ID   S38AA_HUMAN             Reviewed;        1119 AA.
AC   Q9HBR0; Q6ZRC5; Q8NA99; Q96C66;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Solute carrier family 38 member 10 {ECO:0000250|UniProtKB:Q5I012};
DE   AltName: Full=Amino acid transporter SLC38A10 {ECO:0000250|UniProtKB:Q5I012};
GN   Name=SLC38A10 {ECO:0000250|UniProtKB:Q5I012,
GN   ECO:0000312|HGNC:HGNC:28237}; ORFNames=PP1744;
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 [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 209-1119 (ISOFORM 2).
RC   TISSUE=Thymus;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16625196; DOI=10.1038/nature04689;
RA   Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA   Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA   Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA   Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA   DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA   Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA   Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA   LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA   Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA   Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA   Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA   Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA   Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT   "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT   human lineage.";
RL   Nature 440:1045-1049(2006).
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] (ISOFORM 2).
RC   TISSUE=Muscle;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 784-1119, AND VARIANT GLY-831.
RX   PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA   Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA   Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA   Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT   "Large-scale cDNA transfection screening for genes related to cancer
RT   development and progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-772; SER-802; SER-965 AND
RP   SER-997, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: Facilitates bidirectional transport of amino acids. May act
CC       as a glutamate sensor that regulates glutamate-glutamine cycle and mTOR
CC       signaling in the brain. The transport mechanism remains to be
CC       elucidated. {ECO:0000250|UniProtKB:Q5I012}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC         ChEBI:CHEBI:29985; Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66337;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:66338;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-glutamine(out) = L-glutamine(in); Xref=Rhea:RHEA:73419,
CC         ChEBI:CHEBI:58359; Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:73420;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73421;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-alanine(in) = L-alanine(out); Xref=Rhea:RHEA:70719,
CC         ChEBI:CHEBI:57972; Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70720;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:70721;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-serine(in) = L-serine(out); Xref=Rhea:RHEA:35031,
CC         ChEBI:CHEBI:33384; Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35032;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-leucine(in) = L-leucine(out); Xref=Rhea:RHEA:73011,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000250|UniProtKB:Q5I012};
CC       PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:73013;
CC         Evidence={ECO:0000250|UniProtKB:Q5I012};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q9HBR0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9HBR0-2; Sequence=VSP_031324, VSP_031327;
CC       Name=3;
CC         IsoId=Q9HBR0-3; Sequence=VSP_031323, VSP_031325, VSP_031326;
CC   -!- SIMILARITY: Belongs to the amino acid/polyamine transporter 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAG17235.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAC04027.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AK093037; BAC04027.1; ALT_INIT; mRNA.
DR   EMBL; AK128330; BAC87387.1; -; mRNA.
DR   EMBL; AC027601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471099; EAW89643.1; -; Genomic_DNA.
DR   EMBL; BC014642; AAH14642.1; -; mRNA.
DR   EMBL; AF217993; AAG17235.1; ALT_INIT; mRNA.
DR   CCDS; CCDS11780.1; -. [Q9HBR0-2]
DR   CCDS; CCDS42397.1; -. [Q9HBR0-1]
DR   RefSeq; NP_001033073.1; NM_001037984.2. [Q9HBR0-1]
DR   RefSeq; NP_612637.1; NM_138570.3. [Q9HBR0-2]
DR   AlphaFoldDB; Q9HBR0; -.
DR   SMR; Q9HBR0; -.
DR   BioGRID; 125874; 108.
DR   IntAct; Q9HBR0; 17.
DR   MINT; Q9HBR0; -.
DR   STRING; 9606.ENSP00000363891; -.
DR   TCDB; 2.A.18.6.16; the amino acid/auxin permease (aaap) family.
DR   GlyCosmos; Q9HBR0; 3 sites, 1 glycan.
DR   GlyGen; Q9HBR0; 17 sites, 2 O-linked glycans (17 sites).
DR   iPTMnet; Q9HBR0; -.
DR   PhosphoSitePlus; Q9HBR0; -.
DR   SwissPalm; Q9HBR0; -.
DR   BioMuta; SLC38A10; -.
DR   DMDM; 172045932; -.
DR   EPD; Q9HBR0; -.
DR   jPOST; Q9HBR0; -.
DR   MassIVE; Q9HBR0; -.
DR   MaxQB; Q9HBR0; -.
DR   PaxDb; 9606-ENSP00000363891; -.
DR   PeptideAtlas; Q9HBR0; -.
DR   ProteomicsDB; 81585; -. [Q9HBR0-1]
DR   ProteomicsDB; 81586; -. [Q9HBR0-2]
DR   ProteomicsDB; 81587; -. [Q9HBR0-3]
DR   Pumba; Q9HBR0; -.
DR   Antibodypedia; 19805; 51 antibodies from 10 providers.
DR   DNASU; 124565; -.
DR   Ensembl; ENST00000288439.9; ENSP00000288439.5; ENSG00000157637.13. [Q9HBR0-2]
DR   Ensembl; ENST00000374759.8; ENSP00000363891.3; ENSG00000157637.13. [Q9HBR0-1]
DR   GeneID; 124565; -.
DR   KEGG; hsa:124565; -.
DR   MANE-Select; ENST00000374759.8; ENSP00000363891.3; NM_001037984.3; NP_001033073.1.
DR   UCSC; uc002jzz.3; human. [Q9HBR0-1]
DR   AGR; HGNC:28237; -.
DR   CTD; 124565; -.
DR   DisGeNET; 124565; -.
DR   GeneCards; SLC38A10; -.
DR   HGNC; HGNC:28237; SLC38A10.
DR   HPA; ENSG00000157637; Low tissue specificity.
DR   MIM; 616525; gene.
DR   neXtProt; NX_Q9HBR0; -.
DR   OpenTargets; ENSG00000157637; -.
DR   PharmGKB; PA162403738; -.
DR   VEuPathDB; HostDB:ENSG00000157637; -.
DR   eggNOG; KOG1305; Eukaryota.
DR   GeneTree; ENSGT00940000159369; -.
DR   HOGENOM; CLU_009020_6_0_1; -.
DR   InParanoid; Q9HBR0; -.
DR   OMA; KCRCGRC; -.
DR   OrthoDB; 5405468at2759; -.
DR   PhylomeDB; Q9HBR0; -.
DR   TreeFam; TF320116; -.
DR   PathwayCommons; Q9HBR0; -.
DR   SignaLink; Q9HBR0; -.
DR   BioGRID-ORCS; 124565; 31 hits in 1159 CRISPR screens.
DR   ChiTaRS; SLC38A10; human.
DR   GeneWiki; SLC38A10; -.
DR   GenomeRNAi; 124565; -.
DR   Pharos; Q9HBR0; Tdark.
DR   PRO; PR:Q9HBR0; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q9HBR0; Protein.
DR   Bgee; ENSG00000157637; Expressed in adenohypophysis and 177 other cell types or tissues.
DR   ExpressionAtlas; Q9HBR0; baseline and differential.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0003333; P:amino acid transmembrane transport; IBA:GO_Central.
DR   GO; GO:0060348; P:bone development; IEA:Ensembl.
DR   InterPro; IPR013057; AA_transpt_TM.
DR   PANTHER; PTHR22950; AMINO ACID TRANSPORTER; 1.
DR   PANTHER; PTHR22950:SF646; SODIUM-COUPLED NEUTRAL AMINO ACID TRANSPORTER 10-RELATED; 1.
DR   Pfam; PF01490; Aa_trans; 1.
DR   Genevisible; Q9HBR0; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Amino-acid transport; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..1119
FT                   /note="Solute carrier family 38 member 10"
FT                   /id="PRO_0000318975"
FT   TRANSMEM        4..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        120..140
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        345..365
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        378..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          438..691
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          731..1071
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        438..458
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        465..479
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..525
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        654..668
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        731..750
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..1020
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1035..1061
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         612
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q5I012"
FT   MOD_RES         772
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         802
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         889
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:E9PT23"
FT   MOD_RES         965
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         997
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   VAR_SEQ         1..82
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031323"
FT   VAR_SEQ         689..780
FT                   /note="EAGRAEMLDHAVLLQVIKEQQVQQKRLLDQQEKLLAVIEEQHKEIHQQRQED
FT                   EEDKPRQVEVHQEPGAAVPRGQEAPEGKARETVENLPPLP -> GKASALQPPASGPGS
FT                   GSPLPQPWGDAQVILGSPARPPFSFQPPAEQTPRRAFCSLPISSLLSGNLLSALLPFKH
FT                   LRHRHMACDYRFISLAPL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031324"
FT   VAR_SEQ         768
FT                   /note="K -> S (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031325"
FT   VAR_SEQ         769..1119
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_031326"
FT   VAR_SEQ         781..1119
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_031327"
FT   VARIANT         559
FT                   /note="K -> R (in dbSNP:rs35546507)"
FT                   /id="VAR_048126"
FT   VARIANT         831
FT                   /note="A -> G (in dbSNP:rs2725405)"
FT                   /evidence="ECO:0000269|PubMed:15498874"
FT                   /id="VAR_038927"
FT   CONFLICT        1071
FT                   /note="Missing (in Ref. 5; AAG17235)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1119 AA;  119762 MW;  F328CFEB6A5336D9 CRC64;
     MTAAAASNWG LITNIVNSIV GVSVLTMPFC FKQCGIVLGA LLLVFCSWMT HQSCMFLVKS
     ASLSKRRTYA GLAFHAYGKA GKMLVETSMI GLMLGTCIAF YVVIGDLGSN FFARLFGFQV
     GGTFRMFLLF AVSLCIVLPL SLQRNMMASI QSFSAMALLF YTVFMFVIVL SSLKHGLFSG
     QWLRRVSYVR WEGVFRCIPI FGMSFACQSQ VLPTYDSLDE PSVKTMSSIF ASSLNVVTTF
     YVMVGFFGYV SFTEATAGNV LMHFPSNLVT EMLRVGFMMS VAVGFPMMIL PCRQALSTLL
     CEQQQKDGTF AAGGYMPPLR FKALTLSVVF GTMVGGILIP NVETILGLTG ATMGSLICFI
     CPALIYKKIH KNALSSQVVL WVGLGVLVVS TVTTLSVSEE VPEDLAEEAP GGRLGEAEGL
     MKVEAARLSA QDPVVAVAED GREKPKLPKE REELEQAQIK GPVDVPGRED GKEAPEEAQL
     DRPGQGIAVP VGEAHRHEPP VPHDKVVVDE GQDREVPEEN KPPSRHAGGK APGVQGQMAP
     PLPDSEREKQ EPEQGEVGKR PGQAQALEEA GDLPEDPQKV PEADGQPAVQ PAKEDLGPGD
     RGLHPRPQAV LSEQQNGLAV GGGEKAKGGP PPGNAAGDTG QPAEDSDHGG KPPLPAEKPA
     PGPGLPPEPR EQRDVERAGG NQAASQLEEA GRAEMLDHAV LLQVIKEQQV QQKRLLDQQE
     KLLAVIEEQH KEIHQQRQED EEDKPRQVEV HQEPGAAVPR GQEAPEGKAR ETVENLPPLP
     LDPVLRAPGG RPAPSQDLNQ RSLEHSEGPV GRDPAGPPDG GPDTEPRAAQ AKLRDGQKDA
     APRAAGTVKE LPKGPEQVPV PDPAREAGGP EERLAEEFPG QSQDVTGGSQ DRKKPGKEVA
     ATGTSILKEA NWLVAGPGAE TGDPRMKPKQ VSRDLGLAAD LPGGAEGAAA QPQAVLRQPE
     LRVISDGEQG GQQGHRLDHG GHLEMRKARG GDHVPVSHEQ PRGGEDAAVQ EPRQRPEPEL
     GLKRAVPGGQ RPDNAKPNRD LKLQAGSDLR RRRRDLGPHA EGQLAPRDGV IIGLNPLPDV
     QVNDLRGALD AQLRQAAGGA LQVVHSRQLR QAPGPPEES
//