ID   S19A1_MOUSE             Reviewed;         512 AA.
AC   P41438; Q62450; Q62451;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Reduced folate transporter {ECO:0000305};
DE   AltName: Full=Intestinal folate carrier 1 {ECO:0000303|PubMed:8664315};
DE            Short=IFC-1 {ECO:0000303|PubMed:8664315};
DE   AltName: Full=Plasma membrane folate antiporter SLC19A1 {ECO:0000305};
DE   AltName: Full=Reduced folate carrier 1 {ECO:0000303|PubMed:8276792};
DE            Short=RFC-1 {ECO:0000303|PubMed:8276792, ECO:0000303|PubMed:9111015};
DE            Short=RFC1 {ECO:0000303|PubMed:8276792};
DE   AltName: Full=Solute carrier family 19 member 1 {ECO:0000305};
GN   Name=Slc19a1 {ECO:0000312|MGI:MGI:103182};
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], AND FUNCTION.
RC   STRAIN=DBA;
RX   PubMed=8276792; DOI=10.1016/s0021-9258(17)42301-5;
RA   Dixon K.H., Lanpher B.C., Chiu J., Kelly K., Cowan K.H.;
RT   "A novel cDNA restores reduced folate carrier activity and methotrexate
RT   sensitivity to transport deficient cells.";
RL   J. Biol. Chem. 269:17-20(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC   STRAIN=DBA/2J; TISSUE=Intestine;
RX   PubMed=8664315; DOI=10.1016/0005-2736(96)00005-3;
RA   Said H.M., Nguyen T.T., Dyer D.L., Cowan K.H., Rubin S.A.;
RT   "Intestinal folate transport: identification of a cDNA involved in folate
RT   transport and the functional expression and distribution of its mRNA.";
RL   Biochim. Biophys. Acta 1281:164-172(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=DBA/2J;
RX   PubMed=7559435; DOI=10.1074/jbc.270.39.22974;
RA   Brigle K.E., Spinella M.J., Sierra E.E., Goldman I.D.;
RT   "Characterization of a mutation in the reduced folate carrier in a
RT   transport defective L1210 murine leukemia cell line.";
RL   J. Biol. Chem. 270:22974-22979(1995).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2 AND 3).
RX   PubMed=9161403; DOI=10.1016/s0378-1119(96)00676-2;
RA   Tolner B.M., Roy K., Sirotnak F.M.;
RT   "Organization, structure and alternate splicing of the murine RFC-1 gene
RT   encoding a folate transporter.";
RL   Gene 189:1-7(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N; 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-467 AND SER-477, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472 AND SER-477, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Kidney;
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).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=10787414; DOI=10.1074/jbc.m002328200;
RA   Chancy C.D., Kekuda R., Huang W., Prasad P.D., Kuhnel J.M., Sirotnak F.M.,
RA   Roon P., Ganapathy V., Smith S.B.;
RT   "Expression and differential polarization of the reduced-folate
RT   transporter-1 and the folate receptor alpha in mammalian retinal pigment
RT   epithelium.";
RL   J. Biol. Chem. 275:20676-20684(2000).
RN   [9]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9111015; DOI=10.1074/jbc.272.17.11165;
RA   Chiao J.H., Roy K., Tolner B., Yang C.H., Sirotnak F.M.;
RT   "RFC-1 gene expression regulates folate absorption in mouse small
RT   intestine.";
RL   J. Biol. Chem. 272:11165-11170(1997).
RN   [10]
RP   FUNCTION, TRANSPORTER ACTIVITY, AND MUTAGENESIS OF ILE-48 AND TRP-105.
RX   PubMed=9748272; DOI=10.1074/jbc.273.40.25953;
RA   Tse A., Brigle K., Taylor S.M., Moran R.G.;
RT   "Mutations in the reduced folate carrier gene which confer dominant
RT   resistance to 5,10-dideazatetrahydrofolate.";
RL   J. Biol. Chem. 273:25953-25960(1998).
RN   [11]
RP   LACK OF CYCLIC DINUCLEOTIDE TRANSPORTER ACTIVITY.
RX   PubMed=31511694; DOI=10.1038/s41586-019-1553-0;
RA   Luteijn R.D., Zaver S.A., Gowen B.G., Wyman S.K., Garelis N.E., Onia L.,
RA   McWhirter S.M., Katibah G.E., Corn J.E., Woodward J.J., Raulet D.H.;
RT   "SLC19A1 transports immunoreactive cyclic dinucleotides.";
RL   Nature 573:434-438(2019).
CC   -!- FUNCTION: Antiporter that mediates the import of reduced folates
CC       (PubMed:8276792, PubMed:8664315, PubMed:9111015, PubMed:9748272).
CC       Mechanistically, acts as a secondary active transporter, which exports
CC       intracellular organic anions down their concentration gradients to
CC       facilitate the uptake of its substrates (By similarity). Has high
CC       affinity for N5-methyltetrahydrofolate, the predominant circulating
CC       form of folate (PubMed:8276792, PubMed:9111015). Also able to mediate
CC       the import of antifolate drug methotrexate (PubMed:8276792,
CC       PubMed:8664315, PubMed:9748272). 5-amino-4-imidazolecarboxamide
CC       riboside (AICAR), when phosphorylated to AICAR monophosphate, can serve
CC       as an organic anion for antiporter activity (By similarity).
CC       {ECO:0000250|UniProtKB:P41440, ECO:0000269|PubMed:8276792,
CC       ECO:0000269|PubMed:8664315, ECO:0000269|PubMed:9111015,
CC       ECO:0000269|PubMed:9748272}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate(out) + 5-amino-1-(5-
CC         phospho-beta-D-ribosyl)imidazole-4-carboxamide(in) = (6S)-5-
CC         methyl-5,6,7,8-tetrahydrofolate(in) + 5-amino-1-(5-phospho-beta-D-
CC         ribosyl)imidazole-4-carboxamide(out); Xref=Rhea:RHEA:60460,
CC         ChEBI:CHEBI:18608, ChEBI:CHEBI:58475;
CC         Evidence={ECO:0000269|PubMed:9111015, ECO:0000269|PubMed:9748272};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:60461;
CC         Evidence={ECO:0000269|PubMed:9111015, ECO:0000269|PubMed:9748272};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.8 uM for N5-methyltetrahydrofolate (at pH 6.2)
CC         {ECO:0000269|PubMed:9111015};
CC         KM=2.3 uM for N5-methyltetrahydrofolate (at pH 7.4)
CC         {ECO:0000269|PubMed:9111015};
CC         Vmax=0.8 pmol/min/mg enzyme with N5-methyltetrahydrofolate as
CC         substrate (at pH 6.2) {ECO:0000269|PubMed:9111015};
CC         Vmax=0.2 pmol/min/mg enzyme with N5-methyltetrahydrofolate as
CC         substrate (at pH 7.4) {ECO:0000269|PubMed:9111015};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10787414};
CC       Multi-pass membrane protein {ECO:0000255}. Apical cell membrane
CC       {ECO:0000269|PubMed:10787414}; Multi-pass membrane protein
CC       {ECO:0000255}. Basolateral cell membrane
CC       {ECO:0000250|UniProtKB:P41440}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=P41438-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P41438-2; Sequence=VSP_006125;
CC       Name=3;
CC         IsoId=P41438-3; Sequence=VSP_006126, VSP_006127;
CC   -!- SIMILARITY: Belongs to the reduced folate carrier (RFC) transporter
CC       (TC 2.A.48) family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to human, not able to transport immunoreactive
CC       cyclic dinucleotides, such as cyclic GMP-AMP (2'-3'-cGAMP), an immune
CC       messenger produced in response to DNA virus in the cytosol.
CC       {ECO:0000269|PubMed:31511694}.
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DR   EMBL; L36539; AAB38483.1; -; mRNA.
DR   EMBL; L23755; AAA39738.1; -; mRNA.
DR   EMBL; U32469; AAC52258.1; -; mRNA.
DR   EMBL; U66103; AAC53287.1; -; mRNA.
DR   EMBL; U57784; AAC53288.1; -; Genomic_DNA.
DR   EMBL; U57781; AAC53288.1; JOINED; Genomic_DNA.
DR   EMBL; U57782; AAC53288.1; JOINED; Genomic_DNA.
DR   EMBL; U57783; AAC53288.1; JOINED; Genomic_DNA.
DR   EMBL; U57785; AAC53289.1; -; Genomic_DNA.
DR   EMBL; U57781; AAC53289.1; JOINED; Genomic_DNA.
DR   EMBL; U57782; AAC53289.1; JOINED; Genomic_DNA.
DR   EMBL; U57783; AAC53289.1; JOINED; Genomic_DNA.
DR   EMBL; U57785; AAC53290.1; -; Genomic_DNA.
DR   EMBL; U57781; AAC53290.1; JOINED; Genomic_DNA.
DR   EMBL; U57782; AAC53290.1; JOINED; Genomic_DNA.
DR   EMBL; U57783; AAC53290.1; JOINED; Genomic_DNA.
DR   EMBL; U57784; AAC53290.1; JOINED; Genomic_DNA.
DR   EMBL; U57785; AAC53291.1; -; Genomic_DNA.
DR   EMBL; U57781; AAC53291.1; JOINED; Genomic_DNA.
DR   EMBL; U57782; AAC53291.1; JOINED; Genomic_DNA.
DR   EMBL; U57783; AAC53291.1; JOINED; Genomic_DNA.
DR   EMBL; BC015263; AAH15263.1; -; mRNA.
DR   CCDS; CCDS35947.1; -. [P41438-1]
DR   PIR; A53092; A53092.
DR   RefSeq; NP_001186200.1; NM_001199271.1. [P41438-1]
DR   RefSeq; NP_112473.1; NM_031196.3. [P41438-1]
DR   RefSeq; XP_006513477.1; XM_006513414.3. [P41438-1]
DR   RefSeq; XP_006513478.1; XM_006513415.3. [P41438-1]
DR   RefSeq; XP_006513479.1; XM_006513416.2. [P41438-1]
DR   RefSeq; XP_006513480.1; XM_006513417.2. [P41438-1]
DR   RefSeq; XP_006513481.1; XM_006513418.3.
DR   AlphaFoldDB; P41438; -.
DR   SMR; P41438; -.
DR   STRING; 10090.ENSMUSP00000101050; -.
DR   iPTMnet; P41438; -.
DR   PhosphoSitePlus; P41438; -.
DR   SwissPalm; P41438; -.
DR   EPD; P41438; -.
DR   jPOST; P41438; -.
DR   MaxQB; P41438; -.
DR   PaxDb; 10090-ENSMUSP00000101050; -.
DR   PeptideAtlas; P41438; -.
DR   ProteomicsDB; 253354; -. [P41438-1]
DR   ProteomicsDB; 253355; -. [P41438-2]
DR   ProteomicsDB; 253356; -. [P41438-3]
DR   Antibodypedia; 10491; 134 antibodies from 21 providers.
DR   DNASU; 20509; -.
DR   Ensembl; ENSMUST00000105410.10; ENSMUSP00000101050.4; ENSMUSG00000001436.16. [P41438-1]
DR   Ensembl; ENSMUST00000144234.8; ENSMUSP00000116784.2; ENSMUSG00000001436.16. [P41438-1]
DR   GeneID; 20509; -.
DR   KEGG; mmu:20509; -.
DR   UCSC; uc007fvc.2; mouse. [P41438-1]
DR   AGR; MGI:103182; -.
DR   CTD; 6573; -.
DR   MGI; MGI:103182; Slc19a1.
DR   VEuPathDB; HostDB:ENSMUSG00000001436; -.
DR   eggNOG; KOG3810; Eukaryota.
DR   GeneTree; ENSGT00950000183022; -.
DR   HOGENOM; CLU_036909_2_0_1; -.
DR   InParanoid; P41438; -.
DR   OMA; MQFMELF; -.
DR   OrthoDB; 51626at2759; -.
DR   PhylomeDB; P41438; -.
DR   TreeFam; TF313684; -.
DR   Reactome; R-MMU-196757; Metabolism of folate and pterines.
DR   BioGRID-ORCS; 20509; 5 hits in 78 CRISPR screens.
DR   ChiTaRS; Slc19a1; mouse.
DR   PRO; PR:P41438; -.
DR   Proteomes; UP000000589; Chromosome 10.
DR   RNAct; P41438; Protein.
DR   Bgee; ENSMUSG00000001436; Expressed in paneth cell and 275 other cell types or tissues.
DR   ExpressionAtlas; P41438; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0016323; C:basolateral plasma membrane; ISO:MGI.
DR   GO; GO:0031526; C:brush border membrane; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0061507; F:2',3'-cyclic GMP-AMP binding; ISO:MGI.
DR   GO; GO:0015297; F:antiporter activity; ISS:UniProtKB.
DR   GO; GO:0008518; F:folate:monoatomic anion antiporter activity; ISS:UniProtKB.
DR   GO; GO:0005542; F:folic acid binding; ISO:MGI.
DR   GO; GO:0008517; F:folic acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0015350; F:methotrexate transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0008514; F:organic anion transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0042910; F:xenobiotic transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR   GO; GO:1904447; P:folate import across plasma membrane; IDA:UniProtKB.
DR   GO; GO:0098838; P:folate transmembrane transport; IDA:UniProtKB.
DR   GO; GO:0015884; P:folic acid transport; ISO:MGI.
DR   GO; GO:0051958; P:methotrexate transport; IDA:UniProtKB.
DR   GO; GO:0015711; P:organic anion transport; ISO:MGI.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; ISO:MGI.
DR   Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR   InterPro; IPR002666; Folate_carrier.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR028339; SLC19A1.
DR   NCBIfam; TIGR00806; rfc; 1.
DR   PANTHER; PTHR10686; FOLATE TRANSPORTER; 1.
DR   PANTHER; PTHR10686:SF12; REDUCED FOLATE TRANSPORTER; 1.
DR   Pfam; PF01770; Folate_carrier; 1.
DR   PIRSF; PIRSF028739; Folate_carrier; 1.
DR   PIRSF; PIRSF500793; Folate_transporter_1; 1.
DR   SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR   Genevisible; P41438; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Antiport; Cell membrane; Folate-binding;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Reduced folate transporter"
FT                   /id="PRO_0000178661"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        28..48
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..64
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        65..85
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        86..91
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        92..112
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        113..121
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        122..142
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        143..155
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        156..176
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        177..180
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        181..201
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        202..271
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        272..292
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        293..304
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        305..325
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        326..329
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        330..350
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        351..354
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        355..375
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        376..390
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        391..411
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        412..426
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   TRANSMEM        427..447
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        448..512
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   REGION          400..412
FT                   /note="Required for substrate-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   REGION          478..512
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..512
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         1
FT                   /note="N-acetylmethionine"
FT                   /evidence="ECO:0000250|UniProtKB:P41440"
FT   MOD_RES         467
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   MOD_RES         472
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         477
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319,
FT                   ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         273..313
FT                   /note="WWVFNSSGYYLITYYVHVLWRSTDSSLSYNGAVDAASTLLS -> C (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:9161403"
FT                   /id="VSP_006125"
FT   VAR_SEQ         378..379
FT                   /note="FQ -> PS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9161403"
FT                   /id="VSP_006126"
FT   VAR_SEQ         380..512
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:9161403"
FT                   /id="VSP_006127"
FT   MUTAGEN         48
FT                   /note="I->F: Induces resistance to
FT                   5,10-dideazatetrahydrofolate; when associated with G-105."
FT                   /evidence="ECO:0000269|PubMed:9748272"
FT   MUTAGEN         105
FT                   /note="W->G: Induces resistance to
FT                   5,10-dideazatetrahydrofolate; when associated with F-48."
FT                   /evidence="ECO:0000269|PubMed:9748272"
SQ   SEQUENCE   512 AA;  58150 MW;  640CB7AD2624BF67 CRC64;
     MVPTGQVAEK QAYEEPRQDH ELKSWRCLVF YLCFFGFMAQ LRPGESFITP FLLERKFTKE
     QVTNEIIPML PYSHLAVLVP VFLLTDYLRY KPVLVLQCLS FVCVWLLLLL GTSVVHMQLM
     EVFYSVTMAA RIAYSSYIFS LVHPSRYQRM ASYSRAAVLL GVFISSVLGQ ALVTVGHIST
     YTLNCVSLGF ILFSLVLSLF LKRPKRSLFF NRSTLARGAL PCELDQMHPG PDRPETRKLD
     RMLGTCRDSF LVRMLSELVE NARQPQLRLW CLWWVFNSSG YYLITYYVHV LWRSTDSSLS
     YNGAVDAAST LLSAITSFSA GFLSIRWTLW SKLVIAGVIA IQASLVFCMF QIRDIWVCYV
     TFVLFRGAYQ FLVPIATFQI ASSLSKELCA LVFGINTFLA TALKTCITLV VSDKRGLGLQ
     VRDQFRIYFI YFLMLSITCF AWAGLDGLRY CQRGRHQPLA QAQELRSPLE TSVQAISLQD
     GDLRGPQPSA PQLLSEDGME DDRGDLRVEA KA
//