ID   AAA1_MOUSE              Reviewed;         530 AA.
AC   P63115; Q9CW25; Q9JMH8;
DT   13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 138.
DE   RecName: Full=Asc-type amino acid transporter 1;
DE            Short=Asc-1 {ECO:0000303|PubMed:25755256};
DE   AltName: Full=D-serine transporter;
DE   AltName: Full=Solute carrier family 7 member 10;
GN   Name=Slc7a10; Synonyms=Asc1;
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], FUNCTION, TRANSPORT ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=10734121; DOI=10.1074/jbc.275.13.9690;
RA   Fukasawa Y., Segawa H., Kim J.Y., Chairoungdua A., Kim D.K., Matsuo H.,
RA   Cha S.H., Endou H., Kanai Y.;
RT   "Identification and characterization of a Na+-independent neutral amino
RT   acid transporter that associates with the 4F2 heavy chain and exhibits
RT   substrate selectivity for small neutral D- and L- amino acids.";
RL   J. Biol. Chem. 275:9690-9698(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 170-530.
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
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   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=25755256; DOI=10.15252/embr.201439561;
RA   Safory H., Neame S., Shulman Y., Zubedat S., Radzishevsky I., Rosenberg D.,
RA   Sason H., Engelender S., Avital A., Huelsmann S., Schiller J., Wolosker H.;
RT   "The alanine-serine-cysteine-1 (Asc-1) transporter controls glycine levels
RT   in the brain and is required for glycinergic inhibitory transmission.";
RL   EMBO Rep. 16:590-598(2015).
RN   [5]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=27759100; DOI=10.1038/srep35592;
RA   Ehmsen J.T., Liu Y., Wang Y., Paladugu N., Johnson A.E., Rothstein J.D.,
RA   du Lac S., Mattson M.P., Hoeke A.;
RT   "The astrocytic transporter SLC7A10 (Asc-1) mediates glycinergic inhibition
RT   of spinal cord motor neurons.";
RL   Sci. Rep. 6:35592-35592(2016).
RN   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=34749773; DOI=10.1186/s13041-021-00874-8;
RA   Tatsumi K., Kinugawa K., Isonishi A., Kitabatake M., Okuda H., Takemura S.,
RA   Tanaka T., Mori E., Wanaka A.;
RT   "Olig2-astrocytes express neutral amino acid transporter SLC7A10 (Asc-1) in
RT   the adult brain.";
RL   Mol. Brain 14:163-163(2021).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=33707431; DOI=10.1038/s41467-021-21826-9;
RA   Suwandhi L., Altun I., Karlina R., Miok V., Wiedemann T., Fischer D.,
RA   Walzthoeni T., Lindner C., Boettcher A., Heinzmann S.S., Israel A.,
RA   Khalil A.E.M.M., Braun A., Pramme-Steinwachs I., Burtscher I.,
RA   Schmitt-Kopplin P., Heinig M., Elsner M., Lickert H., Theis F.J., Ussar S.;
RT   "Asc-1 regulates white versus beige adipocyte fate in a subcutaneous
RT   stromal cell population.";
RL   Nat. Commun. 12:1588-1588(2021).
CC   -!- FUNCTION: Associates with SLC3A2/4F2hc to form a functional
CC       heterodimeric complex that translocates small neutral L- and D-amino
CC       acids across the plasma membrane. Preferentially mediates exchange
CC       transport, but can also operate via facilitated diffusion
CC       (PubMed:10734121) (By similarity). Acts as a major transporter for
CC       glycine, L- and D-serine in the central nervous system. At the spinal
CC       cord and brainstem regulates glycine metabolism and glycinergic
CC       inhibitory neurotransmission by providing for glycine de novo synthesis
CC       from L-serine and glycine recycling from astrocytes to glycinergic
CC       motor neurons (PubMed:25755256, PubMed:27759100). At Schaffer
CC       collateral-CA1 synapses mediates D-serine and glycine release that
CC       modulates post-synaptic activation of NMDA receptors and excitatory
CC       glutamatergic transmission (By similarity). May regulate D-serine
CC       release from mesenchymal progenitors located in developing subcutaneous
CC       adipose tissue, favoring white adipocyte over thermogenic beige
CC       adipocyte lineage commitment (PubMed:33707431).
CC       {ECO:0000250|UniProtKB:P63116, ECO:0000269|PubMed:10734121,
CC       ECO:0000269|PubMed:25755256, ECO:0000269|PubMed:27759100,
CC       ECO:0000269|PubMed:33707431}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycine(out) + L-alanine(in) = glycine(in) + L-alanine(out);
CC         Xref=Rhea:RHEA:74019, ChEBI:CHEBI:57305, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-serine(out) = L-alanine(out) + L-serine(in);
CC         Xref=Rhea:RHEA:74023, ChEBI:CHEBI:33384, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-threonine(out) = L-alanine(out) + L-
CC         threonine(in); Xref=Rhea:RHEA:74027, ChEBI:CHEBI:57926,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-cysteine(out) = L-alanine(out) + L-
CC         cysteine(in); Xref=Rhea:RHEA:74031, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-aminoisobutanoate(out) + L-alanine(in) = 2-
CC         aminoisobutanoate(in) + L-alanine(out); Xref=Rhea:RHEA:74063,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:193090;
CC         Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(out) + L-alanine(in) = D-serine(in) + L-alanine(out);
CC         Xref=Rhea:RHEA:74035, ChEBI:CHEBI:35247, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-alanine(out) + L-alanine(in) = D-alanine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74039, ChEBI:CHEBI:57416,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-valine(out) = L-alanine(out) + L-valine(in);
CC         Xref=Rhea:RHEA:74047, ChEBI:CHEBI:57762, ChEBI:CHEBI:57972;
CC         Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) + L-methionine(out) = L-alanine(out) + L-
CC         methionine(in); Xref=Rhea:RHEA:74043, ChEBI:CHEBI:57844,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-alanine(out) + L-alanine(in) = beta-alanine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74059, ChEBI:CHEBI:57966,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-cysteine(out) + L-alanine(in) = D-cysteine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74055, ChEBI:CHEBI:35236,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-threonine(out) + L-alanine(in) = D-threonine(in) + L-
CC         alanine(out); Xref=Rhea:RHEA:74051, ChEBI:CHEBI:57757,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000269|PubMed:10734121};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-isoleucine(out) + D-serine(in) = D-isoleucine(in) + D-
CC         serine(out); Xref=Rhea:RHEA:74299, ChEBI:CHEBI:35247,
CC         ChEBI:CHEBI:193151; Evidence={ECO:0000250|UniProtKB:P63116};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:74300;
CC         Evidence={ECO:0000250|UniProtKB:P63116};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-serine(in) = D-serine(out); Xref=Rhea:RHEA:29455,
CC         ChEBI:CHEBI:35247; Evidence={ECO:0000250|UniProtKB:P63116};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23 uM for L-alanine {ECO:0000269|PubMed:10734121};
CC         KM=7.8 uM for glycine {ECO:0000269|PubMed:10734121};
CC         KM=11.3 uM for L-serine {ECO:0000269|PubMed:10734121};
CC         KM=19.3 uM for L-threonine {ECO:0000269|PubMed:10734121};
CC         KM=23.7 uM for L-cysteine {ECO:0000269|PubMed:10734121};
CC         KM=112 uM for L-valine {ECO:0000269|PubMed:10734121};
CC         KM=139 uM for L-methionine {ECO:0000269|PubMed:10734121};
CC         KM=160 uM for L-isoleucine {ECO:0000269|PubMed:10734121};
CC         KM=245 uM for L-leucine {ECO:0000269|PubMed:10734121};
CC         KM=368 uM for L-histidine {ECO:0000269|PubMed:10734121};
CC         KM=464 uM for L-phenylalanine {ECO:0000269|PubMed:10734121};
CC         KM=22.7 uM for 2-aminoisobutanoate {ECO:0000269|PubMed:10734121};
CC         KM=100 uM for D-alanine {ECO:0000269|PubMed:10734121};
CC         KM=52 uM for D-serine {ECO:0000269|PubMed:10734121};
CC         KM=281 uM for beta-alanine {ECO:0000269|PubMed:10734121};
CC       pH dependence:
CC         Active from pH 5.5 to 8.5. {ECO:0000269|PubMed:10734121};
CC   -!- SUBUNIT: Disulfide-linked heterodimer with the amino acid transport
CC       protein SLC3A2/4F2hc. {ECO:0000269|PubMed:10734121}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:33707431,
CC       ECO:0000269|PubMed:34749773}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Colocalizes with OLIG2 in astrocytic processes
CC       (PubMed:34749773). Localizes to the plasma membrane in mature
CC       adipocytes and to intracellular structures in preadipocytes
CC       (PubMed:33707431). {ECO:0000269|PubMed:33707431,
CC       ECO:0000269|PubMed:34749773}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain and lung, and to a lesser
CC       extent in placenta and small intestine (PubMed:10734121). Expressed in
CC       a subpopulation of astrocytes enriched at glycinergic synapses in the
CC       spinal cord and brainstem (at protein level). Expressed in OLIG2-
CC       positive astrocytes of the lateral globus pallidus (at protein level)
CC       (PubMed:27759100, PubMed:34749773). Expressed in CD34-positive, DPP4-
CC       positive mesenchymal progenitors in developing subcutaneous adipose
CC       tissue (PubMed:33707431). {ECO:0000269|PubMed:10734121,
CC       ECO:0000269|PubMed:27759100, ECO:0000269|PubMed:33707431,
CC       ECO:0000269|PubMed:34749773}.
CC   -!- INDUCTION: Up-regulated upon adipocyte differentiation in response to
CC       INS. Down-regulated by treatment with rosiglitazone.
CC       {ECO:0000269|PubMed:33707431}.
CC   -!- DISRUPTION PHENOTYPE: Mutant mice develop hyperekplexia-like phenotype
CC       due to impaired glycinergic inhibitory transmission. Administration of
CC       glycine and L-serine reverses the phenotype.
CC       {ECO:0000269|PubMed:25755256}.
CC   -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC       superfamily. {ECO:0000305}.
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DR   EMBL; AB026688; BAA93617.1; -; mRNA.
DR   EMBL; BC054765; AAH54765.1; -; mRNA.
DR   EMBL; AK005282; BAB23930.1; -; mRNA.
DR   CCDS; CCDS21146.1; -.
DR   RefSeq; NP_059090.3; NM_017394.4.
DR   AlphaFoldDB; P63115; -.
DR   SMR; P63115; -.
DR   STRING; 10090.ENSMUSP00000001854; -.
DR   TCDB; 2.A.3.8.13; the amino acid-polyamine-organocation (apc) family.
DR   iPTMnet; P63115; -.
DR   PhosphoSitePlus; P63115; -.
DR   SwissPalm; P63115; -.
DR   jPOST; P63115; -.
DR   MaxQB; P63115; -.
DR   PaxDb; 10090-ENSMUSP00000001854; -.
DR   ProteomicsDB; 296429; -.
DR   Antibodypedia; 47948; 110 antibodies from 20 providers.
DR   DNASU; 53896; -.
DR   Ensembl; ENSMUST00000001854.12; ENSMUSP00000001854.6; ENSMUSG00000030495.13.
DR   GeneID; 53896; -.
DR   KEGG; mmu:53896; -.
DR   UCSC; uc009gjn.2; mouse.
DR   AGR; MGI:1858261; -.
DR   CTD; 56301; -.
DR   MGI; MGI:1858261; Slc7a10.
DR   VEuPathDB; HostDB:ENSMUSG00000030495; -.
DR   eggNOG; KOG1287; Eukaryota.
DR   GeneTree; ENSGT00940000156469; -.
DR   HOGENOM; CLU_007946_3_0_1; -.
DR   InParanoid; P63115; -.
DR   OMA; PWRDVVP; -.
DR   OrthoDB; 1103451at2759; -.
DR   PhylomeDB; P63115; -.
DR   TreeFam; TF313355; -.
DR   Reactome; R-MMU-352230; Amino acid transport across the plasma membrane.
DR   BioGRID-ORCS; 53896; 3 hits in 77 CRISPR screens.
DR   PRO; PR:P63115; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P63115; Protein.
DR   Bgee; ENSMUSG00000030495; Expressed in lumbar subsegment of spinal cord and 138 other cell types or tissues.
DR   ExpressionAtlas; P63115; baseline and differential.
DR   GO; GO:0097440; C:apical dendrite; ISO:MGI.
DR   GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0015175; F:neutral L-amino acid transmembrane transporter activity; IDA:UniProtKB.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0042941; P:D-alanine transport; IMP:MGI.
DR   GO; GO:0042942; P:D-serine transport; IMP:UniProtKB.
DR   GO; GO:0015816; P:glycine transport; IDA:UniProtKB.
DR   GO; GO:1903444; P:negative regulation of brown fat cell differentiation; IMP:UniProtKB.
DR   GO; GO:0015804; P:neutral amino acid transport; IDA:UniProtKB.
DR   GO; GO:0060094; P:positive regulation of synaptic transmission, glycinergic; IMP:UniProtKB.
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:SF73; ASC-TYPE AMINO ACID TRANSPORTER 1; 1.
DR   Pfam; PF13520; AA_permease_2; 1.
DR   PIRSF; PIRSF006060; AA_transporter; 1.
DR   Genevisible; P63115; MM.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Disulfide bond; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..530
FT                   /note="Asc-type amino acid transporter 1"
FT                   /id="PRO_0000054277"
FT   TRANSMEM        46..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        78..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        192..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        430..450
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..530
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..33
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   530 AA;  57549 MW;  0C5A80BF922DB54D CRC64;
     MRRDSDMASH IQQPGGHGNP GPAPSPSPGP GPGPGASERV ALKKEIGLVS ACTIIIGNII
     GSGIFISPKG VLEHSGSVGL ALFVWVLGGG VTALGSLCYA ELGVAIPKSG GDYAYVTEIF
     GGLAGFLLLW SAVLIMYPTS LAVISMTFSN YVLQPVFPNC IPPATASRVL SMACLMLLTW
     VNSSSVRWAT RIQVIFTGGK LLALSLIITV GFVQIFQGHF EELRPTNAFA FWMTPSVGHL
     ALAFLQGSFA FSGWNFLNYV TEELVDPRKN LPRAIFISIP LVTFVYTFTN VAYFTAMSPQ
     ELLSSNAVAV TFGEKLLGYF SWVMPVSVAL STFGGINGYL FTSSRLCFSG AREGHLPSFL
     AMIHVRRCTP IPALLVCCGA TAVIMLVGDT YTLINYVSFI NYLCYGVTIL GLLVLRWRRP
     ALHRPIKVNL LVPVVYLVFW AFLLVFSFIS EPMVCGVGII IILTGVPIFF LGVFWRSKPK
     CVHRFTESMT RWGQELCFVV YPQGSLEEEE NGPMGQPSPL PITDKPLKTQ
//