SO4C1_PONAB
ID SO4C1_PONAB Reviewed; 724 AA.
AC Q5RFF0; Q5R7Z2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Solute carrier organic anion transporter family member 4C1;
DE AltName: Full=Solute carrier family 21 member 20;
GN Name=SLCO4C1 {ECO:0000250|UniProtKB:Q6ZQN7};
GN Synonyms=OATP4C1 {ECO:0000250|UniProtKB:Q6ZQN7},
GN SLC21A20 {ECO:0000250|UniProtKB:Q6ZQN7};
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1] {ECO:0000312|EMBL:CAH89507.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:CAH89507.1};
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC {ECO:0000250|UniProtKB:Q6ZQN7, ECO:0000250|UniProtKB:Q8BGD4}.
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 -!- SIMILARITY: Belongs to the organo anion transporter (TC 2.A.60) family.
CC {ECO:0000255}.
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DR EMBL; CR857208; CAH89507.1; -; mRNA.
DR EMBL; CR859966; CAH92118.1; -; mRNA.
DR RefSeq; NP_001128739.1; NM_001135267.2.
DR AlphaFoldDB; Q5RFF0; -.
DR SMR; Q5RFF0; -.
DR STRING; 9601.ENSPPYP00000017512; -.
DR PRIDE; Q5RFF0; -.
DR GeneID; 100189631; -.
DR KEGG; pon:100189631; -.
DR CTD; 353189; -.
DR eggNOG; KOG3626; Eukaryota.
DR InParanoid; Q5RFF0; -.
DR OrthoDB; 228564at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
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 2: Evidence at transcript 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_0000337153"
FT TOPO_DOM 1..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..145
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..172
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 173..197
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 198..224
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..254
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 255..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 296..311
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 312..336
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 337..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..399
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 400..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 420..443
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..471
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 472..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 495..549
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT REGION 24..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..56
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: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 501..530
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 507..526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 516..547
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 617
FT /note="I -> T (in Ref. 1; CAH92118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 724 AA; 78786 MW; DDD5240BC2764E77 CRC64;
MKSAKGIENL AFVPSSPDIL RRLSASPSQV EVSALSSDPQ RENSQPQELQ KPQEPQKSPE
PSLPSAPPNV SEEKLRSLSL SDFEEGPYGW RNFHPQCLQR CNTPGGFLLH YCLLAVTQGI
VVNGLVNISI STIEKRYEMK SSLTGLISSS YDISFCLLSL FVSFFGERGH KPRWLAFAAF
MIGLGALVFS LPQFFSGEYK LGSLFEDTCV TTRNSTSCTS STSSLSNYLY VFILGQLLLG
AGGTPLYTLG TAFLDDSVPT HKSSLYIGTG YAMSILGPAI GYVLGGQLLT IYVDVAMGES
TDITEDDPRW LGAWWIGFLL SWIFAWSLII PFSCFPKHLP GTAEIQAGKT SQAHQSNSNA
DAKFGKSIKD FPAALKNLMK NAVFMCLVLS TSSEALITTG FATFLPKFIE NQFGLTSSFA
ATLGGAVLIP GAALGQILGG FLVSKFKMTC KNTMKFALFT SGVALTLSFV FIYAKCGNEP
FAGVSESYNG TGELGNLIAP CNANCNCLRS YYYPVCGDGV QYFSPCFAGC SNSVAHRKPK
VYYNCSCIER KTETTSTAET FGFEAKAGKC ETHCAKLPIF LCIFFIVIIF TFMAGTPITV
SILRCVNHRQ RSLALGIQFM VLRLLGTIPG PIIFGFTIDS TCILWDINDC GIKGACRIYD
NIKMAHMLVA ISVTCKVITM FFNGFAIFLY KPPPSATDLS FHKENAVVTN VLAEQDLNKI
VKEG
