesicle and 103 other tissues.
DR Genevisible; Q8BGD4; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; ISO:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
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; ISO:MGI.
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..722
FT /note="Solute carrier organic anion transporter family
FT member 4C1"
FT /id="PRO_0000337152"
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..578
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 579..601
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 602..610
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..636
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 637..670
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 671..688
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 689..722
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..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q71MB6"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 19
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 24
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 26
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 28
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 722 AA; 78412 MW; A48F2F5853DBAE7D CRC64;
MQGSKGIENP AFVPSSPGTP RRASASPSQV EVSAVASRNQ NGGSQPRESE EPQKSTEPSP
PSSNPPASDE PPGSQLSELE EGPCGWRGFH PQCLQRCNTP QGFLLHYCLL ALTQGIVVNG
LVNISISTIE KRYEMKSSLT GLISSSYDIS FCVLSLFVSF FGERGHKPRW LAFASFMIGL
GALVFSLPHF FSGRYELGSI FEDTCLTRNS TRCSSSTSLL SNYFYVFVLG QLLLGTGGTP
LYTLGTAFID DSVPTHKSSL YIGIGYSMSI LGPAIGYVLG GQLLTMYIDI AMGQSSDLTE
DDPRWLGAWW IGFLLAWLFA WSLIMPFSCF PKHLPGTAKI QAGKTSQTHQ NNSTSFQHTD
ENFGKSIKDF PTAVKNLMRN TVFICLVLST TSEALITTGF ATFLPKFIEN QFGLTSSFAA
TLGGAVLIPG AALGQILGGV LVSKFKMKCK NTMKFALCTS GVALVLSFVF IYAKCENEPF
AGVSESYNGT GEMGNLTAPC NANCNCLRSY YYPLCGSDGI QYFSPCFAGC LNSVSNRKPK
VYYNCSCIER KITSTAESTD FEAKAGKCRT RCSNLPIFLG IFFITVIFTF MAGTPITVSI
LRCVNHRHRS LALGVQFMLL RLLGTIPGPI IFGVIIDSTC VLWDVNECGI KGACWIYDNI
KMAHMLVAIS VTCKVITIFF NGLAIVLYKP PPPGTEVSFQ SQNVIVSTIS VEEDLDKAEN
EG
