ID   S22A6_RAT               Reviewed;         551 AA.
AC   O35956;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Solute carrier family 22 member 6 {ECO:0000250|UniProtKB:Q4U2R8};
DE   AltName: Full=Organic anion transporter 1 {ECO:0000303|PubMed:9374486};
DE            Short=rOAT1 {ECO:0000303|PubMed:9374486};
DE   AltName: Full=renal organic anion transporter 1 {ECO:0000303|PubMed:9374486};
DE            Short=rROAT1;
GN   Name=Slc22a6 {ECO:0000312|RGD:69338}; Synonyms=Oat1;
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]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND
RP   MISCELLANEOUS.
RC   TISSUE=Kidney;
RX   PubMed=9374486; DOI=10.1074/jbc.272.48.30088;
RA   Sweet D.H., Wolff N.A., Pritchard J.B.;
RT   "Expression cloning and characterization of ROAT1. The basolateral organic
RT   anion transporter in rat kidney.";
RL   J. Biol. Chem. 272:30088-30095(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, TISSUE
RP   SPECIFICITY, AND MISCELLANEOUS.
RC   STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX   PubMed=9228014; DOI=10.1074/jbc.272.30.18526;
RA   Sekine T., Watanabe N., Hosoyamada M., Kanai Y., Endou H.;
RT   "Expression cloning and characterization of a novel multispecific organic
RT   anion transporter.";
RL   J. Biol. Chem. 272:18526-18529(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
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]
RP   MISCELLANEOUS.
RX   PubMed=10462545; DOI=10.1124/mol.56.3.570;
RA   Cihlar T., Lin D.C., Pritchard J.B., Fuller M.D., Mendel D.B., Sweet D.H.;
RT   "The antiviral nucleotide analogs cidofovir and adefovir are novel
RT   substrates for human and rat renal organic anion transporter 1.";
RL   Mol. Pharmacol. 56:570-580(1999).
RN   [5]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=14675047; DOI=10.1111/j.1523-1755.2004.00354.x;
RA   Deguchi T., Kusuhara H., Takadate A., Endou H., Otagiri M., Sugiyama Y.;
RT   "Characterization of uremic toxin transport by organic anion transporters
RT   in the kidney.";
RL   Kidney Int. 65:162-174(2004).
RN   [6]
RP   INDUCTION BY PGE2.
RX   PubMed=16338963; DOI=10.1681/asn.2005070727;
RA   Sauvant C., Holzinger H., Gekle M.;
RT   "Prostaglandin E2 inhibits its own renal transport by downregulation of
RT   organic anion transporters rOAT1 and rOAT3.";
RL   J. Am. Soc. Nephrol. 17:46-53(2006).
RN   [7]
RP   INDUCTION.
RX   PubMed=17245393; DOI=10.1038/sj.ki.5002104;
RA   Matsuzaki T., Watanabe H., Yoshitome K., Morisaki T., Hamada A.,
RA   Nonoguchi H., Kohda Y., Tomita K., Inui K., Saito H.;
RT   "Downregulation of organic anion transporters in rat kidney under
RT   ischemia/reperfusion-induced acute renal failure.";
RL   Kidney Int. 71:539-547(2007).
RN   [8]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND MISCELLANEOUS.
RX   PubMed=23832370; DOI=10.1271/bbb.130178;
RA   Uwai Y., Honjo E.;
RT   "Transport of xanthurenic acid by rat/human organic anion transporters OAT1
RT   and OAT3.";
RL   Biosci. Biotechnol. Biochem. 77:1517-1521(2013).
CC   -!- FUNCTION: Secondary active transporter that functions as a Na(+)-
CC       independent organic anion (OA)/dicarboxylate antiporter where the
CC       uptake of one molecule of OA into the cell is coupled with an efflux of
CC       one molecule of intracellular dicarboxylate such as alpha-ketoglutarate
CC       or glutarate (PubMed:9374486, PubMed:9228014, PubMed:14675047,
CC       PubMed:23832370). Mediates the uptake of OA across the basolateral side
CC       of proximal tubule epithelial cells, thereby contributing to the renal
CC       elimination of endogenous OA from the systemic circulation into the
CC       urine (By similarity). Function as a biopterin transporters involved in
CC       the uptake and the secretion of coenzymes tetrahydrobiopterin (BH4)
CC       dihydrobiopterin (BH2) and sepiapterin to urine, thereby determining
CC       baseline levels of blood biopterins (By similarity). Transports
CC       prostaglandin E2 (PGE2) and prostaglandin F2-alpha (PGF2-alpha) and may
CC       contribute to their renal excretion (PubMed:9228014). Also mediates the
CC       uptake of cyclic nucleotides such as cAMP and cGMP (PubMed:9228014).
CC       Involved in the transport of neuroactive tryptophan metabolites
CC       kynurenate (KYNA) and xanthurenate (XA) and may contribute to their
CC       secretion from the brain (PubMed:23832370). May transport glutamate (By
CC       similarity). Also involved in the disposition of uremic toxins and
CC       potentially toxic xenobiotics by the renal organic anion secretory
CC       pathway, helping reduce their undesired toxicological effects on the
CC       body (PubMed:9228014, PubMed:14675047). Uremic toxins include the
CC       indoxyl sulfate (IS), hippurate, indole acetate (IA), 3-carboxy-
CC       4- methyl-5-propyl-2-furanpropionate(CMPF) and urate (PubMed:9228014,
CC       PubMed:14675047). Xenobiotics include the mycotoxin ochratoxin (OTA)
CC       (By similarity). May also contribute to the transport of organic
CC       compounds in testes across the blood-testis-barrier (By similarity).
CC       May also work as a bidirectional OA/dicarboxylate exchanger
CC       (PubMed:9228014). {ECO:0000250|UniProtKB:Q4U2R8,
CC       ECO:0000269|PubMed:14675047, ECO:0000269|PubMed:23832370,
CC       ECO:0000269|PubMed:9228014, ECO:0000269|PubMed:9374486}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(out) + a
CC         dicarboxylate(in) = (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin(in) +
CC         a dicarboxylate(out); Xref=Rhea:RHEA:76071, ChEBI:CHEBI:28965,
CC         ChEBI:CHEBI:59560; Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + L-erythro-7,8-dihydrobiopterin(out) = a
CC         dicarboxylate(out) + L-erythro-7,8-dihydrobiopterin(in);
CC         Xref=Rhea:RHEA:76075, ChEBI:CHEBI:28965, ChEBI:CHEBI:43029;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + L-sepiapterin(out) = a
CC         dicarboxylate(out) + L-sepiapterin(in); Xref=Rhea:RHEA:76079,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:194527;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + prostaglandin F2alpha(out) = a
CC         dicarboxylate(out) + prostaglandin F2alpha(in); Xref=Rhea:RHEA:76119,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:57404;
CC         Evidence={ECO:0000250|UniProtKB:Q4U2R8};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + prostaglandin E2(out) = a
CC         dicarboxylate(out) + prostaglandin E2(in); Xref=Rhea:RHEA:76123,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:606564;
CC         Evidence={ECO:0000269|PubMed:9228014};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP(out) + a dicarboxylate(in) = 3',5'-cyclic
CC         AMP(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76127,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:58165;
CC         Evidence={ECO:0000269|PubMed:9228014};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic GMP(out) + a dicarboxylate(in) = 3',5'-cyclic
CC         GMP(in) + a dicarboxylate(out); Xref=Rhea:RHEA:76131,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:57746;
CC         Evidence={ECO:0000269|PubMed:9228014};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + urate(out) = a dicarboxylate(out) +
CC         urate(in); Xref=Rhea:RHEA:76135, ChEBI:CHEBI:17775,
CC         ChEBI:CHEBI:28965; Evidence={ECO:0000269|PubMed:9228014};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutarate(in) + kynurenate(out) = glutarate(out) +
CC         kynurenate(in); Xref=Rhea:RHEA:75999, ChEBI:CHEBI:30921,
CC         ChEBI:CHEBI:58454; Evidence={ECO:0000269|PubMed:23832370};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(indol-3-yl)acetate(out) + a dicarboxylate(in) = (indol-3-
CC         yl)acetate(in) + a dicarboxylate(out); Xref=Rhea:RHEA:75983,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:30854;
CC         Evidence={ECO:0000269|PubMed:14675047};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + indoxyl sulfate(out) = a
CC         dicarboxylate(out) + indoxyl sulfate(in); Xref=Rhea:RHEA:75987,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:144643;
CC         Evidence={ECO:0000269|PubMed:14675047};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a dicarboxylate(in) + N-benzoylglycine(out) = a
CC         dicarboxylate(out) + N-benzoylglycine(in); Xref=Rhea:RHEA:75991,
CC         ChEBI:CHEBI:28965, ChEBI:CHEBI:606565;
CC         Evidence={ECO:0000269|PubMed:14675047};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-carboxy-4-methyl-5-propyl-2-furanpropanoate(out) + a
CC         dicarboxylate(in) = 3-carboxy-4-methyl-5-propyl-2-furanpropanoate(in)
CC         + a dicarboxylate(out); Xref=Rhea:RHEA:75995, ChEBI:CHEBI:28965,
CC         ChEBI:CHEBI:194524; Evidence={ECO:0000269|PubMed:14675047};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=27.5 uM for hippurate/N-benzoylglycine
CC         {ECO:0000269|PubMed:14675047};
CC         KM=47.1 uM for indole acetate {ECO:0000269|PubMed:14675047};
CC         KM=17.7 uM for indoxyl sulfate {ECO:0000269|PubMed:14675047};
CC         KM=154 uM for 3-carboxy-4- methyl-5-propyl-2-furanpropionate
CC         {ECO:0000269|PubMed:14675047};
CC         Vmax=519 pmol/min/mg enzyme for hippurate/N-benzoylglycine uptake
CC         {ECO:0000269|PubMed:14675047};
CC         Vmax=387 pmol/min/mg enzyme for indole acetate uptake
CC         {ECO:0000269|PubMed:14675047};
CC         Vmax=350 pmol/min/mg enzyme for indoxyl sulfate uptake
CC         {ECO:0000269|PubMed:14675047};
CC         Vmax=1669 pmol/min/mg enzyme for
CC         3-carboxy-4- methyl-5-propyl-2-furanpropionate uptake
CC         {ECO:0000269|PubMed:14675047};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VC69};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8VC69}. Basolateral
CC       cell membrane {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane
CC       protein {ECO:0000305}. Basal cell membrane
CC       {ECO:0000250|UniProtKB:Q4U2R8}; Multi-pass membrane protein
CC       {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney; in the particular
CC       segment of the proximal tubule (PubMed:9374486, PubMed:9228014). In
CC       kidney, found preferentially in the cortex and outer medulla and weakly
CC       in the inner medulla (PubMed:9228014). Expressed to a lower extent in
CC       brain (PubMed:9228014). {ECO:0000269|PubMed:9228014,
CC       ECO:0000269|PubMed:9374486}.
CC   -!- INDUCTION: Down-regulated by PGE2 and in ischemic kidney.
CC       {ECO:0000269|PubMed:16338963, ECO:0000269|PubMed:17245393}.
CC   -!- DOMAIN: Multiple cysteine residues are necessary for proper targeting
CC       to the plasma membrane. {ECO:0000250|UniProtKB:Q8VC69}.
CC   -!- PTM: Glycosylated. Glycosylation is necessary for proper targeting of
CC       the transporter to the plasma membrane. {ECO:0000250|UniProtKB:Q4U2R8}.
CC   -!- MISCELLANEOUS: Involved in the renal transport of a variety of drugs
CC       with well-known nephrotoxic potential, therefore may play a role in the
CC       etiology of the drug-associated nephrotoxicity (PubMed:10462545).
CC       Uptakes the diagnostic agent PAH/para-aminohippurate and clinically
CC       used drugs (PubMed:9374486, PubMed:9228014, PubMed:10462545,
CC       PubMed:23832370). Mediates the bidirectional transport of PAH/para-
CC       aminohippurate (By similarity). {ECO:0000250|UniProtKB:Q4U2R8,
CC       ECO:0000269|PubMed:10462545, ECO:0000269|PubMed:23832370,
CC       ECO:0000269|PubMed:9228014, ECO:0000269|PubMed:9374486}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
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DR   EMBL; AF008221; AAC18772.1; -; mRNA.
DR   EMBL; AB004559; BAA22086.1; -; mRNA.
DR   EMBL; BC104692; AAI04693.1; -; mRNA.
DR   RefSeq; NP_058920.1; NM_017224.2.
DR   PDB; 8BVR; EM; 3.52 A; A=1-542.
DR   PDB; 8BVS; EM; 3.61 A; A=1-542.
DR   PDB; 8BVT; EM; 3.94 A; A=1-541.
DR   PDB; 8BW7; EM; 3.53 A; A=1-542.
DR   PDB; 8OMU; EM; 3.43 A; A=1-541.
DR   PDB; 8SDU; EM; 2.05 A; A=1-551.
DR   PDB; 8SDY; EM; 2.79 A; A=1-551.
DR   PDB; 8SDZ; EM; 2.86 A; A=1-551.
DR   PDBsum; 8BVR; -.
DR   PDBsum; 8BVS; -.
DR   PDBsum; 8BVT; -.
DR   PDBsum; 8BW7; -.
DR   PDBsum; 8OMU; -.
DR   PDBsum; 8SDU; -.
DR   PDBsum; 8SDY; -.
DR   PDBsum; 8SDZ; -.
DR   AlphaFoldDB; O35956; -.
DR   EMDB; EMD-16269; -.
DR   EMDB; EMD-16270; -.
DR   EMDB; EMD-16271; -.
DR   EMDB; EMD-16280; -.
DR   EMDB; EMD-16977; -.
DR   EMDB; EMD-40352; -.
DR   EMDB; EMD-40354; -.
DR   EMDB; EMD-40355; -.
DR   SMR; O35956; -.
DR   BioGRID; 248147; 1.
DR   IntAct; O35956; 1.
DR   STRING; 10116.ENSRNOP00000024756; -.
DR   BindingDB; O35956; -.
DR   ChEMBL; CHEMBL1777665; -.
DR   DrugCentral; O35956; -.
DR   TCDB; 2.A.1.19.4; the major facilitator superfamily (mfs).
DR   GlyCosmos; O35956; 4 sites, No reported glycans.
DR   GlyGen; O35956; 4 sites.
DR   PhosphoSitePlus; O35956; -.
DR   PaxDb; 10116-ENSRNOP00000024756; -.
DR   Ensembl; ENSRNOT00000024757.5; ENSRNOP00000024756.2; ENSRNOG00000018215.7.
DR   Ensembl; ENSRNOT00055040476; ENSRNOP00055032879; ENSRNOG00055023538.
DR   Ensembl; ENSRNOT00060057288; ENSRNOP00060047364; ENSRNOG00060033018.
DR   Ensembl; ENSRNOT00065056349; ENSRNOP00065046382; ENSRNOG00065032764.
DR   GeneID; 29509; -.
DR   KEGG; rno:29509; -.
DR   UCSC; RGD:69338; rat.
DR   AGR; RGD:69338; -.
DR   CTD; 9356; -.
DR   RGD; 69338; Slc22a6.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000157004; -.
DR   HOGENOM; CLU_001265_33_3_1; -.
DR   InParanoid; O35956; -.
DR   OMA; MEAYMGA; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; O35956; -.
DR   TreeFam; TF315847; -.
DR   Reactome; R-RNO-561048; Organic anion transport.
DR   SABIO-RK; O35956; -.
DR   PRO; PR:O35956; -.
DR   Proteomes; UP000002494; Chromosome 1.
DR   Bgee; ENSRNOG00000018215; Expressed in adult mammalian kidney and 12 other cell types or tissues.
DR   GO; GO:0009925; C:basal plasma membrane; ISS:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005901; C:caveola; IDA:RGD.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR   GO; GO:0015139; F:alpha-ketoglutarate transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015297; F:antiporter activity; IDA:UniProtKB.
DR   GO; GO:0031404; F:chloride ion binding; IDA:RGD.
DR   GO; GO:0042802; F:identical protein binding; IPI:RGD.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015132; F:prostaglandin transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IDA:RGD.
DR   GO; GO:0005452; F:solute:inorganic anion antiporter activity; ISS:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; ISO:RGD.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0015742; P:alpha-ketoglutarate transport; ISS:UniProtKB.
DR   GO; GO:0072237; P:metanephric proximal tubule development; IEP:RGD.
DR   GO; GO:0006820; P:monoatomic anion transport; ISO:RGD.
DR   GO; GO:0015711; P:organic anion transport; IDA:MGI.
DR   GO; GO:0015732; P:prostaglandin transport; IDA:UniProtKB.
DR   GO; GO:0097254; P:renal tubular secretion; ISS:UniProtKB.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IDA:RGD.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR005828; MFS_sugar_transport-like.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004749; Orgcat_transp/SVOP.
DR   NCBIfam; TIGR00898; 2A0119; 1.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   PANTHER; PTHR24064:SF294; SOLUTE CARRIER FAMILY 22 MEMBER 6; 1.
DR   Pfam; PF00083; Sugar_tr; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; O35956; RN.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..551
FT                   /note="Solute carrier family 22 member 6"
FT                   /id="PRO_0000324171"
FT   TOPO_DOM        1..9
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        31..135
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        136..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        157..164
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        165..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..195
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        196..216
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        217..224
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        225..245
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        246..248
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        270..337
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        359..368
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        369..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        390..395
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        396..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        417..425
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        426..446
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        447..484
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        485..505
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        506..551
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   REGION          514..551
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        39
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        92
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        113
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   HELIX           3..10
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          12..14
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           15..23
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           28..36
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           38..41
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          47..49
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           57..60
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          109..111
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           120..123
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           133..159
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           163..180
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           185..213
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   TURN            217..220
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           221..243
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           247..264
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           265..267
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           272..277
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           282..295
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           298..302
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           306..312
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           326..331
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           333..357
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           367..391
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           395..414
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           421..446
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   TURN            451..453
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           454..476
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           477..480
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           485..500
FT                   /evidence="ECO:0007829|PDB:8OMU"
FT   HELIX           516..524
FT                   /evidence="ECO:0007829|PDB:8OMU"
SQ   SEQUENCE   551 AA;  60766 MW;  8BA47BE628324BF2 CRC64;
     MAFNDLLKQV GGVGRFQLIQ VTMVVAPLLL MASHNTLQNF TAAIPPHHCR PPANANLSKD
     GGLEAWLPLD KQGQPESCLR FTSPQWGPPF YNGTEANGTR VTEPCIDGWV YDNSTFPSTI
     VTEWNLVCSH RAFRQLAQSL YMVGVLLGAM VFGYLADRLG RRKVLILNYL QTAVSGTCAA
     YAPNYTVYCV FRLLSGMSLA SIAINCMTLN VEWMPIHTRA YVGTLIGYVY SLGQFLLAGI
     AYAVPHWRHL QLVVSVPFFI AFIYSWFFIE SARWYSSSGR LDLTLRALQR VARINGKQEE
     GAKLSIEVLR TSLQKELTLS KGQASAMELL RCPTLRHLFL CLSMLWFATS FAYYGLVMDL
     QGFGVSMYLI QVIFGAVDLP AKFVCFLVIN SMGRRPAQMA SLLLAGICIL VNGIIPKSHT
     IIRTSLAVLG KGCLASSFNC IFLYTGELYP TVIRQTGLGM GSTMARVGSI VSPLVSMTAE
     FYPSMPLFIF GAVPVVASAV TALLPETLGQ PLPDTVQDLK SRSRGKQNQQ QQEQQKQMMP
     LQASTQEKNG L
//