MOT2_HUMAN
ID MOT2_HUMAN Reviewed; 478 AA.
AC O60669; Q8NEM3; Q9UPB3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Monocarboxylate transporter 2;
DE Short=MCT 2;
DE AltName: Full=Solute carrier family 16 member 7;
GN Name=SLC16A7; Synonyms=MCT2;
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, AND SUBCELLULAR LOCATION.
RC TISSUE=Liver;
RX PubMed=9786900; DOI=10.1074/jbc.273.44.28959;
RA Lin R.-Y., Vera J.C., Chaganti R.S.K., Golde D.W.;
RT "Human monocarboxylate transporter 2 (MCT2) is a high affinity pyruvate
RT transporter.";
RL J. Biol. Chem. 273:28959-28965(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-445.
RC TISSUE=Liver;
RA Dao L., Landschulz W.H., Landschulz K.T.;
RT "Cloning of human monocarboxylate transporter 2 (hMCT2).";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15505343; DOI=10.1369/jhc.4a6306.2004;
RA Merezhinskaya N., Ogunwuyi S.A., Mullick F.G., Fishbein W.N.;
RT "Presence and localization of three lactic acid transporters (MCT1, -2, and
RT -4) in separated human granulocytes, lymphocytes, and monocytes.";
RL J. Histochem. Cytochem. 52:1483-1493(2004).
CC -!- FUNCTION: Proton-coupled monocarboxylate transporter. Catalyzes the
CC rapid transport across the plasma membrane of many monocarboxylates
CC such as lactate, pyruvate, branched-chain oxo acids derived from
CC leucine, valine and isoleucine, and the ketone bodies acetoacetate,
CC beta-hydroxybutyrate and acetate. Functions as high-affinity pyruvate
CC transporter. {ECO:0000269|PubMed:9786900}.
CC -!- SUBUNIT: Interacts with GRID2IP (By similarity). Interacts with EMB (By
CC similarity). Interacts with isoform 2 of BSG (By similarity).
CC {ECO:0000250|UniProtKB:O70451, ECO:0000250|UniProtKB:Q63344}.
CC -!- INTERACTION:
CC O60669; Q9ULC5: ACSL5; NbExp=3; IntAct=EBI-3921243, EBI-2876927;
CC O60669; O14735: CDIPT; NbExp=3; IntAct=EBI-3921243, EBI-358858;
CC O60669; P21964: COMT; NbExp=3; IntAct=EBI-3921243, EBI-372265;
CC O60669; Q9H0Q3: FXYD6; NbExp=3; IntAct=EBI-3921243, EBI-713304;
CC O60669; O00155: GPR25; NbExp=3; IntAct=EBI-3921243, EBI-10178951;
CC O60669; P09601: HMOX1; NbExp=3; IntAct=EBI-3921243, EBI-2806151;
CC O60669; Q01628: IFITM3; NbExp=3; IntAct=EBI-3921243, EBI-7932862;
CC O60669; Q68G75: LEMD1; NbExp=3; IntAct=EBI-3921243, EBI-12268900;
CC O60669; Q9H9B4: SFXN1; NbExp=3; IntAct=EBI-3921243, EBI-355861;
CC O60669; Q0VAQ4: SMAGP; NbExp=3; IntAct=EBI-3921243, EBI-10226799;
CC O60669; O14925: TIMM23; NbExp=3; IntAct=EBI-3921243, EBI-1047996;
CC O60669; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-3921243, EBI-1059156;
CC O60669; Q9UEU0: VTI1B; NbExp=3; IntAct=EBI-3921243, EBI-723716;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15505343,
CC ECO:0000269|PubMed:9786900}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15505343, ECO:0000269|PubMed:9786900}.
CC -!- TISSUE SPECIFICITY: Detected in heart and in blood lymphocytes and
CC monocytes (at protein level). High expression in testis, moderate to
CC low in spleen, heart, kidney, pancreas, skeletal muscle, brain and
CC Leukocyte. Restricted expression in normal tissues, but widely
CC expressed in cancer cells. {ECO:0000269|PubMed:15505343}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}.
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DR EMBL; AF049608; AAC70919.1; -; mRNA.
DR EMBL; AF058056; AAC13721.1; -; mRNA.
DR EMBL; AK313345; BAG36148.1; -; mRNA.
DR EMBL; AC079905; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471054; EAW97096.1; -; Genomic_DNA.
DR EMBL; BC030693; AAH30693.1; -; mRNA.
DR CCDS; CCDS8961.1; -.
DR RefSeq; NP_001257551.1; NM_001270622.1.
DR RefSeq; NP_001257552.1; NM_001270623.1.
DR RefSeq; NP_004722.2; NM_004731.4.
DR RefSeq; XP_005269288.1; XM_005269231.4.
DR PDB; 7BP3; EM; 3.80 A; A/B=1-478.
DR PDBsum; 7BP3; -.
DR AlphaFoldDB; O60669; -.
DR SMR; O60669; -.
DR BioGRID; 114629; 30.
DR IntAct; O60669; 21.
DR MINT; O60669; -.
DR STRING; 9606.ENSP00000261187; -.
DR ChEMBL; CHEMBL2073704; -.
DR DrugBank; DB01762; Acetoacetic acid.
DR DrugBank; DB03773; alpha-D-quinovopyranose.
DR DrugBank; DB04074; alpha-Ketoisovalerate.
DR DrugBank; DB03066; D-Lactic acid.
DR DrugBank; DB01440; gamma-Hydroxybutyric acid.
DR DrugBank; DB04398; Lactic acid.
DR DrugBank; DB04552; Niflumic acid.
DR DrugBank; DB01032; Probenecid.
DR DrugBank; DB00119; Pyruvic acid.
DR DrugBank; DB04216; Quercetin.
DR GuidetoPHARMACOLOGY; 990; -.
DR TCDB; 2.A.1.13.5; the major facilitator superfamily (mfs).
DR GlyGen; O60669; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O60669; -.
DR PhosphoSitePlus; O60669; -.
DR BioMuta; SLC16A7; -.
DR EPD; O60669; -.
DR jPOST; O60669; -.
DR MassIVE; O60669; -.
DR PaxDb; O60669; -.
DR PeptideAtlas; O60669; -.
DR PRIDE; O60669; -.
DR ProteomicsDB; 49513; -.
DR Antibodypedia; 1576; 256 antibodies from 36 providers.
DR DNASU; 9194; -.
DR Ensembl; ENST00000261187.8; ENSP00000261187.4; ENSG00000118596.12.
DR Ensembl; ENST00000547379.6; ENSP00000448071.1; ENSG00000118596.12.
DR Ensembl; ENST00000552024.5; ENSP00000448742.1; ENSG00000118596.12.
DR Ensembl; ENST00000552432.5; ENSP00000449547.1; ENSG00000118596.12.
DR GeneID; 9194; -.
DR KEGG; hsa:9194; -.
DR MANE-Select; ENST00000547379.6; ENSP00000448071.1; NM_001270623.2; NP_001257552.1.
DR UCSC; uc001sqs.5; human.
DR CTD; 9194; -.
DR DisGeNET; 9194; -.
DR GeneCards; SLC16A7; -.
DR HGNC; HGNC:10928; SLC16A7.
DR HPA; ENSG00000118596; Tissue enhanced (heart).
DR MIM; 603654; gene.
DR neXtProt; NX_O60669; -.
DR OpenTargets; ENSG00000118596; -.
DR PharmGKB; PA35819; -.
DR VEuPathDB; HostDB:ENSG00000118596; -.
DR eggNOG; KOG2504; Eukaryota.
DR GeneTree; ENSGT00940000157309; -.
DR InParanoid; O60669; -.
DR OMA; ALNWPVR; -.
DR OrthoDB; 916876at2759; -.
DR PhylomeDB; O60669; -.
DR TreeFam; TF313792; -.
DR PathwayCommons; O60669; -.
DR Reactome; R-HSA-433692; Proton-coupled monocarboxylate transport.
DR SABIO-RK; O60669; -.
DR SignaLink; O60669; -.
DR BioGRID-ORCS; 9194; 16 hits in 1073 CRISPR screens.
DR ChiTaRS; SLC16A7; human.
DR GenomeRNAi; 9194; -.
DR Pharos; O60669; Tchem.
DR PRO; PR:O60669; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O60669; protein.
DR Bgee; ENSG00000118596; Expressed in heart right ventricle and 204 other tissues.
DR ExpressionAtlas; O60669; baseline and differential.
DR Genevisible; O60669; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0015129; F:lactate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005477; F:pyruvate secondary active transmembrane transporter activity; TAS:ProtInc.
DR GO; GO:0050833; F:pyruvate transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0035873; P:lactate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0015718; P:monocarboxylic acid transport; IBA:GO_Central.
DR GO; GO:1901475; P:pyruvate transmembrane transport; IDA:UniProtKB.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 1.20.1250.20; -; 1.
DR InterPro; IPR004743; MCT.
DR InterPro; IPR027178; MCT2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR11360:SF25; PTHR11360:SF25; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00892; 2A0113; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Reference proteome; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..478
FT /note="Monocarboxylate transporter 2"
FT /id="PRO_0000211385"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..89
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..115
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 137..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..173
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 195..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..312
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 313..333
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 334..338
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..373
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 395..406
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 407..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 200..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..460
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 445
FT /note="T -> S (in dbSNP:rs3763980)"
FT /evidence="ECO:0000269|Ref.2"
FT /id="VAR_031660"
FT CONFLICT 26
FT /note="A -> T (in Ref. 2; AAC70919)"
FT /evidence="ECO:0000305"
FT CONFLICT 154
FT /note="S -> N (in Ref. 2; AAC70919)"
FT /evidence="ECO:0000305"
FT CONFLICT 268
FT /note="L -> P (in Ref. 2; AAC70919)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 478 AA; 52200 MW; E508D650E8D7DE98 CRC64;
MPPMPSAPPV HPPPDGGWGW IVVGAAFISI GFSYAFPKAV TVFFKEIQQI FHTTYSEIAW
ISSIMLAVMY AGGPVSSVLV NKYGSRPVVI AGGLLCCLGM VLASFSSSVV QLYLTMGFIT
GLGLAFNLQP ALTIIGKYFY RKRPMANGLA MAGSPVFLSS LAPFNQYLFN TFGWKGSFLI
LGSLLLNACV AGSLMRPLGP NQTTSKSKNK TGKTEDDSSP KKIKTKKSTW EKVNKYLDFS
LFKHRGFLIY LSGNVIMFLG FFAPIIFLAP YAKDQGIDEY SAAFLLSVMA FVDMFARPSV
GLIANSKYIR PRIQYFFSFA IMFNGVCHLL CPLAQDYTSL VLYAVFFGLG FGSVSSVLFE
TLMDLVGAPR FSSAVGLVTI VECGPVLLGP PLAGKLVDLT GEYKYMYMSC GAIVVAASVW
LLIGNAINYR LLAKERKEEN ARQKTRESEP LSKSKHSEDV NVKVSNAQSV TSERETNI
