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S22A7_HUMAN
ID   S22A7_HUMAN             Reviewed;         548 AA.
AC   Q9Y694; B2CZX6; Q5T046; Q5T048; Q5T050; Q9H2W5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 176.
DE   RecName: Full=Solute carrier family 22 member 7;
DE   AltName: Full=Novel liver transporter;
DE   AltName: Full=Organic anion transporter 2;
DE            Short=hOAT2;
GN   Name=SLC22A7; Synonyms=NLT, OAT2;
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).
RC   TISSUE=Liver;
RA   Kim R.B., Leake B.L., Cvetkovic M.;
RT   "Molecular cloning of a human liver-specific transporter, NLT.";
RL   Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC   TISSUE=Kidney;
RA   Reid G., Bahn A., Ebbinghaus C., Wolff N.A., Burckhardt G.;
RT   "Identification of a human organic anion transporter 2 homolog.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA   Kobayashi Y., Ohshiro N., Sekine T., Endoh H., Yamamoto T.;
RT   "Cloning, characterization and localization of human organic anion
RT   transporter 2.";
RL   Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC   TISSUE=Kidney;
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS LYS-303; TRP-327 AND
RP   VAL-507.
RG   NIEHS SNPs program;
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
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] (ISOFORM 1).
RC   TISSUE=Colon;
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   FUNCTION, 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 SUBCELLULAR LOCATION.
RX   PubMed=12023506; DOI=10.1124/jpet.301.3.797;
RA   Enomoto A., Takeda M., Shimoda M., Narikawa S., Kobayashi Y., Kobayashi Y.,
RA   Yamamoto T., Sekine T., Cha S.H., Niwa T., Endou H.;
RT   "Interaction of human organic anion transporters 2 and 4 with organic anion
RT   transport inhibitors.";
RL   J. Pharmacol. Exp. Ther. 301:797-802(2002).
RN   [11]
RP   FUNCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   SUBCELLULAR LOCATION.
RX   PubMed=11907186; DOI=10.1124/jpet.301.1.293;
RA   Kimura H., Takeda M., Narikawa S., Enomoto A., Ichida K., Endou H.;
RT   "Human organic anion transporters and human organic cation transporters
RT   mediate renal transport of prostaglandins.";
RL   J. Pharmacol. Exp. Ther. 301:293-298(2002).
RN   [12]
RP   FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=11855680; DOI=10.1254/jjp.88.69;
RA   Babu E., Takeda M., Narikawa S., Kobayashi Y., Yamamoto T., Cha S.H.,
RA   Sekine T., Sakthisekaran D., Endou H.;
RT   "Human organic anion transporters mediate the transport of tetracycline.";
RL   Jpn. J. Pharmacol. 88:69-76(2002).
RN   [13]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15901346; DOI=10.1211/0022357055966;
RA   Kobayashi Y., Ohshiro N., Sakai R., Ohbayashi M., Kohyama N., Yamamoto T.;
RT   "Transport mechanism and substrate specificity of human organic anion
RT   transporter 2 (hOat2 [SLC22A7]).";
RL   J. Pharm. Pharmacol. 57:573-578(2005).
RN   [14]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-91.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
CC   -!- FUNCTION: Mediates sodium-independent multispecific organic anion
CC       transport. Transport of prostaglandin E2, prostaglandin F2,
CC       tetracycline, bumetanide, estrone sulfate, glutarate,
CC       dehydroepiandrosterone sulfate, allopurinol, 5-fluorouracil,
CC       paclitaxel, L-ascorbic acid, salicylate, ethotrexate, and alpha-
CC       ketoglutarate. {ECO:0000269|PubMed:11327718,
CC       ECO:0000269|PubMed:11855680, ECO:0000269|PubMed:11907186,
CC       ECO:0000269|PubMed:12023506, ECO:0000269|PubMed:15901346}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=713 nM for prostaglandin E2 {ECO:0000269|PubMed:11855680,
CC         ECO:0000269|PubMed:11907186};
CC         KM=440 uM for tetracycline {ECO:0000269|PubMed:11855680,
CC         ECO:0000269|PubMed:11907186};
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:11907186, ECO:0000269|PubMed:12023506}; Multi-pass
CC       membrane protein {ECO:0000269|PubMed:11907186,
CC       ECO:0000269|PubMed:12023506}. Note=Apical side of the renal tubule.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q9Y694-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y694-2; Sequence=VSP_030992;
CC       Name=3;
CC         IsoId=Q9Y694-3; Sequence=VSP_030992, VSP_030994;
CC       Name=4;
CC         IsoId=Q9Y694-4; Sequence=VSP_030991, VSP_030993;
CC   -!- TISSUE SPECIFICITY: Expressed in liver and kidney.
CC       {ECO:0000269|PubMed:11327718, ECO:0000269|PubMed:11907186,
CC       ECO:0000269|PubMed:15901346}.
CC   -!- SIMILARITY: Belongs to the major facilitator (TC 2.A.1) superfamily.
CC       Organic cation transporter (TC 2.A.1.19) family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/slc22a7/";
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DR   EMBL; AF097518; AAD37091.1; -; mRNA.
DR   EMBL; AF210455; AAG43523.1; -; mRNA.
DR   EMBL; AY050498; AAL12496.1; -; mRNA.
DR   EMBL; AK290796; BAF83485.1; -; mRNA.
DR   EMBL; AK290806; BAF83495.1; -; mRNA.
DR   EMBL; EU562669; ACB21045.1; -; Genomic_DNA.
DR   EMBL; AL583834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04172.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX04175.1; -; Genomic_DNA.
DR   EMBL; BC033805; AAH33805.1; -; mRNA.
DR   CCDS; CCDS4892.1; -. [Q9Y694-2]
DR   CCDS; CCDS4893.2; -. [Q9Y694-1]
DR   RefSeq; NP_006663.2; NM_006672.3. [Q9Y694-2]
DR   RefSeq; NP_696961.2; NM_153320.2. [Q9Y694-1]
DR   AlphaFoldDB; Q9Y694; -.
DR   SMR; Q9Y694; -.
DR   IntAct; Q9Y694; 2.
DR   STRING; 9606.ENSP00000361666; -.
DR   BindingDB; Q9Y694; -.
DR   ChEMBL; CHEMBL1955711; -.
DR   DrugBank; DB00437; Allopurinol.
DR   DrugBank; DB00345; Aminohippuric acid.
DR   DrugBank; DB00887; Bumetanide.
DR   DrugBank; DB00456; Cefalotin.
DR   DrugBank; DB01326; Cefamandole.
DR   DrugBank; DB01329; Cefoperazone.
DR   DrugBank; DB00493; Cefotaxime.
DR   DrugBank; DB02659; Cholic Acid.
DR   DrugBank; DB00501; Cimetidine.
DR   DrugBank; DB01211; Clarithromycin.
DR   DrugBank; DB02527; Cyclic adenosine monophosphate.
DR   DrugBank; DB01160; Dinoprost tromethamine.
DR   DrugBank; DB00917; Dinoprostone.
DR   DrugBank; DB01248; Docetaxel.
DR   DrugBank; DB00584; Enalapril.
DR   DrugBank; DB00544; Fluorouracil.
DR   DrugBank; DB01004; Ganciclovir.
DR   DrugBank; DB03553; Glutaric Acid.
DR   DrugBank; DB01016; Glyburide.
DR   DrugBank; DB00328; Indomethacin.
DR   DrugBank; DB01009; Ketoprofen.
DR   DrugBank; DB00563; Methotrexate.
DR   DrugBank; DB01017; Minocycline.
DR   DrugBank; DB01303; Oxtriphylline.
DR   DrugBank; DB00595; Oxytetracycline.
DR   DrugBank; DB00175; Pravastatin.
DR   DrugBank; DB01032; Probenecid.
DR   DrugBank; DB01045; Rifampicin.
DR   DrugBank; DB00936; Salicylic acid.
DR   DrugBank; DB09327; Tegafur-uracil.
DR   DrugBank; DB00624; Testosterone.
DR   DrugBank; DB13943; Testosterone cypionate.
DR   DrugBank; DB13944; Testosterone enanthate.
DR   DrugBank; DB13946; Testosterone undecanoate.
DR   DrugBank; DB00759; Tetracycline.
DR   DrugBank; DB00277; Theophylline.
DR   DrugBank; DB00313; Valproic acid.
DR   DrugBank; DB00943; Zalcitabine.
DR   DrugBank; DB00495; Zidovudine.
DR   TCDB; 2.A.1.19.25; the major facilitator superfamily (mfs).
DR   GlyGen; Q9Y694; 1 site.
DR   iPTMnet; Q9Y694; -.
DR   PhosphoSitePlus; Q9Y694; -.
DR   BioMuta; SLC22A7; -.
DR   DMDM; 74753520; -.
DR   MassIVE; Q9Y694; -.
DR   PaxDb; Q9Y694; -.
DR   PeptideAtlas; Q9Y694; -.
DR   PRIDE; Q9Y694; -.
DR   ProteomicsDB; 86628; -. [Q9Y694-1]
DR   ProteomicsDB; 86629; -. [Q9Y694-2]
DR   ProteomicsDB; 86630; -. [Q9Y694-3]
DR   ProteomicsDB; 86631; -. [Q9Y694-4]
DR   Antibodypedia; 30365; 111 antibodies from 23 providers.
DR   DNASU; 10864; -.
DR   Ensembl; ENST00000372574.7; ENSP00000361655.3; ENSG00000137204.15. [Q9Y694-3]
DR   Ensembl; ENST00000372585.10; ENSP00000361666.5; ENSG00000137204.15. [Q9Y694-1]
DR   Ensembl; ENST00000372589.7; ENSP00000361670.3; ENSG00000137204.15. [Q9Y694-2]
DR   GeneID; 10864; -.
DR   KEGG; hsa:10864; -.
DR   MANE-Select; ENST00000372585.10; ENSP00000361666.5; NM_153320.2; NP_696961.2.
DR   UCSC; uc003ous.4; human. [Q9Y694-1]
DR   CTD; 10864; -.
DR   DisGeNET; 10864; -.
DR   GeneCards; SLC22A7; -.
DR   HGNC; HGNC:10971; SLC22A7.
DR   HPA; ENSG00000137204; Tissue enriched (liver).
DR   MIM; 604995; gene.
DR   neXtProt; NX_Q9Y694; -.
DR   OpenTargets; ENSG00000137204; -.
DR   PharmGKB; PA35848; -.
DR   VEuPathDB; HostDB:ENSG00000137204; -.
DR   eggNOG; KOG0255; Eukaryota.
DR   GeneTree; ENSGT00940000154922; -.
DR   HOGENOM; CLU_001265_33_3_1; -.
DR   InParanoid; Q9Y694; -.
DR   OMA; FPMETRA; -.
DR   OrthoDB; 435631at2759; -.
DR   PhylomeDB; Q9Y694; -.
DR   TreeFam; TF315847; -.
DR   PathwayCommons; Q9Y694; -.
DR   Reactome; R-HSA-561048; Organic anion transport.
DR   Reactome; R-HSA-9749641; Aspirin ADME.
DR   SignaLink; Q9Y694; -.
DR   BioGRID-ORCS; 10864; 9 hits in 1064 CRISPR screens.
DR   ChiTaRS; SLC22A7; human.
DR   GeneWiki; SLC22A7; -.
DR   GenomeRNAi; 10864; -.
DR   Pharos; Q9Y694; Tbio.
DR   PRO; PR:Q9Y694; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q9Y694; protein.
DR   Bgee; ENSG00000137204; Expressed in right lobe of liver and 138 other tissues.
DR   ExpressionAtlas; Q9Y694; baseline and differential.
DR   Genevisible; Q9Y694; HS.
DR   GO; GO:0016323; C:basolateral plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; IDA:ARUK-UCL.
DR   GO; GO:0015301; F:anion:anion antiporter activity; TAS:Reactome.
DR   GO; GO:0015347; F:sodium-independent organic anion transmembrane transporter activity; TAS:Reactome.
DR   GO; GO:0015711; P:organic anion transport; TAS:ProtInc.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   InterPro; IPR011701; MFS.
DR   InterPro; IPR020846; MFS_dom.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR004749; Orgcat_transp/SVOP.
DR   Pfam; PF07690; MFS_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   TIGRFAMs; TIGR00898; 2A0119; 1.
DR   PROSITE; PS50850; MFS; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..548
FT                   /note="Solute carrier family 22 member 7"
FT                   /id="PRO_0000317481"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        346..366
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        376..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        404..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        432..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        466..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        493..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          522..548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        91
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         1..307
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030991"
FT   VAR_SEQ         132..133
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT                   /id="VSP_030992"
FT   VAR_SEQ         308..317
FT                   /note="PVCEDSFSQE -> MLQPHLLPYQ (in isoform 4)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_030993"
FT   VAR_SEQ         531..548
FT                   /note="SAPTSLQEEEMPMKQVQN -> RCVHRTVSVYV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT                   /id="VSP_030994"
FT   VARIANT         303
FT                   /note="R -> K (in dbSNP:rs70953684)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_047875"
FT   VARIANT         327
FT                   /note="R -> W (in dbSNP:rs36040909)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_047876"
FT   VARIANT         507
FT                   /note="G -> V (in dbSNP:rs70953693)"
FT                   /evidence="ECO:0000269|Ref.5"
FT                   /id="VAR_047877"
FT   CONFLICT        304
FT                   /note="L -> P (in Ref. 2; AAG43523)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413
FT                   /note="T -> A (in Ref. 2; AAG43523)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   548 AA;  60026 MW;  5BA4C3FCC3C57533 CRC64;
     MGFEELLEQV GGFGPFQLRN VALLALPRVL LPLHFLLPIF LAAVPAHRCA LPGAPANFSH
     QDVWLEAHLP REPDGTLSSC LRFAYPQALP NTTLGEERQS RGELEDEPAT VPCSQGWEYD
     HSEFSSTIAT ESQWDLVCEQ KGLNRAASTF FFAGVLVGAV AFGYLSDRFG RRRLLLVAYV
     STLVLGLASA ASVSYVMFAI TRTLTGSALA GFTIIVMPLE LEWLDVEHRT VAGVLSSTFW
     TGGVMLLALV GYLIRDWRWL LLAVTLPCAP GILSLWWVPE SARWLLTQGH VKEAHRYLLH
     CARLNGRPVC EDSFSQEAVS KVAAGERVVR RPSYLDLFRT PRLRHISLCC VVVWFGVNFS
     YYGLSLDVSG LGLNVYQTQL LFGAVELPSK LLVYLSVRYA GRRLTQAGTL LGTALAFGTR
     LLVSSDMKSW STVLAVMGKA FSEAAFTTAY LFTSELYPTV LRQTGMGLTA LVGRLGGSLA
     PLAALLDGVW LSLPKLTYGG IALLAAGTAL LLPETRQAQL PETIQDVERK SAPTSLQEEE
     MPMKQVQN
 
 
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