ID   S7A13_HUMAN             Reviewed;         470 AA.
AC   Q8TCU3; Q05C37; Q08AH9; Q96N84;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   02-SEP-2026, entry version 151.
DE   RecName: Full=Solute carrier family 7 member 13;
DE   AltName: Full=Sodium-independent aspartate/glutamate transporter 1;
DE   AltName: Full=X-amino acid transporter 2;
GN   Name=SLC7A13; Synonyms=AGT1, XAT2;
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.
RC   TISSUE=Kidney;
RX   PubMed=11943479; DOI=10.1016/s0378-1119(02)00435-3;
RA   Blondeau J.-P.;
RT   "Homologues of amino acid permeases: cloning and tissue expression of XAT1
RT   and XAT2.";
RL   Gene 286:241-248(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-249.
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP   MET-249.
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).
CC   -!- FUNCTION: Associates with SLC3A1/rBAT to form a functional
CC       heterodimeric complex that transports anionic and neutral amino acids
CC       across the apical plasma membrane of renal epithelium. Preferentially
CC       mediates exchange transport, but can also operate via facilitated
CC       diffusion. May act as a major transporter for L-cystine in late
CC       proximal tubules, ensuring its reabsorption from the luminal fluid in
CC       exchange for cytosolic L-glutamate or L-aspartate.
CC       {ECO:0000250|UniProtKB:Q91WN3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cystine(out) + L-aspartate(in) = L-cystine(in) + L-
CC         aspartate(out); Xref=Rhea:RHEA:76299, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:35491; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cystine(out) = L-cystine(in); Xref=Rhea:RHEA:76303,
CC         ChEBI:CHEBI:35491; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate(in) + L-glutamate(out) = L-aspartate(out) + L-
CC         glutamate(in); Xref=Rhea:RHEA:76307, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:29991; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate(in) + L-glutamine(out) = L-aspartate(out) + L-
CC         glutamine(in); Xref=Rhea:RHEA:76311, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate(in) + L-methionine(out) = L-aspartate(out) + L-
CC         methionine(in); Xref=Rhea:RHEA:76315, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57844; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(out) + L-aspartate(in) = L-leucine(in) + L-
CC         aspartate(out); Xref=Rhea:RHEA:76319, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-valine(out) + L-aspartate(in) = L-valine(in) + L-
CC         aspartate(out); Xref=Rhea:RHEA:76323, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57762; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate(in) + L-phenylalanine(out) = L-aspartate(out) + L-
CC         phenylalanine(in); Xref=Rhea:RHEA:76327, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:58095; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosine(out) + L-aspartate(in) = L-tyrosine(in) + L-
CC         aspartate(out); Xref=Rhea:RHEA:76331, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:58315; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tryptophan(out) + L-aspartate(in) = L-tryptophan(in) + L-
CC         aspartate(out); Xref=Rhea:RHEA:76335, ChEBI:CHEBI:29991,
CC         ChEBI:CHEBI:57912; Evidence={ECO:0000250|UniProtKB:Q91WN3};
CC   -!- SUBUNIT: Disulfide-linked heterodimer composed of the catalytic light
CC       subunit SLC7A13 and the heavy subunit SLC3A1.
CC       {ECO:0000250|UniProtKB:Q91WN3}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q91WN3}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8TCU3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TCU3-2; Sequence=VSP_033067, VSP_033068, VSP_033069;
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney.
CC       {ECO:0000269|PubMed:11943479}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AJ417661; CAD10393.1; -; mRNA.
DR   EMBL; AK055815; BAB71021.1; -; mRNA.
DR   EMBL; CH471060; EAW91633.1; -; Genomic_DNA.
DR   EMBL; BC125165; AAI25166.1; -; mRNA.
DR   EMBL; BC125166; AAI25167.1; -; mRNA.
DR   EMBL; BC029436; AAH29436.1; ALT_TERM; mRNA.
DR   CCDS; CCDS34917.1; -. [Q8TCU3-1]
DR   RefSeq; NP_620172.2; NM_138817.3. [Q8TCU3-1]
DR   PDB; 8WK6; EM; 2.64 A; A/B=1-470.
DR   AlphaFoldDB; Q8TCU3; -.
DR   EMDB; EMD-37596; -.
DR   SMR; Q8TCU3; -.
DR   BioGRID; 127618; 9.
DR   FunCoup; Q8TCU3; 4.
DR   IntAct; Q8TCU3; 3.
DR   MINT; Q8TCU3; -.
DR   STRING; 9606.ENSP00000297524; -.
DR   TCDB; 2.A.3.8.24; the amino acid-polyamine-organocation (apc) family.
DR   iPTMnet; Q8TCU3; -.
DR   PhosphoSitePlus; Q8TCU3; -.
DR   BioMuta; SLC7A13; -.
DR   DMDM; 74751412; -.
DR   PaxDb; 9606-ENSP00000297524; -.
DR   PeptideAtlas; Q8TCU3; -.
DR   Antibodypedia; 54555; 4 antibodies from 4 providers.
DR   DNASU; 157724; -.
DR   Ensembl; ENST00000297524.8; ENSP00000297524.3; ENSG00000164893.9. [Q8TCU3-1]
DR   Ensembl; ENST00000419776.2; ENSP00000410982.2; ENSG00000164893.9. [Q8TCU3-2]
DR   GeneID; 157724; -.
DR   KEGG; hsa:157724; -.
DR   MANE-Select; ENST00000297524.8; ENSP00000297524.3; NM_138817.3; NP_620172.2.
DR   UCSC; uc003ydq.2; human. [Q8TCU3-1]
DR   AGR; HGNC:23092; -.
DR   ClinPGx; PA134980828; -.
DR   CTD; 157724; -.
DR   DisGeNET; 157724; -.
DR   GeneCards; SLC7A13; -.
DR   HGNC; HGNC:23092; SLC7A13.
DR   HPA; ENSG00000164893; Tissue enriched (kidney).
DR   MalaCards; SLC7A13; -.
DR   MIM; 617256; gene.
DR   OpenTargets; ENSG00000164893; -.
DR   VEuPathDB; HostDB:ENSG00000164893; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000162798; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; Q8TCU3; -.
DR   OMA; EGSNWSW; -.
DR   OrthoDB; 9477746at2759; -.
DR   PAN-GO; Q8TCU3; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q8TCU3; -.
DR   PathwayCommons; Q8TCU3; -.
DR   SignaLink; Q8TCU3; -.
DR   Agora; ENSG00000164893; -.
DR   BioGRID-ORCS; 157724; 9 hits in 1146 CRISPR screens.
DR   ChiTaRS; SLC7A13; human.
DR   GenomeRNAi; 157724; -.
DR   Pharos; Q8TCU3; Tdark.
DR   PRO; PR:Q8TCU3; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q8TCU3; protein.
DR   Bgee; ENSG00000164893; Expressed in kidney epithelium and 36 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0015810; P:aspartate transmembrane transport; IEA:Ensembl.
DR   GO; GO:0015811; P:L-cystine transport; IEA:Ensembl.
DR   GO; GO:0015813; P:L-glutamate transmembrane transport; IEA:Ensembl.
DR   FunFam; 1.20.1740.10:FF:000036; Solute carrier family 7 member 13; 1.
DR   Gene3D; 1.20.1740.10; Amino acid/polyamine transporter I; 1.
DR   InterPro; IPR002293; AA/rel_permease1.
DR   InterPro; IPR050598; AminoAcid_Transporter.
DR   PANTHER; PTHR11785; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR11785:SF238; SOLUTE CARRIER FAMILY 7 MEMBER 13; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   PDBsum; 8WK6; -.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Amino-acid transport; Antiport;
KW   Cell membrane; Disulfide bond; Membrane; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..470
FT                   /note="Solute carrier family 7 member 13"
FT                   /id="PRO_0000330725"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..45
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        46..66
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..87
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        88..108
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        109..128
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        129..149
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        150..162
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        163..183
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..206
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        207..227
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        228..240
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..287
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical; Name=8"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..336
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        337..357
FT                   /note="Helical; Name=9"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        358
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical; Name=10"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..393
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical; Name=11"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        415..421
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        422..442
FT                   /note="Helical; Name=12"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        443..470
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         221..229
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033067"
FT   VAR_SEQ         394..442
FT                   /note="VFLSFPLATIVIDVGLVVIPLVKSPNVHYVYVLLLVLSGLLFYIPLIHF ->
FT                   SLILVVQAGEAGVQWHDLGLLQPLLPGFKRFSCLSLPSSWDYRCFCHFH (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033068"
FT   VAR_SEQ         443..470
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_033069"
FT   VARIANT         249
FT                   /note="V -> M (in dbSNP:rs2976189)"
FT                   /evidence="ECO:0000269|PubMed:14702039,
FT                   ECO:0000269|PubMed:15489334"
FT                   /id="VAR_042716"
FT   VARIANT         380
FT                   /note="R -> K (in dbSNP:rs4419794)"
FT                   /id="VAR_042717"
FT   VARIANT         452
FT                   /note="M -> T (in dbSNP:rs9656982)"
FT                   /id="VAR_042718"
FT   VARIANT         470
FT                   /note="E -> K (in dbSNP:rs9693999)"
FT                   /id="VAR_042719"
FT   HELIX           17..27
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           30..32
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           34..40
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           46..73
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           77..87
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           90..120
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   STRAND          124..127
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           128..130
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           131..149
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           157..184
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           187..190
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   TURN            191..193
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           204..219
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           225..228
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   TURN            234..237
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           238..263
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           266..271
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           275..283
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           290..318
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   TURN            332..334
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           338..353
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           357..380
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   TURN            381..383
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           386..388
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   STRAND          393..396
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           397..416
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           421..440
FT                   /evidence="ECO:0007829|PDB:8WK6"
FT   HELIX           447..460
FT                   /evidence="ECO:0007829|PDB:8WK6"
SQ   SEQUENCE   470 AA;  52114 MW;  F8593B829E2050E7 CRC64;
     MDRGEKIQLK RVFGYWWGTS FLLINIIGAG IFVSPKGVLA YSCMNVGVSL CVWAGCAILA
     MTSTLCSAEI SISFPCSGAQ YYFLKRYFGS TVAFLNLWTS LFLGSGVVAG QALLLAEYSI
     QPFFPSCSVP KLPKKCLALA MLWIVGILTS RGVKEVTWLQ IASSVLKVSI LSFISLTGVV
     FLIRGKKENV ERFQNAFDAE LPDISHLIQA IFQGYFAYSG GACFTLIAGE LKKPRTTIPK
     CIFTALPLVT VVYLLVNISY LTVLTPREIL SSDAVAITWA DRAFPSLAWI MPFAISTSLF
     SNLLISIFKS SRPIYLASQE GQLPLLFNTL NSHSSPFTAV LLLVTLGSLA IILTSLIDLI
     NYIFFTGSLW SILLMIGILR RRYQEPNLSI PYKVFLSFPL ATIVIDVGLV VIPLVKSPNV
     HYVYVLLLVL SGLLFYIPLI HFKIRLAWFE KMTCYLQLLF NICLPDVSEE
//