ID   S23A2_MOUSE             Reviewed;         648 AA.
AC   Q9EPR4; Q80Y23; Q8C327; Q9JM78;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   22-SEP-2009, sequence version 2.
DT   27-MAR-2024, entry version 175.
DE   RecName: Full=Solute carrier family 23 member 2;
DE   AltName: Full=Na(+)/L-ascorbic acid transporter 2;
DE   AltName: Full=Sodium-dependent vitamin C transporter 2;
DE            Short=SVCT-2;
DE            Short=mSVCT2;
DE   AltName: Full=Yolk sac permease-like molecule 2;
GN   Name=Slc23a2;
GN   Synonyms=Kiaa0238 {ECO:0000303|PubMed:12693553}, Svct2, Yspl2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   STRAIN=129/SvEv; TISSUE=Brain;
RX   PubMed=11214969; DOI=10.1093/dnares/7.6.339;
RA   Gispert S., Dutra A., Lieberman A., Friedlich D., Nussbaum R.L.;
RT   "Cloning and genomic organization of the mouse gene slc23a1 encoding a
RT   vitamin C transporter.";
RL   DNA Res. 7:339-345(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Lung;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Embryo;
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   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 8-647 (ISOFORM 1).
RC   TISSUE=Brain;
RA   Fujita I., Hirano J., Tanaka K.;
RT   "Mouse sodium dependent vitamin C transporter 2 (mSVCT2).";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 108-648 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA   Nakajima D., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT   The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:35-48(2003).
RN   [8]
RP   TISSUE SPECIFICITY, AND DISEASE.
RX   PubMed=17689499; DOI=10.1016/j.bcp.2007.05.024;
RA   Wu X., Iguchi T., Hirano J., Fujita I., Ueda H., Itoh N., Tanaka K.,
RA   Nakanishi T.;
RT   "Upregulation of sodium-dependent vitamin C transporter 2 expression in
RT   adrenals increases norepinephrine production and aggravates hyperlipidemia
RT   in mice with streptozotocin-induced diabetes.";
RL   Biochem. Pharmacol. 74:1020-1028(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-70; SER-78; THR-79; SER-81
RP   AND THR-647, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, and Lung;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Sodium/ascorbate cotransporter. Mediates electrogenic uptake
CC       of vitamin C, with a stoichiometry of 2 Na(+) for each ascorbate.
CC       {ECO:0000250|UniProtKB:Q9UGH3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-ascorbate(out) + 2 Na(+)(out) = L-ascorbate(in) + 2
CC         Na(+)(in); Xref=Rhea:RHEA:69883, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:38290; Evidence={ECO:0000250|UniProtKB:Q9UGH3};
CC   -!- SUBUNIT: Interacts with CLSTN3. {ECO:0000250|UniProtKB:Q9UGH3}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9UGH3};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9UGH3}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9EPR4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9EPR4-2; Sequence=VSP_007367, VSP_007368;
CC   -!- TISSUE SPECIFICITY: Expressed in metabolically active and specialized
CC       tissues, including high expression in brain and adrenals. Detected in a
CC       wide range of tissues. Expression in kidney is almost undetectable.
CC       {ECO:0000269|PubMed:17689499}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UGH3}.
CC   -!- DISEASE: Note=Elevated expression levels in the adrenals of diabetic
CC       mice. {ECO:0000269|PubMed:17689499}.
CC   -!- SIMILARITY: Belongs to the nucleobase:cation symporter-2 (NCS2)
CC       (TC 2.A.40) family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG02252.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA90751.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC65509.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AY004874; AAG02252.1; ALT_INIT; mRNA.
DR   EMBL; AK087175; BAC39819.1; -; mRNA.
DR   EMBL; AL831706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466519; EDL28341.1; -; Genomic_DNA.
DR   EMBL; BC050823; AAH50823.1; -; mRNA.
DR   EMBL; AB038145; BAA90751.1; ALT_INIT; mRNA.
DR   EMBL; AK122227; BAC65509.1; ALT_SEQ; Transcribed_RNA.
DR   CCDS; CCDS16769.1; -. [Q9EPR4-1]
DR   RefSeq; NP_061294.2; NM_018824.2. [Q9EPR4-1]
DR   RefSeq; XP_006499969.1; XM_006499906.3.
DR   RefSeq; XP_006499970.1; XM_006499907.3. [Q9EPR4-1]
DR   RefSeq; XP_011238000.1; XM_011239698.2. [Q9EPR4-1]
DR   RefSeq; XP_017174620.1; XM_017319131.1.
DR   AlphaFoldDB; Q9EPR4; -.
DR   SMR; Q9EPR4; -.
DR   BioGRID; 207613; 1.
DR   STRING; 10090.ENSMUSP00000028815; -.
DR   GlyCosmos; Q9EPR4; 2 sites, No reported glycans.
DR   GlyGen; Q9EPR4; 2 sites.
DR   iPTMnet; Q9EPR4; -.
DR   PhosphoSitePlus; Q9EPR4; -.
DR   SwissPalm; Q9EPR4; -.
DR   EPD; Q9EPR4; -.
DR   jPOST; Q9EPR4; -.
DR   MaxQB; Q9EPR4; -.
DR   PaxDb; 10090-ENSMUSP00000028815; -.
DR   PeptideAtlas; Q9EPR4; -.
DR   ProteomicsDB; 253366; -. [Q9EPR4-1]
DR   ProteomicsDB; 253367; -. [Q9EPR4-2]
DR   Pumba; Q9EPR4; -.
DR   Antibodypedia; 42663; 143 antibodies from 23 providers.
DR   DNASU; 54338; -.
DR   Ensembl; ENSMUST00000028815.15; ENSMUSP00000028815.9; ENSMUSG00000027340.16. [Q9EPR4-1]
DR   GeneID; 54338; -.
DR   KEGG; mmu:54338; -.
DR   UCSC; uc008mmi.1; mouse. [Q9EPR4-1]
DR   UCSC; uc008mmj.1; mouse. [Q9EPR4-2]
DR   AGR; MGI:1859682; -.
DR   CTD; 9962; -.
DR   MGI; MGI:1859682; Slc23a2.
DR   VEuPathDB; HostDB:ENSMUSG00000027340; -.
DR   eggNOG; KOG1292; Eukaryota.
DR   GeneTree; ENSGT00950000182953; -.
DR   HOGENOM; CLU_017959_5_4_1; -.
DR   InParanoid; Q9EPR4; -.
DR   OMA; NVSAYCR; -.
DR   OrthoDB; 911690at2759; -.
DR   PhylomeDB; Q9EPR4; -.
DR   TreeFam; TF313272; -.
DR   Reactome; R-MMU-196836; Vitamin C (ascorbate) metabolism.
DR   BioGRID-ORCS; 54338; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Slc23a2; mouse.
DR   PRO; PR:Q9EPR4; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q9EPR4; Protein.
DR   Bgee; ENSMUSG00000027340; Expressed in choroid plexus of fourth ventricle and 236 other cell types or tissues.
DR   ExpressionAtlas; Q9EPR4; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; ISO:MGI.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:UniProtKB.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008520; F:L-ascorbate:sodium symporter activity; IMP:MGI.
DR   GO; GO:0015229; F:L-ascorbic acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR   GO; GO:0071361; P:cellular response to ethanol; IEA:Ensembl.
DR   GO; GO:0019852; P:L-ascorbic acid metabolic process; ISO:MGI.
DR   GO; GO:0015882; P:L-ascorbic acid transmembrane transport; IDA:UniProtKB.
DR   GO; GO:1903861; P:positive regulation of dendrite extension; ISO:MGI.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
DR   InterPro; IPR006043; NCS2.
DR   InterPro; IPR006042; Xan_ur_permease.
DR   PANTHER; PTHR11119:SF33; SOLUTE CARRIER FAMILY 23 MEMBER 2; 1.
DR   PANTHER; PTHR11119; XANTHINE-URACIL / VITAMIN C PERMEASE FAMILY MEMBER; 1.
DR   Pfam; PF00860; Xan_ur_permease; 1.
DR   PROSITE; PS01116; XANTH_URACIL_PERMASE; 1.
DR   Genevisible; Q9EPR4; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW   Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW   Sodium; Sodium transport; Symport; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..648
FT                   /note="Solute carrier family 23 member 2"
FT                   /id="PRO_0000165979"
FT   TOPO_DOM        9..110
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..139
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        161
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        183..216
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        217..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        238..264
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        265..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..286
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        287..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        301..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..369
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        370..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        391..415
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        416..436
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        437..459
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        460..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        481..483
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        484..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        505..514
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        515..535
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        536..545
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        546..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        567..648
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         70
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         75
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTW8"
FT   MOD_RES         78
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         79
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         81
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         647
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   CARBOHYD        188
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        196
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         162..272
FT                   /note="LPLFQASAFAFLAPARAILSLDKWKCNTTEITVANGTAELLEHIWHPRIQEI
FT                   QGAIIMSSLIEVVIGLLGLPGALLRYIGPLTITPTVALIGLSGFQAAGERAGKHWGIAM
FT                   -> DYSCQWNGRAVGTHLASPNPRDPGGYHHVLTDRSGHWPPWPAWGSAEVYWTLDHHT
FT                   HRGPHWPLWFPGSRRESRKALGHCHAVSVLRELQGWGTIFTTMWDSLVEYLKQSH (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007367"
FT   VAR_SEQ         273..648
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_007368"
SQ   SEQUENCE   648 AA;  70049 MW;  2590BB11B2A257CB CRC64;
     MMGIGKNTAS KSVEAGGSTE GKYEEEAKHS NFFTLPVVIN GGATSSGEQD NEDTELMAIY
     TTENGIAEKS SLAETLDSTG SLDPQRSDMI YTIEDVPPWY LCIFLGLQHY LTCFSGTIAV
     PFLLADAMCV GDDQWATSQL IGTIFFCVGI TTLLQTTFGC RLPLFQASAF AFLAPARAIL
     SLDKWKCNTT EITVANGTAE LLEHIWHPRI QEIQGAIIMS SLIEVVIGLL GLPGALLRYI
     GPLTITPTVA LIGLSGFQAA GERAGKHWGI AMLTIFLVLL FSQYARNVKF PLPIYKSKKG
     WTAYKFQLFK MFPIILAILV SWLLCFIFTV TDVFPSNSTD YGYYARTDAR KGVLLVAPWF
     KVPYPFQWGM PTVSAAGVIG MLSAVVASII ESIGDYYACA RLSCAPPPPI HAINRGIFVE
     GLSCVLDGIF GTGNGSTSSS PNIGVLGITK VGSRRVIQYG AALMLGLGMV GKFSALFASL
     PDPVLGALFC TLFGMITAVG LSNLQFIDLN SSRNLFVLGF SIFFGLVLPS YLRQNPLVTG
     ITGIDQILNV LLTTAMFVGG CVAFILDNTI PGTPEERGIK KWKKGVSKGS KSLDGMESYN
     LPFGMNIIKK YRCFSYLPIS PTFAGYTWKG FGKSENSRSS DKDSQATV
//