ID   S28A2_HUMAN             Reviewed;         658 AA.
AC   O43868; A8K7F9; O43239; Q52LZ0;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 2.
DT   27-MAR-2024, entry version 185.
DE   RecName: Full=Sodium/nucleoside cotransporter 2;
DE   AltName: Full=Concentrative nucleoside transporter 2;
DE            Short=CNT 2;
DE            Short=hCNT2;
DE   AltName: Full=Na(+)/nucleoside cotransporter 2;
DE   AltName: Full=Sodium-coupled nucleoside transporter 2;
DE   AltName: Full=Sodium/purine nucleoside co-transporter {ECO:0000303|PubMed:9435697};
DE            Short=SPNT {ECO:0000303|PubMed:9435697};
DE   AltName: Full=Solute carrier family 28 member 2;
GN   Name=SLC28A2; Synonyms=CNT2;
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], FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY
RP   REGULATION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=9435697; DOI=10.1152/ajprenal.1997.273.6.f1058;
RA   Wang J., Su S.-F., Dresser M.J., Schaner M.E., Washington C.B.,
RA   Giacomini K.M.;
RT   "Na+-dependent purine nucleoside transporter from human kidney: cloning and
RT   functional characterization.";
RL   Am. J. Physiol. 273:F1058-F1065(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, AND VARIANT
RP   ARG-75.
RC   TISSUE=Small intestine;
RX   PubMed=10087507; DOI=10.3109/09687689709044322;
RA   Ritzel M.W.L., Yao S.Y.M., Ng A.M.L., Mackey J.R., Cass C.E., Young J.D.;
RT   "Molecular cloning, functional expression and chromosomal localization of a
RT   cDNA encoding a human Na+/nucleoside cotransporter (hCNT2) selective for
RT   purine nucleosides and uridine.";
RL   Mol. Membr. Biol. 15:203-211(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Small intestine;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Colon;
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   MUTAGENESIS.
RX   PubMed=10455109; DOI=10.1074/jbc.274.35.24475;
RA   Loewen S.K., Ng A.M.L., Yao S.Y.M., Cass C.E., Baldwin S.A., Young J.D.;
RT   "Identification of amino acid residues responsible for the pyrimidine and
RT   purine nucleoside specificities of human concentrative Na(+) nucleoside
RT   cotransporters hCNT1 and hCNT2.";
RL   J. Biol. Chem. 274:24475-24484(1999).
RN   [6]
RP   FUNCTION, AND TRANSPORTER ACTIVITY.
RX   PubMed=21795683; DOI=10.1074/jbc.m111.236117;
RA   Yao S.Y., Ng A.M., Cass C.E., Baldwin S.A., Young J.D.;
RT   "Nucleobase transport by human equilibrative nucleoside transporter 1
RT   (hENT1).";
RL   J. Biol. Chem. 286:32552-32562(2011).
RN   [7]
RP   FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=35307651; DOI=10.1124/dmd.121.000748;
RA   Hau R.K., Klein R.R., Wright S.H., Cherrington N.J.;
RT   "Localization of Xenobiotic Transporters Expressed at the Human Blood-
RT   Testis Barrier.";
RL   Drug Metab. Dispos. 50:770-780(2022).
RN   [8]
RP   VARIANTS LEU-22; ARG-75; TRP-163; THR-245; SER-355 AND PHE-462.
RX   PubMed=15861032; DOI=10.1097/01213011-200502000-00004;
RA   Owen R.P., Gray J.H., Taylor T.R., Carlson E.J., Huang C.C., Kawamoto M.,
RA   Johns S.J., Stryke D., Ferrin T.E., Giacomini K.M.;
RT   "Genetic analysis and functional characterization of polymorphisms in the
RT   human concentrative nucleoside transporter, CNT2.";
RL   Pharmacogenet. Genomics 15:83-90(2005).
RN   [9]
RP   VARIANTS PRO-12; LEU-22; ARG-75; HIS-142; TRP-163; ASP-172; LYS-385 AND
RP   THR-612.
RX   PubMed=17700367; DOI=10.1097/fpc.0b013e3281c10e41;
RA   Li L., Tan C.M.F., Koo S.H., Chong K.T., Lee E.J.D.;
RT   "Identification and functional analysis of variants in the human
RT   concentrative nucleoside transporter 2, hCNT2 (SLC28A2) in Chinese, Malays
RT   and Indians.";
RL   Pharmacogenet. Genomics 17:783-786(2007).
CC   -!- FUNCTION: Sodium-dependent and purine-selective transporter
CC       (PubMed:9435697, PubMed:10087507). Exhibits the transport
CC       characteristics of the nucleoside transport system cif or N1 subtype
CC       (N1/cif) (selective for purine nucleosides and uridine)
CC       (PubMed:9435697, PubMed:10087507, PubMed:21795683). Plays a critical
CC       role in specific uptake and salvage of purine nucleosides in kidney and
CC       other tissues (PubMed:9435697). May contribute to regulate the
CC       transport of organic compounds in testes across the blood-testis-
CC       barrier (Probable). {ECO:0000269|PubMed:10087507,
CC       ECO:0000269|PubMed:21795683, ECO:0000269|PubMed:9435697,
CC       ECO:0000305|PubMed:35307651}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine(out) + Na(+)(out) = adenosine(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:69927, ChEBI:CHEBI:16335, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:10087507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=inosine(out) + Na(+)(out) = inosine(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:69931, ChEBI:CHEBI:17596, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:10087507, ECO:0000269|PubMed:9435697};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(out) + Na(+)(out) = guanosine(in) + Na(+)(in);
CC         Xref=Rhea:RHEA:69935, ChEBI:CHEBI:16750, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:10087507};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Na(+)(out) + uridine(out) = Na(+)(in) + uridine(in);
CC         Xref=Rhea:RHEA:69887, ChEBI:CHEBI:16704, ChEBI:CHEBI:29101;
CC         Evidence={ECO:0000269|PubMed:10087507, ECO:0000269|PubMed:21795683,
CC         ECO:0000269|PubMed:9435697};
CC   -!- ACTIVITY REGULATION: Inhibited by formycin B.
CC       {ECO:0000269|PubMed:9435697}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305|PubMed:9435697}; Multi-pass
CC       membrane protein {ECO:0000255}. Apicolateral cell membrane
CC       {ECO:0000269|PubMed:35307651}; Multi-pass membrane protein
CC       {ECO:0000255}. Note=Localized to the apicolateral membranes of Sertoli
CC       cells and vascular endothelial cells in testis.
CC       {ECO:0000269|PubMed:35307651}.
CC   -!- TISSUE SPECIFICITY: Expressed in heart and skeletal muscle followed by
CC       liver, kidney, intestine, pancreas, placenta and brain
CC       (PubMed:9435697). Weak expression in lung (PubMed:9435697). In testis,
CC       primarily localized to the apicolateral membranes of Sertoli cells and
CC       vascular endothelial cells, and weakly expressed in Leydig cells,
CC       peritubular myoid cells and germ cells (PubMed:35307651).
CC       {ECO:0000269|PubMed:35307651, ECO:0000269|PubMed:9435697}.
CC   -!- SIMILARITY: Belongs to the concentrative nucleoside transporter (CNT)
CC       (TC 2.A.41) family. {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; U84392; AAC51930.1; -; mRNA.
DR   EMBL; AF036109; AAB88539.1; -; mRNA.
DR   EMBL; AK291974; BAF84663.1; -; mRNA.
DR   EMBL; BC093737; AAH93737.1; -; mRNA.
DR   CCDS; CCDS10121.1; -.
DR   RefSeq; NP_004203.2; NM_004212.3.
DR   RefSeq; XP_011520500.1; XM_011522198.2.
DR   AlphaFoldDB; O43868; -.
DR   SMR; O43868; -.
DR   BioGRID; 114600; 16.
DR   STRING; 9606.ENSP00000315006; -.
DR   BindingDB; O43868; -.
DR   ChEMBL; CHEMBL5780; -.
DR   DrugBank; DB00640; Adenosine.
DR   DrugBank; DB01033; Mercaptopurine.
DR   DrugBank; DB09327; Tegafur-uracil.
DR   GuidetoPHARMACOLOGY; 1115; -.
DR   TCDB; 2.A.41.2.4; the concentrative nucleoside transporter (cnt) family.
DR   CarbonylDB; O43868; -.
DR   iPTMnet; O43868; -.
DR   PhosphoSitePlus; O43868; -.
DR   BioMuta; SLC28A2; -.
DR   MassIVE; O43868; -.
DR   PaxDb; 9606-ENSP00000315006; -.
DR   PeptideAtlas; O43868; -.
DR   ProteomicsDB; 49214; -.
DR   Antibodypedia; 24414; 163 antibodies from 27 providers.
DR   DNASU; 9153; -.
DR   Ensembl; ENST00000347644.8; ENSP00000315006.4; ENSG00000137860.12.
DR   GeneID; 9153; -.
DR   KEGG; hsa:9153; -.
DR   MANE-Select; ENST00000347644.8; ENSP00000315006.4; NM_004212.4; NP_004203.2.
DR   UCSC; uc001zva.3; human.
DR   AGR; HGNC:11002; -.
DR   CTD; 9153; -.
DR   DisGeNET; 9153; -.
DR   GeneCards; SLC28A2; -.
DR   HGNC; HGNC:11002; SLC28A2.
DR   HPA; ENSG00000137860; Tissue enriched (intestine).
DR   MIM; 606208; gene.
DR   neXtProt; NX_O43868; -.
DR   OpenTargets; ENSG00000137860; -.
DR   PharmGKB; PA386; -.
DR   VEuPathDB; HostDB:ENSG00000137860; -.
DR   eggNOG; KOG3747; Eukaryota.
DR   GeneTree; ENSGT00390000016025; -.
DR   HOGENOM; CLU_016813_3_2_1; -.
DR   InParanoid; O43868; -.
DR   OMA; RAVFLWF; -.
DR   OrthoDB; 1333063at2759; -.
DR   PhylomeDB; O43868; -.
DR   TreeFam; TF314131; -.
DR   PathwayCommons; O43868; -.
DR   Reactome; R-HSA-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR   Reactome; R-HSA-9748787; Azathioprine ADME.
DR   Reactome; R-HSA-9755088; Ribavirin ADME.
DR   BioGRID-ORCS; 9153; 9 hits in 1140 CRISPR screens.
DR   GeneWiki; Concentrative_nucleoside_transporter_2; -.
DR   GenomeRNAi; 9153; -.
DR   Pharos; O43868; Tchem.
DR   PRO; PR:O43868; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; O43868; Protein.
DR   Bgee; ENSG00000137860; Expressed in jejunal mucosa and 90 other cell types or tissues.
DR   ExpressionAtlas; O43868; baseline and differential.
DR   GO; GO:0016327; C:apicolateral plasma membrane; IDA:UniProtKB.
DR   GO; GO:0031526; C:brush border membrane; ISS:ARUK-UCL.
DR   GO; GO:0030135; C:coated vesicle; ISS:ARUK-UCL.
DR   GO; GO:0016020; C:membrane; TAS:ProtInc.
DR   GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR   GO; GO:0012506; C:vesicle membrane; ISS:ARUK-UCL.
DR   GO; GO:1901474; F:azole transmembrane transporter activity; ISS:ARUK-UCL.
DR   GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0005415; F:nucleoside:sodium symporter activity; IDA:ARUK-UCL.
DR   GO; GO:0005345; F:purine nucleobase transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015211; F:purine nucleoside transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015389; F:pyrimidine- and adenosine-specific:sodium symporter activity; IDA:ARUK-UCL.
DR   GO; GO:0015213; F:uridine transmembrane transporter activity; IDA:ARUK-UCL.
DR   GO; GO:0032238; P:adenosine transport; IDA:ARUK-UCL.
DR   GO; GO:0045117; P:azole transmembrane transport; ISS:ARUK-UCL.
DR   GO; GO:0035340; P:inosine transport; IDA:ARUK-UCL.
DR   GO; GO:0006836; P:neurotransmitter transport; IDA:ARUK-UCL.
DR   GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR   GO; GO:1901642; P:nucleoside transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:1904823; P:purine nucleobase transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0015860; P:purine nucleoside transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0072531; P:pyrimidine-containing compound transmembrane transport; IDA:ARUK-UCL.
DR   GO; GO:0001895; P:retina homeostasis; IBA:GO_Central.
DR   GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR   GO; GO:0015862; P:uridine transport; IDA:ARUK-UCL.
DR   GO; GO:0006805; P:xenobiotic metabolic process; TAS:Reactome.
DR   GO; GO:0006855; P:xenobiotic transmembrane transport; TAS:Reactome.
DR   InterPro; IPR008276; C_nuclsd_transpt.
DR   InterPro; IPR018270; C_nuclsd_transpt_met_bac.
DR   InterPro; IPR011657; CNT_C_dom.
DR   InterPro; IPR002668; CNT_N_dom.
DR   InterPro; IPR011642; Gate_dom.
DR   NCBIfam; TIGR00804; nupC; 1.
DR   PANTHER; PTHR10590; SODIUM/NUCLEOSIDE COTRANSPORTER; 1.
DR   PANTHER; PTHR10590:SF11; SODIUM_NUCLEOSIDE COTRANSPORTER 2; 1.
DR   Pfam; PF07670; Gate; 1.
DR   Pfam; PF07662; Nucleos_tra2_C; 1.
DR   Pfam; PF01773; Nucleos_tra2_N; 1.
DR   Genevisible; O43868; HS.
PE   2: Evidence at transcript level;
KW   Cell membrane; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..658
FT                   /note="Sodium/nucleoside cotransporter 2"
FT                   /id="PRO_0000070450"
FT   TRANSMEM        80..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..123
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        233..253
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        295..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        362..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        454..474
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        529..549
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        567..587
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         45
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q62773"
FT   VARIANT         12
FT                   /note="L -> P (in dbSNP:rs567096708)"
FT                   /evidence="ECO:0000269|PubMed:17700367"
FT                   /id="VAR_036817"
FT   VARIANT         22
FT                   /note="P -> L (in dbSNP:rs11854484)"
FT                   /evidence="ECO:0000269|PubMed:15861032,
FT                   ECO:0000269|PubMed:17700367"
FT                   /id="VAR_024639"
FT   VARIANT         75
FT                   /note="S -> R (in dbSNP:rs1060896)"
FT                   /evidence="ECO:0000269|PubMed:10087507,
FT                   ECO:0000269|PubMed:15861032, ECO:0000269|PubMed:17700367"
FT                   /id="VAR_024640"
FT   VARIANT         142
FT                   /note="R -> H (in dbSNP:rs115740452)"
FT                   /evidence="ECO:0000269|PubMed:17700367"
FT                   /id="VAR_036818"
FT   VARIANT         163
FT                   /note="L -> W (in dbSNP:rs2271437)"
FT                   /evidence="ECO:0000269|PubMed:15861032,
FT                   ECO:0000269|PubMed:17700367"
FT                   /id="VAR_022001"
FT   VARIANT         172
FT                   /note="E -> D (in dbSNP:rs113624548)"
FT                   /evidence="ECO:0000269|PubMed:17700367"
FT                   /id="VAR_036819"
FT   VARIANT         245
FT                   /note="S -> T (in dbSNP:rs10519020)"
FT                   /evidence="ECO:0000269|PubMed:15861032"
FT                   /id="VAR_024641"
FT   VARIANT         355
FT                   /note="F -> S (in dbSNP:rs17215633)"
FT                   /evidence="ECO:0000269|PubMed:15861032"
FT                   /id="VAR_024642"
FT   VARIANT         385
FT                   /note="E -> K (in dbSNP:rs376327143)"
FT                   /evidence="ECO:0000269|PubMed:17700367"
FT                   /id="VAR_036820"
FT   VARIANT         462
FT                   /note="L -> F (in dbSNP:rs17222057)"
FT                   /evidence="ECO:0000269|PubMed:15861032"
FT                   /id="VAR_024643"
FT   VARIANT         509
FT                   /note="G -> E (in dbSNP:rs9635306)"
FT                   /id="VAR_028724"
FT   VARIANT         612
FT                   /note="M -> T (in dbSNP:rs373539209)"
FT                   /evidence="ECO:0000269|PubMed:17700367"
FT                   /id="VAR_036821"
SQ   SEQUENCE   658 AA;  71926 MW;  273545EE75E0D663 CRC64;
     MEKASGRQSI ALSTVETGTV NPGLELMEKE VEPEGSKRTD AQGHSLGDGL GPSTYQRRSR
     WPFSKARSFC KTHASLFKKI LLGLLCLAYA AYLLAACILN FQRALALFVI TCLVIFVLVH
     SFLKKLLGKK LTRCLKPFEN SRLRLWTKWV FAGVSLVGLI LWLALDTAQR PEQLIPFAGI
     CMFILILFAC SKHHSAVSWR TVFSGLGLQF VFGILVIRTD LGYTVFQWLG EQVQIFLNYT
     VAGSSFVFGD TLVKDVFAFQ ALPIIIFFGC VVSILYYLGL VQWVVQKVAW FLQITMGTTA
     TETLAVAGNI FVGMTEAPLL IRPYLGDMTL SEIHAVMTGG FATISGTVLG AFIAFGVDAS
     SLISASVMAA PCALASSKLA YPEVEESKFK SEEGVKLPRG KERNVLEAAS NGAVDAIGLA
     TNVAANLIAF LAVLAFINAA LSWLGELVDI QGLTFQVICS YLLRPMVFMM GVEWTDCPMV
     AEMVGIKFFI NEFVAYQQLS QYKNKRLSGM EEWIEGEKQW ISVRAEIITT FSLCGFANLS
     SIGITLGGLT SIVPHRKSDL SKVVVRALFT GACVSLISAC MAGILYVPRG AEADCVSFPN
     TSFTNRTYET YMCCRGLFQS TSLNGTNPPS FSGPWEDKEF SAMALTNCCG FYNNTVCA
//