S43A3_HUMAN
ID S43A3_HUMAN Reviewed; 491 AA.
AC Q8NBI5; B4DNR8; E7EQD2; Q9NSS4;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Equilibrative nucleobase transporter 1 {ECO:0000303|PubMed:26455426, ECO:0000303|PubMed:32339528};
DE AltName: Full=Protein FOAP-13;
DE AltName: Full=Solute carrier family 43 member 3;
GN Name=SLC43A3;
GN Synonyms=ENBT1 {ECO:0000303|PubMed:26455426, ECO:0000303|PubMed:32339528};
GN ORFNames=PSEC0252;
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), AND TISSUE SPECIFICITY.
RA Fujii Y., Tsuritani K., Yajima Y., Amemiya T., Ukai Y., Naito K.,
RA Kawaguchi A., Takayama K.;
RT "Molecular cloning of a human novel gene, FOAP-13, which are highly
RT expressed in macrophages.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Melanoma;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
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] (ISOFORM 1).
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-258, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-253 AND THR-258, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=26455426; DOI=10.1038/srep15057;
RA Furukawa J., Inoue K., Maeda J., Yasujima T., Ohta K., Kanai Y., Takada T.,
RA Matsuo H., Yuasa H.;
RT "Functional identification of SLC43A3 as an equilibrative nucleobase
RT transporter involved in purine salvage in mammals.";
RL Sci. Rep. 5:15057-15057(2015).
RN [13]
RP FUNCTION (ISOFORMS 1 AND 2), BIOPHYSICOCHEMICAL PROPERTIES (ISOFORMS 1 AND
RP 2), AND ACTIVITY REGULATION (ISOFORM 1 AND 2).
RX PubMed=30910793; DOI=10.1124/mol.118.114389;
RA Ruel N.M., Nguyen K.H., Vilas G., Hammond J.R.;
RT "Characterization of 6-Mercaptopurine Transport by the SLC43A3-Encoded
RT Nucleobase Transporter.";
RL Mol. Pharmacol. 95:584-596(2019).
RN [14]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=32339528; DOI=10.1016/j.xphs.2020.04.013;
RA Takenaka R., Yasujima T., Furukawa J., Hishikawa Y., Yamashiro T., Ohta K.,
RA Inoue K., Yuasa H.;
RT "Functional Analysis of the Role of Equilibrative Nucleobase Transporter 1
RT (ENBT1/SLC43A3) in Adenine Transport in HepG2 Cells.";
RL J. Pharm. Sci. 109:2622-2628(2020).
CC -!- FUNCTION: Sodium-independent purine-selective nucleobase transporter
CC which mediates the equilibrative transport of extracellular purine
CC nucleobases such as adenine, guanine and hypoxanthine (PubMed:26455426,
CC PubMed:32339528). May regulate fatty acid (FA) transport in adipocytes,
CC acting as a positive regulator of FA efflux and as a negative regulator
CC of FA uptake (By similarity). {ECO:0000250|UniProtKB:A2AVZ9,
CC ECO:0000269|PubMed:26455426, ECO:0000269|PubMed:32339528}.
CC -!- FUNCTION: [Isoform 1]: Sodium-independent purine-selective nucleobase
CC transporter which mediates the equilibrative transport of extracellular
CC purine nucleobase adenine (PubMed:30910793). Mediates the influx and
CC efflux of the purine nucleobase analog drug 6-mercaptopurine across the
CC membrane (PubMed:30910793). {ECO:0000269|PubMed:30910793}.
CC -!- FUNCTION: [Isoform 2]: Sodium-independent purine-selective nucleobase
CC transporter which mediates the equilibrative transport of extracellular
CC purine nucleobase adenine (PubMed:30910793). Mediates the influx and
CC efflux of the purine nucleobase analog drug 6-mercaptopurine across the
CC membrane (PubMed:30910793). {ECO:0000269|PubMed:30910793}.
CC -!- ACTIVITY REGULATION: Adenine transport is strongly inhibited by
CC decynium-22. {ECO:0000269|PubMed:26455426,
CC ECO:0000269|PubMed:32339528}.
CC -!- ACTIVITY REGULATION: [Isoform 1]: 6-mercaptopurine-transport is
CC inhibited by 6-thioguanine, 6-methylmercaptopurine and decynium-22.
CC {ECO:0000269|PubMed:30910793}.
CC -!- ACTIVITY REGULATION: [Isoform 2]: 6-mercaptopurine-transport is
CC inhibited by 6-thioguanine, 6-methylmercaptopurine and decynium-22.
CC {ECO:0000269|PubMed:30910793}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.94 uM for adenine {ECO:0000269|PubMed:26455426};
CC KM=0.268 uM for adenine {ECO:0000269|PubMed:32339528};
CC KM=37 uM for adenine (isoform 1) {ECO:0000269|PubMed:32339528};
CC KM=40 uM for adenine (isoform 2) {ECO:0000269|PubMed:32339528};
CC KM=1.70 uM for guanine {ECO:0000269|PubMed:26455426};
CC KM=1.32 uM for hypoxanthine {ECO:0000269|PubMed:26455426};
CC KM=163 uM for 6-mercaptopurine (isoform 1)
CC {ECO:0000269|PubMed:32339528};
CC KM=188 uM for 6-mercaptopurine (isoform 2)
CC {ECO:0000269|PubMed:32339528};
CC Vmax=107.8 pmol/min/mg enzyme for adenine uptake
CC {ECO:0000269|PubMed:26455426};
CC Vmax=14.1 pmol/min/mg enzyme for adenine uptake
CC {ECO:0000269|PubMed:32339528};
CC Vmax=34 pmol/sec/mg enzyme for adenine uptake (isoform 1)
CC {ECO:0000269|PubMed:30910793};
CC Vmax=7.9 pmol/sec/mg enzyme for adenine uptake (isoform 2)
CC {ECO:0000269|PubMed:30910793};
CC Vmax=98.2 pmol/min/mg enzyme for guanine uptake
CC {ECO:0000269|PubMed:26455426};
CC Vmax=73.1 pmol/min/mg enzyme for hypoxanthine uptake
CC {ECO:0000269|PubMed:26455426};
CC Vmax=82 pmol/sec/mg enzyme for 6-mercaptopurine uptake (isoform 1)
CC {ECO:0000269|PubMed:30910793};
CC Vmax=32 pmol/sec/mg enzyme for 6-mercaptopurine uptake (isoform 2)
CC {ECO:0000269|PubMed:30910793};
CC -!- INTERACTION:
CC Q8NBI5; P55072: VCP; NbExp=3; IntAct=EBI-2855542, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC {ECO:0000269|PubMed:26455426}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8NBI5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NBI5-2; Sequence=VSP_055620;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in the liver
CC and lung, followed by the pancreas (PubMed:26455426). Highly expressed
CC in macrophages (Ref.1). {ECO:0000269|PubMed:26455426,
CC ECO:0000269|Ref.1}.
CC -!- SIMILARITY: Belongs to the SLC43A transporter (TC 2.A.1.44) family.
CC {ECO:0000305}.
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DR EMBL; AB028927; BAB82466.1; -; mRNA.
DR EMBL; AK298028; BAG60330.1; -; mRNA.
DR EMBL; CR457391; CAG33672.1; -; mRNA.
DR EMBL; AK075552; BAC11695.1; -; mRNA.
DR EMBL; AL157431; CAB75655.1; -; mRNA.
DR EMBL; AP000781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW73741.1; -; Genomic_DNA.
DR EMBL; BC003163; AAH03163.1; -; mRNA.
DR CCDS; CCDS60784.1; -. [Q8NBI5-2]
DR CCDS; CCDS7956.1; -. [Q8NBI5-1]
DR PIR; T46915; T46915.
DR RefSeq; NP_001265130.1; NM_001278201.1. [Q8NBI5-1]
DR RefSeq; NP_001265135.1; NM_001278206.1. [Q8NBI5-2]
DR RefSeq; NP_054815.2; NM_014096.3. [Q8NBI5-1]
DR RefSeq; NP_060081.1; NM_017611.2. [Q8NBI5-1]
DR RefSeq; NP_955361.1; NM_199329.2. [Q8NBI5-1]
DR AlphaFoldDB; Q8NBI5; -.
DR BioGRID; 118823; 54.
DR IntAct; Q8NBI5; 13.
DR STRING; 9606.ENSP00000434515; -.
DR DrugBank; DB00993; Azathioprine.
DR TCDB; 2.A.1.44.3; the major facilitator superfamily (mfs).
DR GlyGen; Q8NBI5; 4 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NBI5; -.
DR PhosphoSitePlus; Q8NBI5; -.
DR SwissPalm; Q8NBI5; -.
DR BioMuta; SLC43A3; -.
DR DMDM; 158706361; -.
DR EPD; Q8NBI5; -.
DR jPOST; Q8NBI5; -.
DR MassIVE; Q8NBI5; -.
DR MaxQB; Q8NBI5; -.
DR PaxDb; Q8NBI5; -.
DR PeptideAtlas; Q8NBI5; -.
DR PRIDE; Q8NBI5; -.
DR ProteomicsDB; 17547; -.
DR ProteomicsDB; 72772; -. [Q8NBI5-1]
DR Antibodypedia; 14150; 76 antibodies from 18 providers.
DR DNASU; 29015; -.
DR Ensembl; ENST00000352187.5; ENSP00000337561.1; ENSG00000134802.18. [Q8NBI5-1]
DR Ensembl; ENST00000395123.6; ENSP00000378555.2; ENSG00000134802.18. [Q8NBI5-1]
DR Ensembl; ENST00000395124.6; ENSP00000378556.1; ENSG00000134802.18. [Q8NBI5-1]
DR Ensembl; ENST00000529554.5; ENSP00000436254.1; ENSG00000134802.18. [Q8NBI5-1]
DR Ensembl; ENST00000533524.5; ENSP00000434515.1; ENSG00000134802.18. [Q8NBI5-2]
DR GeneID; 29015; -.
DR KEGG; hsa:29015; -.
DR MANE-Select; ENST00000395124.6; ENSP00000378556.1; NM_199329.3; NP_955361.1.
DR UCSC; uc001nkg.5; human. [Q8NBI5-1]
DR CTD; 29015; -.
DR DisGeNET; 29015; -.
DR GeneCards; SLC43A3; -.
DR HGNC; HGNC:17466; SLC43A3.
DR HPA; ENSG00000134802; Tissue enhanced (liver).
DR MIM; 618034; gene.
DR neXtProt; NX_Q8NBI5; -.
DR OpenTargets; ENSG00000134802; -.
DR PharmGKB; PA134924689; -.
DR VEuPathDB; HostDB:ENSG00000134802; -.
DR eggNOG; ENOG502QRYG; Eukaryota.
DR GeneTree; ENSGT00940000157622; -.
DR HOGENOM; CLU_035676_1_1_1; -.
DR InParanoid; Q8NBI5; -.
DR OMA; VCYEQEL; -.
DR OrthoDB; 639867at2759; -.
DR PhylomeDB; Q8NBI5; -.
DR TreeFam; TF328358; -.
DR PathwayCommons; Q8NBI5; -.
DR SignaLink; Q8NBI5; -.
DR BioGRID-ORCS; 29015; 21 hits in 1084 CRISPR screens.
DR ChiTaRS; SLC43A3; human.
DR GenomeRNAi; 29015; -.
DR Pharos; Q8NBI5; Tbio.
DR PRO; PR:Q8NBI5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q8NBI5; protein.
DR Bgee; ENSG00000134802; Expressed in right lobe of liver and 164 other tissues.
DR ExpressionAtlas; Q8NBI5; baseline and differential.
DR Genevisible; Q8NBI5; HS.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015207; F:adenine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015245; F:fatty acid transmembrane transporter activity; ISS:UniProtKB.
DR GO; GO:0015208; F:guanine transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0042910; F:xenobiotic transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0035344; P:hypoxanthine transport; IDA:UniProtKB.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR027197; SLC43A3.
DR PANTHER; PTHR20765; PTHR20765; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Glycoprotein; Lipid transport;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..491
FT /note="Equilibrative nucleobase transporter 1"
FT /id="PRO_0000305036"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 396..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 456..476
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOD_RES 253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 258
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 220
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 61
FT /note="A -> AGRLGCMGDLFSTP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055620"
FT VARIANT 53
FT /note="P -> L (in dbSNP:rs34799622)"
FT /id="VAR_035156"
FT CONFLICT 172
FT /note="V -> A (in Ref. 2; BAG60330)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="N -> D (in Ref. 4; BAC11695)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 491 AA; 54529 MW; C6BC8E48F38B1D8C CRC64;
MAGQGLPLHV ATLLTGLLEC LGFAGVLFGW PSLVFVFKNE DYFKDLCGPD AGPIGNATGQ
ADCKAQDERF SLIFTLGSFM NNFMTFPTGY IFDRFKTTVA RLIAIFFYTT ATLIIAFTSA
GSAVLLFLAM PMLTIGGILF LITNLQIGNL FGQHRSTIIT LYNGAFDSSS AVFLIIKLLY
EKGISLRASF IFISVCSTWH VARTFLLMPR GHIPYPLPPN YSYGLCPGNG TTKEEKETAE
HENRELQSKE FLSAKEETPG AGQKQELRSF WSYAFSRRFA WHLVWLSVIQ LWHYLFIGTL
NSLLTNMAGG DMARVSTYTN AFAFTQFGVL CAPWNGLLMD RLKQKYQKEA RKTGSSTLAV
ALCSTVPSLA LTSLLCLGFA LCASVPILPL QYLTFILQVI SRSFLYGSNA AFLTLAFPSE
HFGKLFGLVM ALSAVVSLLQ FPIFTLIKGS LQNDPFYVNV MFMLAILLTF FHPFLVYREC
RTWKESPSAI A
