ID   S22A9_HUMAN             Reviewed;         553 AA.
AC   Q8IVM8; A0AVB7; A4PB24; Q8TCC8; Q8TEC0; Q8WYN7;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=Organic anion transporter 7 {ECO:0000303|PubMed:17393504};
DE            Short=OAT7 {ECO:0000303|PubMed:17393504};
DE   AltName: Full=Organic anion/short-chain fatty acid exchanger;
DE   AltName: Full=Solute carrier family 22 member 9;
GN   Name=SLC22A9; Synonyms=hOAT4, OAT7, UST3;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP   AND DEVELOPMENTAL STAGE.
RC   TISSUE=Liver;
RX   PubMed=17393504; DOI=10.1002/hep.21596;
RA   Shin H.J., Anzai N., Enomoto A., He X., Kim do K., Endou H., Kanai Y.;
RT   "Novel liver-specific organic anion transporter OAT7 that operates the
RT   exchange of sulfate conjugates for short chain fatty acid butyrate.";
RL   Hepatology 45:1046-1055(2007).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Engel K., Gruendemann D., Schoemig E.;
RT   "Putative integral membrane transport protein UST3H.";
RL   Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Fetal liver;
RA   Takanaga H., Ohtsuki S., Hosoya K., Terasaki T.;
RT   "Isolation of novel clone of amphiphilic solute facilitator family from
RT   human fetal liver.";
RL   Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA   Guo J.H., Yu L.;
RL   Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hepatoma;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16554811; DOI=10.1038/nature04632;
RA   Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA   Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA   Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA   Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA   Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA   Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT   "Human chromosome 11 DNA sequence and analysis including novel gene
RT   identification.";
RL   Nature 440:497-500(2006).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain, and Liver;
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   [9]
RP   IDENTIFICATION, AND TISSUE SPECIFICITY.
RX   PubMed=11327718; DOI=10.1006/bbrc.2001.4774;
RA   Sun W., Wu R.R., van Poelje P.D., Erion M.D.;
RT   "Isolation of a family of organic anion transporters from human liver and
RT   kidney.";
RL   Biochem. Biophys. Res. Commun. 283:417-422(2001).
RN   [10]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=26239079; DOI=10.1038/tpj.2015.55;
RA   Emami Riedmaier A., Burk O., van Eijck B.A., Schaeffeler E., Klein K.,
RA   Fehr S., Biskup S., Mueller S., Winter S., Zanger U.M., Schwab M.,
RA   Nies A.T.;
RT   "Variability in hepatic expression of organic anion transporter 7/SLC22A9,
RT   a novel pravastatin uptake transporter: impact of genetic and regulatory
RT   factors.";
RL   Pharmacogenomics J. 16:341-351(2016).
RN   [11]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=28945155; DOI=10.1080/00498254.2017.1384595;
RA   Mathialagan S., Costales C., Tylaska L., Kimoto E., Vildhede A.,
RA   Johnson J., Johnson N., Sarashina T., Hashizume K., Isringhausen C.D.,
RA   Vermeer L.M.M., Wolff A.R., Rodrigues A.D.;
RT   "In vitro studies with two human organic anion transporters: OAT2 and
RT   OAT7.";
RL   Xenobiotica 48:1037-1049(2018).
RN   [12]
RP   VARIANTS [LARGE SCALE ANALYSIS] VAL-393; VAL-487 AND LYS-521.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Sodium-independent organic anion transporter, exhibits high
CC       specificity for sulfated conjugates of xenobiotics and steroid hormones
CC       such as estrone 3-sulfate (E1S) and dehydroepiandrosterone sulfate
CC       (DHEAS) (PubMed:17393504, PubMed:26239079, PubMed:28945155). Can
CC       transport the statin pravastatin and may contribute to its disposition
CC       into the hepatocytes when the function of OATPs is compromised
CC       (PubMed:26239079). It is specifically activated by 3 to 5 carbons-
CC       containing short-chain fatty acids/SCFAs, including propionate
CC       (propanoate), butyrate (butanoate) and valerate (pentanoate)
CC       (PubMed:17393504). May operate the exchange of sulfated organic
CC       components against short-chain fatty acids/SCFAs, in particular
CC       butanoate, at the sinusoidal membrane of hepatocytes (PubMed:17393504).
CC       {ECO:0000269|PubMed:17393504, ECO:0000269|PubMed:26239079,
CC       ECO:0000269|PubMed:28945155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoate(out) + estrone 3-sulfate(in) = butanoate(in) +
CC         estrone 3-sulfate(out); Xref=Rhea:RHEA:72051, ChEBI:CHEBI:17968,
CC         ChEBI:CHEBI:60050; Evidence={ECO:0000269|PubMed:17393504,
CC         ECO:0000305|PubMed:28945155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) + propanoate(in) = estrone 3-
CC         sulfate(in) + propanoate(out); Xref=Rhea:RHEA:72555,
CC         ChEBI:CHEBI:17272, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:17393504, ECO:0000305|PubMed:28945155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=estrone 3-sulfate(out) + pentanoate(in) = estrone 3-
CC         sulfate(in) + pentanoate(out); Xref=Rhea:RHEA:72559,
CC         ChEBI:CHEBI:31011, ChEBI:CHEBI:60050;
CC         Evidence={ECO:0000269|PubMed:17393504, ECO:0000305|PubMed:28945155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=butanoate(out) + dehydroepiandrosterone 3-sulfate(in) =
CC         butanoate(in) + dehydroepiandrosterone 3-sulfate(out);
CC         Xref=Rhea:RHEA:72563, ChEBI:CHEBI:17968, ChEBI:CHEBI:57905;
CC         Evidence={ECO:0000305|PubMed:17393504, ECO:0000305|PubMed:28945155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dehydroepiandrosterone 3-sulfate(in) + propanoate(out) =
CC         dehydroepiandrosterone 3-sulfate(out) + propanoate(in);
CC         Xref=Rhea:RHEA:72567, ChEBI:CHEBI:17272, ChEBI:CHEBI:57905;
CC         Evidence={ECO:0000305|PubMed:17393504, ECO:0000305|PubMed:28945155};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dehydroepiandrosterone 3-sulfate(in) + pentanoate(out) =
CC         dehydroepiandrosterone 3-sulfate(out) + pentanoate(in);
CC         Xref=Rhea:RHEA:72571, ChEBI:CHEBI:31011, ChEBI:CHEBI:57905;
CC         Evidence={ECO:0000305|PubMed:17393504, ECO:0000305|PubMed:28945155};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=8.7 uM for estrone 3-sulfate {ECO:0000269|PubMed:17393504};
CC         KM=2.2 uM for dehydroepiandrosterone sulfate
CC         {ECO:0000269|PubMed:17393504};
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:17393504}; Multi-pass membrane protein
CC       {ECO:0000269|PubMed:17393504}. Note=Enriched at the sinusoidal part of
CC       the plasma membrane.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8IVM8-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8IVM8-2; Sequence=VSP_036710, VSP_036711;
CC   -!- TISSUE SPECIFICITY: Specifically expressed in liver (also at protein
CC       level). {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:17393504,
CC       ECO:0000269|PubMed:26239079}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in fetal liver.
CC       {ECO:0000269|PubMed:17393504}.
CC   -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC       premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC       decay. {ECO:0000305}.
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; AB074812; BAF51552.1; -; mRNA.
DR   EMBL; AJ295270; CAC82910.1; -; mRNA.
DR   EMBL; AB062418; BAB83517.1; -; mRNA.
DR   EMBL; AF440402; AAP97316.1; -; mRNA.
DR   EMBL; AK074246; BAB85030.1; -; mRNA.
DR   EMBL; AP001880; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471076; EAW74146.1; -; Genomic_DNA.
DR   EMBL; CH471076; EAW74148.1; -; Genomic_DNA.
DR   EMBL; BC022379; AAH22379.1; -; mRNA.
DR   EMBL; BC126288; AAI26289.1; -; mRNA.
DR   CCDS; CCDS8043.1; -. [Q8IVM8-1]
DR   RefSeq; NP_543142.2; NM_080866.2. [Q8IVM8-1]
DR   AlphaFoldDB; Q8IVM8; -.
DR   SMR; Q8IVM8; -.
DR   BioGRID; 125322; 148.
DR   IntAct; Q8IVM8; 66.
DR   MINT; Q8IVM8; -.
DR   STRING; 9606.ENSP00000279178; -.
DR   ChEMBL; CHEMBL2073721; -.
DR   TCDB; 2.A.1.19.18; the major facilitator superfamily (mfs).
DR   GlyCosmos; Q8IVM8; 3 sites, No reported glycans.
DR   GlyGen; Q8IVM8; 3 sites.
DR   iPTMnet; Q8IVM8; -.
DR   PhosphoSitePlus; Q8IVM8; -.
DR   BioMuta; SLC22A9; -.
DR   DMDM; 74723638; -.
DR   MassIVE; Q8IVM8; -.
DR   PaxDb; 9606-ENSP00000279178; -.
DR   PeptideAtlas; Q8IVM8; -.
DR   ProteomicsDB; 70744; -. [Q8IVM8-1]
DR   ProteomicsDB; 70745; -. [Q8IVM8-2]
DR   Antibodypedia; 2750; 65 antibodies from 15 providers.
DR   DNASU; 114571; -.
DR   Ensembl; ENST00000279178.4; ENSP00000279178.3; ENSG00000149742.10. [Q8IVM8-1]
DR   Ensembl; ENST00000536333.5; ENSP00000440206.1; ENSG00000149742.10. [Q8IVM8-2]
DR   GeneID; 114571; -.
DR   KEGG; hsa:114571; -.
DR   MANE-Select; ENST00000279178.4; ENSP00000279178.3; NM_080866.3; NP_543142.2.
DR   UCSC; uc001nww.4; human. [Q8IVM8-1]
DR   AGR; HGNC:16261; -.
DR   CTD; 114571; -.
DR   DisGeNET; 114571; -.
DR   GeneCards; SLC22A9; -.
DR   HGNC; HGNC:16261; SLC22A9.
DR   HPA; ENSG00000149742; Tissue enriched (liver).
DR   MIM; 607579; gene.
DR   neXtProt; NX_Q8IVM8; -.
DR   OpenTargets; ENSG00000149742; -.
DR   PharmGKB; PA38102; -.
DR   VEuPathDB; HostDB:ENSG00000149742; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000161239; -.
DR   HOGENOM; CLU_001265_33_0_1; -.
DR   InParanoid; Q8IVM8; -.
DR   OMA; FLGHASW; -.
DR   OrthoDB; 2088942at2759; -.
DR   PhylomeDB; Q8IVM8; -.
DR   TreeFam; TF315847; -.
DR   PathwayCommons; Q8IVM8; -.
DR   SignaLink; Q8IVM8; -.
DR   SIGNOR; Q8IVM8; -.
DR   BioGRID-ORCS; 114571; 13 hits in 1136 CRISPR screens.
DR   GeneWiki; SLC22A9; -.
DR   GenomeRNAi; 114571; -.
DR   Pharos; Q8IVM8; Tbio.
DR   PRO; PR:Q8IVM8; -.
DR   Proteomes; UP000005640; Chromosome 11.
DR   RNAct; Q8IVM8; Protein.
DR   Bgee; ENSG00000149742; Expressed in right lobe of liver and 31 other cell types or tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015636; F:short-chain fatty acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0009914; P:hormone transport; IDA:UniProtKB.
DR   GO; GO:0015711; P:organic anion transport; IBA:GO_Central.
DR   GO; GO:0015913; P:short-chain fatty acid transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0043252; P:sodium-independent organic anion transport; IDA:UniProtKB.
DR   CDD; cd17374; MFS_OAT; 1.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   PANTHER; PTHR24064; SOLUTE CARRIER FAMILY 22 MEMBER; 1.
DR   PANTHER; PTHR24064:SF592; SOLUTE CARRIER FAMILY 22 MEMBER 9; 1.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   PROSITE; PS50850; MFS; 1.
DR   Genevisible; Q8IVM8; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Lipid transport;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..553
FT                   /note="Organic anion transporter 7"
FT                   /id="PRO_0000233715"
FT   TOPO_DOM        1..15
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        37..143
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        144..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        165..177
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        178..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        199..203
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        225..233
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..259
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..350
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        351..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        370..378
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        400..407
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        429..436
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        437..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        458..469
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        470..490
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        491..495
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        496..516
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        517..553
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          528..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..547
FT                   /note="Basic and acidic residues"
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        102
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         169..346
FT                   /note="RFGRRFVLRWCYLQVAIVGTCAALAPTFLIYCSLRFLSGIAAMSLITNTIML
FT                   IAEWATHRFQAMGITLGMCPSGIAFMTLAGLAFAIRDWHILQLVVSVPYFVIFLTSSWL
FT                   LESARWLIINNKPEEGLKELRKAAHRSGMKNARDTLTLEILKSTMKKELEAAQKKKPSL
FT                   CEMLHMPN -> SSRVGNTQIPGHGNYIGNVPFWYCIYDPGRPGFCHSRLAYPPAGGVC
FT                   TILCDLSDLKLAARVCSVAHYQQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036710"
FT   VAR_SEQ         347..553
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_036711"
FT   VARIANT         393
FT                   /note="A -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036403"
FT   VARIANT         487
FT                   /note="M -> V (in a breast cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036404"
FT   VARIANT         521
FT                   /note="N -> K (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs770073076)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036405"
FT   CONFLICT        518
FT                   /note="E -> G (in Ref. 3; BAB83517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        535
FT                   /note="Missing (in Ref. 5; BAB85030)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   553 AA;  62169 MW;  FE0A1B725FCB7617 CRC64;
     MAFQDLLGHA GDLWRFQILQ TVFLSIFAVA TYLHFMLENF TAFIPGHRCW VHILDNDTVS
     DNDTGALSQD ALLRISIPLD SNMRPEKCRR FVHPQWQLLH LNGTFPNTSD ADMEPCVDGW
     VYDRISFSST IVTEWDLVCD SQSLTSVAKF VFMAGMMVGG ILGGHLSDRF GRRFVLRWCY
     LQVAIVGTCA ALAPTFLIYC SLRFLSGIAA MSLITNTIML IAEWATHRFQ AMGITLGMCP
     SGIAFMTLAG LAFAIRDWHI LQLVVSVPYF VIFLTSSWLL ESARWLIINN KPEEGLKELR
     KAAHRSGMKN ARDTLTLEIL KSTMKKELEA AQKKKPSLCE MLHMPNICKR ISLLSFTRFA
     NFMAYFGLNL HVQHLGNNVF LLQTLFGAVI LLANCVAPWA LKYMNRRASQ MLLMFLLAIC
     LLAIIFVPQE MQTLREVLAT LGLGASALAN TLAFAHGNEV IPTIIRARAM GINATFANIA
     GALAPLMMIL SVYSPPLPWI IYGVFPFISG FAFLLLPETR NKPLFDTIQD EKNERKDPRE
     PKQEDPRVEV TQF
//