S6A18_MOUSE
ID S6A18_MOUSE Reviewed; 615 AA.
AC O88576; O88577; O88578; O88579; O88580; O88581; Q91XG6;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Sodium-dependent neutral amino acid transporter B(0)AT3 {ECO:0000303|PubMed:19478081};
DE AltName: Full=Sodium- and chloride-dependent transporter XTRP2;
DE AltName: Full=Solute carrier family 6 member 18;
DE AltName: Full=System B(0) neutral amino acid transporter AT3;
GN Name=Slc6a18; Synonyms=Xt2 {ECO:0000303|PubMed:15121838}, Xtrp2;
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] (ISOFORMS 1; 2; 3; 4; 5 AND 6), AND TISSUE
RP SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=9932288;
RA Nash S.R., Giros B., Kingsmore S.F., Kim K.M., El-Mestikawy S., Dong Q.,
RA Fumagalli F., Seldin M.F., Caron M.G.;
RT "Cloning, gene structure, and genomic localization of an orphan transporter
RT from mouse kidney with six alternatively-spliced isoforms.";
RL Recept. Channels 6:113-128(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [3]
RP DISRUPTION PHENOTYPE.
RX PubMed=15121838; DOI=10.1128/mcb.24.10.4166-4173.2004;
RA Quan H., Athirakul K., Wetsel W.C., Torres G.E., Stevens R., Chen Y.T.,
RA Coffman T.M., Caron M.G.;
RT "Hypertension and impaired glycine handling in mice lacking the orphan
RT transporter XT2.";
RL Mol. Cell. Biol. 24:4166-4173(2004).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH CLTRN.
RX PubMed=19478081; DOI=10.1074/jbc.m109.011171;
RA Singer D., Camargo S.M., Huggel K., Romeo E., Danilczyk U., Kuba K.,
RA Chesnov S., Caron M.G., Penninger J.M., Verrey F.;
RT "Orphan transporter SLC6A18 is renal neutral amino acid transporter
RT B0AT3.";
RL J. Biol. Chem. 284:19953-19960(2009).
RN [5]
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 [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF ASP-21; GLN-25; HIS-50; TYR-72; GLY-78; LYS-90; SER-158;
RP LEU-213; ARG-225; ASN-283; ASP-287; SER-296; MET-297; ILE-456; GLY-464;
RP LEU-477; GLY-495; ASP-502 AND GLN-568.
RX PubMed=26240152; DOI=10.1074/jbc.m115.648519;
RA Fairweather S.J., Broeer A., Subramanian N., Tumer E., Cheng Q.,
RA Schmoll D., O'Mara M.L., Broeer S.;
RT "Molecular basis for the interaction of the mammalian amino acid
RT transporters B0AT1 and B0AT3 with their ancillary protein collectrin.";
RL J. Biol. Chem. 290:24308-24325(2015).
CC -!- FUNCTION: Functions as a sodium and chloride-dependent neutral amino
CC acid transporter in kidneys (PubMed:26240152, PubMed:19478081).
CC Required CLTRN for cell surface expression and for its amino acid
CC transporter activity (PubMed:26240152). {ECO:0000269|PubMed:19478081,
CC ECO:0000269|PubMed:26240152}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.79 mM for L-alanine (in the presence of CLTRN)
CC {ECO:0000269|PubMed:26240152};
CC KM=0.14 mM for L-alanine (in the presence of ACE2)
CC {ECO:0000269|PubMed:26240152};
CC KM=0.99 mM for L-glycine (in the presence of CLTRN)
CC {ECO:0000269|PubMed:26240152};
CC KM=0.27 mM for L-glycine (in the presence of ACE2)
CC {ECO:0000269|PubMed:26240152};
CC -!- SUBUNIT: Interacts with CLTRN; this interaction regulates the
CC trafficking of SLC6A18 to the cell membrane and its activity.
CC {ECO:0000269|PubMed:19478081, ECO:0000269|PubMed:26240152}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000269|PubMed:19478081}; Multi-pass membrane protein
CC {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:26240152}; Multi-pass
CC membrane protein {ECO:0000255}. Note=In kidneys localizes to the apical
CC membrane in distal segments of the proximal tubule.
CC {ECO:0000269|PubMed:19478081}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=A12;
CC IsoId=O88576-1; Sequence=Displayed;
CC Name=2; Synonyms=A11;
CC IsoId=O88576-2; Sequence=VSP_050365;
CC Name=3; Synonyms=B11;
CC IsoId=O88576-3; Sequence=VSP_050364;
CC Name=4; Synonyms=A10;
CC IsoId=O88576-4; Sequence=VSP_050366, VSP_050367;
CC Name=5; Synonyms=B9;
CC IsoId=O88576-5; Sequence=VSP_050364, VSP_050366, VSP_050367;
CC Name=6; Synonyms=A8;
CC IsoId=O88576-6; Sequence=VSP_050363, VSP_050697;
CC -!- TISSUE SPECIFICITY: Expressed predominantly in kidney.
CC {ECO:0000269|PubMed:9932288}.
CC -!- DISRUPTION PHENOTYPE: Animals lacking this protein exhibit no gross
CC abnormalities and grow to adulthood, although they do exhibit
CC hypertension. The elevated blood pressure appears to be attributable to
CC a decreased level of renal glycine. High-affinity renal reabsorption of
CC glycine is eliminated and intrarenal glycine concentration is reduced.
CC {ECO:0000269|PubMed:15121838}.
CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) (TC
CC 2.A.22) family. SLC6A18 subfamily. {ECO:0000305}.
CC -!- CAUTION: Human SLC6A18 has been shown to be an inactive protein.
CC {ECO:0000269|PubMed:26240152}.
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DR EMBL; AF075262; AAC27757.1; -; mRNA.
DR EMBL; AF075263; AAC27758.1; -; mRNA.
DR EMBL; AF075264; AAC27759.1; -; mRNA.
DR EMBL; AF075265; AAC27760.1; -; mRNA.
DR EMBL; AF075266; AAC27761.1; -; mRNA.
DR EMBL; AF075267; AAC27762.1; -; mRNA.
DR EMBL; BC010748; AAH10748.1; -; mRNA.
DR CCDS; CCDS36727.1; -. [O88576-1]
DR CCDS; CCDS49311.1; -. [O88576-3]
DR CCDS; CCDS49312.1; -. [O88576-4]
DR CCDS; CCDS88479.1; -. [O88576-5]
DR CCDS; CCDS88481.1; -. [O88576-2]
DR RefSeq; NP_001035782.1; NM_001040692.3. [O88576-1]
DR RefSeq; NP_001129559.1; NM_001136087.2. [O88576-3]
DR RefSeq; NP_001162115.1; NM_001168644.1. [O88576-4]
DR RefSeq; NP_001162116.1; NM_001168645.1. [O88576-5]
DR RefSeq; NP_001162117.1; NM_001168646.1. [O88576-2]
DR AlphaFoldDB; O88576; -.
DR SMR; O88576; -.
DR DIP; DIP-60421N; -.
DR IntAct; O88576; 1.
DR STRING; 10090.ENSMUSP00000022105; -.
DR GlyGen; O88576; 1 site.
DR iPTMnet; O88576; -.
DR PhosphoSitePlus; O88576; -.
DR jPOST; O88576; -.
DR PaxDb; O88576; -.
DR PRIDE; O88576; -.
DR ProteomicsDB; 260802; -. [O88576-1]
DR ProteomicsDB; 260803; -. [O88576-2]
DR ProteomicsDB; 260804; -. [O88576-3]
DR ProteomicsDB; 260805; -. [O88576-4]
DR ProteomicsDB; 260806; -. [O88576-5]
DR ProteomicsDB; 260807; -. [O88576-6]
DR Antibodypedia; 1938; 78 antibodies from 23 providers.
DR DNASU; 22598; -.
DR Ensembl; ENSMUST00000109679; ENSMUSP00000105301; ENSMUSG00000021612. [O88576-4]
DR Ensembl; ENSMUST00000109680; ENSMUSP00000105302; ENSMUSG00000021612. [O88576-3]
DR Ensembl; ENSMUST00000220650; ENSMUSP00000152403; ENSMUSG00000021612. [O88576-5]
DR Ensembl; ENSMUST00000222029; ENSMUSP00000152525; ENSMUSG00000021612. [O88576-1]
DR Ensembl; ENSMUST00000223026; ENSMUSP00000152516; ENSMUSG00000021612. [O88576-6]
DR Ensembl; ENSMUST00000223074; ENSMUSP00000152146; ENSMUSG00000021612. [O88576-2]
DR GeneID; 22598; -.
DR KEGG; mmu:22598; -.
DR UCSC; uc007rds.2; mouse. [O88576-1]
DR UCSC; uc007rdt.2; mouse. [O88576-2]
DR UCSC; uc007rdu.2; mouse. [O88576-3]
DR UCSC; uc007rdv.2; mouse. [O88576-4]
DR UCSC; uc007rdw.2; mouse. [O88576-5]
DR CTD; 348932; -.
DR MGI; MGI:1336892; Slc6a18.
DR VEuPathDB; HostDB:ENSMUSG00000021612; -.
DR eggNOG; KOG3659; Eukaryota.
DR GeneTree; ENSGT00940000158906; -.
DR HOGENOM; CLU_006855_7_2_1; -.
DR InParanoid; O88576; -.
DR OMA; IPIFHVE; -.
DR OrthoDB; 547281at2759; -.
DR PhylomeDB; O88576; -.
DR TreeFam; TF343812; -.
DR Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR Reactome; R-MMU-442660; Na+/Cl- dependent neurotransmitter transporters.
DR BioGRID-ORCS; 22598; 2 hits in 70 CRISPR screens.
DR ChiTaRS; Slc6a18; mouse.
DR PRO; PR:O88576; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; O88576; protein.
DR Bgee; ENSMUSG00000021612; Expressed in right kidney and 33 other tissues.
DR ExpressionAtlas; O88576; baseline and differential.
DR Genevisible; O88576; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0031526; C:brush border membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0015175; F:neutral amino acid transmembrane transporter activity; IMP:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0003333; P:amino acid transmembrane transport; IDA:MGI.
DR GO; GO:0006836; P:neurotransmitter transport; IEA:UniProtKB-KW.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GO_Central.
DR CDD; cd11517; SLC6sbd_B0AT3; 1.
DR InterPro; IPR042701; B0AT3_SLC6sbd.
DR InterPro; IPR000175; Na/ntran_symport.
DR InterPro; IPR002438; Neutral_aa_SLC6.
DR InterPro; IPR037272; SNS_sf.
DR PANTHER; PTHR11616; PTHR11616; 1.
DR Pfam; PF00209; SNF; 1.
DR PRINTS; PR00176; NANEUSMPORT.
DR PRINTS; PR01206; ORPHTRNSPORT.
DR SUPFAM; SSF161070; SSF161070; 1.
DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1.
DR PROSITE; PS00754; NA_NEUROTRAN_SYMP_2; 1.
DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Amino-acid transport; Cell membrane; Glycoprotein;
KW Membrane; Neurotransmitter transport; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..615
FT /note="Sodium-dependent neutral amino acid transporter
FT B(0)AT3"
FT /id="PRO_0000214807"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..52
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 53..73
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 74..105
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 106..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..177
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..206
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 207..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=8"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 442..462
FT /note="Helical; Name=9"
FT /evidence="ECO:0000255"
FT TOPO_DOM 463..472
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical; Name=10"
FT /evidence="ECO:0000255"
FT TOPO_DOM 494..520
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 521..541
FT /note="Helical; Name=11"
FT /evidence="ECO:0000255"
FT TOPO_DOM 542..570
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 571..591
FT /note="Helical; Name=12"
FT /evidence="ECO:0000255"
FT TOPO_DOM 592..615
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 377..444
FT /note="SASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNMEGVITPL
FT LDMGILPKGIPKEVMT -> PTWKQISGARVLGEGCARLTSRVCEASVLP (in
FT isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:9932288"
FT /id="VSP_050364"
FT VAR_SEQ 377..422
FT /note="SASGPGLAFIVFTEAVLHMPGASVWSVLFFGMLFTLGLSSMFGNME -> VL
FT LCGLCSSLGCCLPWVCPPCLGTWRVSLHHYWTWGSYPKVYPRRS (in isoform
FT 6)"
FT /evidence="ECO:0000303|PubMed:9932288"
FT /id="VSP_050363"
FT VAR_SEQ 423..615
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:9932288"
FT /id="VSP_050697"
FT VAR_SEQ 445..454
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9932288"
FT /id="VSP_050365"
FT VAR_SEQ 499..552
FT /note="FCDDIEWMTGRRPGLYWQVTWRVVSPMLLFGIFLSYIVLLIQTPPSYKAWNP
FT QY -> NIFPQERRSSTQAGCRSPVCSCPSCPHCGSLELLWLSYCPSTNRGGRLRIWKV
FT V (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9932288"
FT /id="VSP_050366"
FT VAR_SEQ 553..615
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:9932288"
FT /id="VSP_050367"
FT MUTAGEN 21
FT /note="D->N: No effect on protein abundance. Increases
FT localization to the cell membrane. Increases alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 25
FT /note="Q->D: No effect on protein abundance. Almost
FT complete loss of cell surface localization. Decreases
FT alanine uptake activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 25
FT /note="Q->V: No effect on protein abundance. Strong
FT decrease of cell surface localization. Decreases alanine
FT uptake."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 50
FT /note="H->Y: No effect on protein abundance. No effect on
FT cell surface localization. Increases alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 72
FT /note="Y->H: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 78
FT /note="G->S: No effect on protein abundance. No effect on
FT cell surface expression. Decreases alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 90
FT /note="K->T: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 158
FT /note="S->D: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 213
FT /note="L->W: No effect on protein abundance. No effect on
FT cell surface localization. Decreases alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 225
FT /note="R->T: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 283
FT /note="N->D: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 287
FT /note="D->K: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 287
FT /note="D->N: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 296
FT /note="S->R: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 297
FT /note="M->C: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 297
FT /note="M->S: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 456
FT /note="I->T: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 464
FT /note="G->N: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 477
FT /note="L->P: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 495
FT /note="G->R: No effect on protein abundance. Strong
FT decreases of cell surface localization. Decreases alanine
FT uptake activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 502
FT /note="D->N: Decreases protein abundance. Strong decreases
FT of cell surface localization. Strong decreases on alanine
FT uptake activity."
FT /evidence="ECO:0000269|PubMed:26240152"
FT MUTAGEN 568
FT /note="Q->R: No effect on protein abundance. No effect on
FT cell surface localization. No effect on alanine uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:26240152"
SQ SEQUENCE 615 AA; 69229 MW; A7925C0397FC63F8 CRC64;
MAQASGMDPL VDIEDERPKW DNKLQYLLSC IGFAVGLGNI WRFPYLCQTH GGGAFLIPYF
IALVFEGIPL FYIELAIGQR LRRGSIGVWK TISPYLGGVG LGCFSVSFLV SLYYNTVLLW
VLWFFLNSFQ HPLPWSTCPL DLNRTGFVQE CQSSGTVSYF WYRQTLNITS DISNTGTIQW
KLFLCLVACW STVYLCVIRG IESTGKVIYF TALFPYLVLT IFLIRGLTLP GATEGLIYLF
TPNMKTLQNP RVWLDAATQI FFSLSLAFGG HIAFASYNPP RNNCEKDAVI IALVNSMTSL
YASIAIFSVM GFKASNDYGR CLDRNILSLI NEFDLPELSI SRDEYPSVLM YLNATQTARV
AQLPLKTCHL EDFLDKSASG PGLAFIVFTE AVLHMPGASV WSVLFFGMLF TLGLSSMFGN
MEGVITPLLD MGILPKGIPK EVMTGVICFA CFLSAICFTL QSGGYWLEIF DSFAASLNLI
IFAFMEVVGV IHIYGMKRFC DDIEWMTGRR PGLYWQVTWR VVSPMLLFGI FLSYIVLLIQ
TPPSYKAWNP QYEHFPSREE KFYPGWVQVT CVLLSFLPSL WVPGVALAQL LSQYKQRWKA
THLESGLKLQ ESRGC
