ID   YLAT2_MOUSE             Reviewed;         515 AA.
AC   Q8BGK6; Q3TMY5; Q3U084; Q6ZQF5; Q8CFY3;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 149.
DE   RecName: Full=Y+L amino acid transporter 2 {ECO:0000305};
DE   AltName: Full=Solute carrier family 7 member 6;
DE   AltName: Full=y(+)L-type amino acid transporter 2;
DE            Short=Y+LAT2;
DE            Short=y+LAT-2;
GN   Name=Slc7a6 {ECO:0000312|MGI:MGI:2142598};
GN   Synonyms=Kiaa0245 {ECO:0000312|EMBL:BAC97909.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAC97909.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Embryonic tail {ECO:0000312|EMBL:BAC97909.1};
RX   PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 10:167-180(2003).
RN   [2] {ECO:0000305, ECO:0000312|EMBL:BAC33770.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC33770.1}, and NOD
RC   {ECO:0000312|EMBL:BAE33971.1};
RC   TISSUE=Embryo {ECO:0000312|EMBL:BAC33770.1}, Embryonic stem cell
RC   {ECO:0000312|EMBL:BAE38304.1}, Embryonic stomach
RC   {ECO:0000312|EMBL:BAE37866.1}, Eye {ECO:0000312|EMBL:BAC35581.1}, Lung
RC   {ECO:0000312|EMBL:BAE38497.1}, and Spleen
RC   {ECO:0000312|EMBL:BAE33971.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAH38404.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=FVB/N {ECO:0000312|EMBL:AAH38404.1};
RC   TISSUE=Mammary tumor {ECO:0000312|EMBL:AAH38404.1};
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   [4] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 140-293 (ISOFORM 1), AND TISSUE SPECIFICITY.
RX   PubMed=10903140; DOI=10.1042/bj3490787;
RA   Broeer A., Wagner C.A., Lang F., Broeer S.;
RT   "The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine
RT   efflux in exchange with glutamine.";
RL   Biochem. J. 349:787-795(2000).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND IDENTIFICATION BY
RP   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   [6]
RP   FUNCTION.
RX   PubMed=24599290; DOI=10.1095/biolreprod.113.116939;
RA   Corbett H.E., Dube C.D., Slow S., Lever M., Trasler J.M., Baltz J.M.;
RT   "Uptake of betaine into mouse cumulus-oocyte complexes via the SLC7A6
RT   isoform of y+L transporter.";
RL   Biol. Reprod. 90:81-81(2014).
CC   -!- FUNCTION: Heterodimer with SLC3A2, that functions as an antiporter
CC       which operates as an efflux route by exporting cationic amino acids
CC       such as L-arginine from inside the cells in exchange with neutral amino
CC       acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and
CC       may participate in nitric oxide synthesis (By similarity). Also
CC       exchanges L-arginine with L-lysine in a sodium-independent manner (By
CC       similarity). The transport mechanism is electroneutral and operates
CC       with a stoichiometry of 1:1 (By similarity). Contributes to ammonia-
CC       induced increase of L-arginine uptake in cerebral cortical astrocytes
CC       leading to ammonia-dependent increase of nitric oxide (NO) production
CC       via inducible nitric oxide synthase (iNOS) induction, and protein
CC       nitration (By similarity). May mediate transport of ornithine in
CC       retinal pigment epithelial (RPE) cells (By similarity). May also
CC       transport glycine betaine in a sodium dependent manner from the cumulus
CC       granulosa into the enclosed oocyte (PubMed:24599290).
CC       {ECO:0000250|UniProtKB:D3ZMM8, ECO:0000250|UniProtKB:Q92536,
CC       ECO:0000269|PubMed:24599290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-lysine(out) = L-arginine(out) + L-
CC         lysine(in); Xref=Rhea:RHEA:70827, ChEBI:CHEBI:32551,
CC         ChEBI:CHEBI:32682; Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-leucine(out) + Na(+)(out) = L-arginine(out)
CC         + L-leucine(in) + Na(+)(in); Xref=Rhea:RHEA:70831, ChEBI:CHEBI:29101,
CC         ChEBI:CHEBI:32682, ChEBI:CHEBI:57427;
CC         Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-glutamine(out) + Na(+)(out) = L-
CC         arginine(out) + L-glutamine(in) + Na(+)(in); Xref=Rhea:RHEA:70835,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:58359;
CC         Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-histidine(out) + Na(+)(out) = L-
CC         arginine(out) + L-histidine(in) + Na(+)(in); Xref=Rhea:RHEA:70839,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57595;
CC         Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-cysteine(out) + Na(+)(out) = L-
CC         arginine(out) + L-cysteine(in) + Na(+)(in); Xref=Rhea:RHEA:70847,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:35235;
CC         Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-arginine(in) + L-methionine(out) + Na(+)(out) = L-
CC         arginine(out) + L-methionine(in) + Na(+)(in); Xref=Rhea:RHEA:70843,
CC         ChEBI:CHEBI:29101, ChEBI:CHEBI:32682, ChEBI:CHEBI:57844;
CC         Evidence={ECO:0000250|UniProtKB:Q92536};
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc. {ECO:0000250|UniProtKB:Q92536}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q92536};
CC       Multi-pass membrane protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1 {ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:16141072};
CC         IsoId=Q8BGK6-1; Sequence=Displayed;
CC       Name=2 {ECO:0000269|PubMed:14621295};
CC         IsoId=Q8BGK6-2; Sequence=VSP_052833, VSP_052834;
CC   -!- TISSUE SPECIFICITY: Strongest expression in brain but also detected in
CC       testis, parotis, small intestine, heart and kidney. Weakly expressed in
CC       spleen, lung and liver. {ECO:0000269|PubMed:10903140}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.
CC       {ECO:0000255}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH38404.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=BAC97909.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AK129099; BAC97909.1; ALT_INIT; mRNA.
DR   EMBL; AK049478; BAC33770.1; -; mRNA.
DR   EMBL; AK053899; BAC35581.1; -; mRNA.
DR   EMBL; AK157127; BAE33971.1; -; mRNA.
DR   EMBL; AK164666; BAE37866.1; -; mRNA.
DR   EMBL; AK165629; BAE38304.1; -; mRNA.
DR   EMBL; AK165979; BAE38497.1; -; mRNA.
DR   EMBL; BC038404; AAH38404.1; ALT_FRAME; mRNA.
DR   CCDS; CCDS22631.1; -. [Q8BGK6-1]
DR   RefSeq; NP_848913.1; NM_178798.3. [Q8BGK6-1]
DR   RefSeq; XP_006531200.1; XM_006531137.3.
DR   RefSeq; XP_006531201.1; XM_006531138.3. [Q8BGK6-1]
DR   RefSeq; XP_017168357.1; XM_017312868.1. [Q8BGK6-1]
DR   AlphaFoldDB; Q8BGK6; -.
DR   SMR; Q8BGK6; -.
DR   BioGRID; 237036; 2.
DR   STRING; 10090.ENSMUSP00000034378; -.
DR   iPTMnet; Q8BGK6; -.
DR   PhosphoSitePlus; Q8BGK6; -.
DR   SwissPalm; Q8BGK6; -.
DR   EPD; Q8BGK6; -.
DR   MaxQB; Q8BGK6; -.
DR   PaxDb; 10090-ENSMUSP00000034378; -.
DR   PeptideAtlas; Q8BGK6; -.
DR   ProteomicsDB; 275118; -. [Q8BGK6-1]
DR   ProteomicsDB; 275119; -. [Q8BGK6-2]
DR   Pumba; Q8BGK6; -.
DR   Antibodypedia; 55124; 122 antibodies from 18 providers.
DR   DNASU; 330836; -.
DR   Ensembl; ENSMUST00000034378.5; ENSMUSP00000034378.4; ENSMUSG00000031904.6. [Q8BGK6-1]
DR   GeneID; 330836; -.
DR   KEGG; mmu:330836; -.
DR   UCSC; uc009nfl.1; mouse. [Q8BGK6-1]
DR   UCSC; uc009nfo.1; mouse. [Q8BGK6-2]
DR   AGR; MGI:2142598; -.
DR   CTD; 9057; -.
DR   MGI; MGI:2142598; Slc7a6.
DR   VEuPathDB; HostDB:ENSMUSG00000031904; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000158295; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q8BGK6; -.
DR   OMA; QIVFRRR; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; Q8BGK6; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 330836; 25 hits in 75 CRISPR screens.
DR   ChiTaRS; Slc7a6; mouse.
DR   PRO; PR:Q8BGK6; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q8BGK6; Protein.
DR   Bgee; ENSMUSG00000031904; Expressed in spermatocyte and 246 other cell types or tissues.
DR   ExpressionAtlas; Q8BGK6; baseline and differential.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0034618; F:arginine binding; ISS:UniProtKB.
DR   GO; GO:0015174; F:basic amino acid transmembrane transporter activity; ISO:MGI.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0061459; F:L-arginine transmembrane transporter activity; ISS:UniProtKB.
DR   GO; GO:0106439; F:L-lysine:L-arginine antiporter activity; ISS:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0031460; P:glycine betaine transport; IDA:UniProtKB.
DR   GO; GO:1903826; P:L-arginine transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0015820; P:leucine transport; ISO:MGI.
DR   GO; GO:0015804; P:neutral amino acid transport; ISS:UniProtKB.
DR   GO; GO:0006809; P:nitric oxide biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0015822; P:ornithine transport; ISO:MGI.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF398; Y+L AMINO ACID TRANSPORTER 2; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; Q8BGK6; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Antiport; Cell membrane;
KW   Disulfide bond; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..515
FT                   /note="Y+L amino acid transporter 2"
FT                   /id="PRO_0000341478"
FT   TOPO_DOM        1..44
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        66..78
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        100..114
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        136..167
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..194
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        216..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..266
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        288..311
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..363
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        364..384
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        385
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        386..406
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        407..424
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        425..445
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        446..451
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        452..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        473..515
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         30
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19144319"
FT   VAR_SEQ         1..164
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_052833"
FT   VAR_SEQ         165..216
FT                   /note="ACRLLAAACVCLLTFVNCAYVKWGTRVQDTFTYAKVLALIAIIIMGLVKLCQ
FT                   -> MFFFLPLPCFLSLFFFLLLFHLFNSPSVFFLFFTFLLSPFSFAWSPTRLCPT (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14621295"
FT                   /id="VSP_052834"
FT   CONFLICT        129
FT                   /note="W -> R (in Ref. 2; BAE33971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        132
FT                   /note="L -> P (in Ref. 2; BAE38304)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   515 AA;  56771 MW;  8DF8352607228507 CRC64;
     MEAQELGSPT PTYHLLPKAN QHTVKEDAGS PSQGSPETMQ LKKEISLLNG VSLVVGNMIG
     SGIFVSPKGV LKYTASYGLS LIVWAIGGLF SVVGALCYAE LGTTITKSGA SYAYILEAFG
     GFIAFIRLWV SLLIVEPTSQ AIIAITFANY IIKPSFPTCD PPYVACRLLA AACVCLLTFV
     NCAYVKWGTR VQDTFTYAKV LALIAIIIMG LVKLCQGHTE HFQDAFKGSS WNVGDLSLAL
     YSALFSYSGW DTLNFVTEEI KNPERNLPLA IGISMPIVTL IYILTNVAYY TVLNIQDVHK
     SDAVAVTFAD QTFGMFSWTI PIAVALSCFG GLNASIFASS RLFFVGSREG HLPNLLSMIH
     IERFTPVPAL LFNCTMTLIY LVVKDVFLLI NYFSFSYWFF VGLSVVGQLY LRWKEPDWPR
     PLKLSLFFPI VFCVCSLFLV AVPLFSDTIN SLIGIGIALS GVPVYFLGVY LPESRRPLFI
     RNVLATVTRV TQKLCFCVLT ELDVTEEKNV ERKTD
//