ID MOT8_HUMAN Reviewed; 539 AA. AC P36021; Q7Z797; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 2. DT 04-MAR-2015, entry version 117. DE RecName: Full=Monocarboxylate transporter 8; DE Short=MCT 8; DE AltName: Full=Monocarboxylate transporter 7; DE Short=MCT 7; DE AltName: Full=Solute carrier family 16 member 2; DE AltName: Full=X-linked PEST-containing transporter; GN Name=SLC16A2; Synonyms=MCT8, XPCT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. RX PubMed=7981683; DOI=10.1093/hmg/3.7.1133; RA Lafreniere R.G., Carrel L., Willard H.F.; RT "A novel transmembrane transporter encoded by the XPCT gene in RT Xq13.2."; RL Hum. Mol. Genet. 3:1133-1140(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Kim D., Kanai Y., Choi H., Shin H., Kim J., Teraoka H., Shigeta Y., RA Chairoungdua A., Babu E., Anzai N., Iribe Y., Endou H.; RT "X-linked PEST-containing transporter (XPCT) identified in the X- RT chromosome inactivation center is an acidic amino acid transporter RT which requires CD147 for its functional expression."; RL Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [4] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [5] RP SUBUNIT. RX PubMed=19797118; DOI=10.1210/en.2009-0699; RA Visser W.E., Philp N.J., van Dijk T.B., Klootwijk W., Friesema E.C., RA Jansen J., Beesley P.W., Ianculescu A.G., Visser T.J.; RT "Evidence for a homodimeric structure of human monocarboxylate RT transporter 8."; RL Endocrinology 150:5163-5170(2009). RN [6] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS]. RX PubMed=22223895; DOI=10.1074/mcp.M111.015131; RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., RA Meinnel T., Giglione C.; RT "Comparative large-scale characterisation of plant vs. mammal proteins RT reveals similar and idiosyncratic N-alpha acetylation features."; RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012). RN [7] RP FUNCTION, AND MUTAGENESIS OF HIS-118; HIS-186 AND HIS-376. RX PubMed=23610131; DOI=10.1210/en.2012-2225; RA Groeneweg S., Lima de Souza E.C., Visser W.E., Peeters R.P., RA Visser T.J.; RT "Importance of His192 in the human thyroid hormone transporter MCT8 RT for substrate recognition."; RL Endocrinology 154:2525-2532(2013). RN [8] RP VARIANT MCT8 DEFICIENCY VAL-150. RA Friesema E., Grueters A., Halestrap A., Reeser M., Visser T.; RT "Mutations in a thyroid hormone transporter in patients with severe RT psychomotor retardation and high serum T3 levels."; RL Thyroid 13:672-672(2003). RN [9] RP VARIANT MCT8 DEFICIENCY PRO-438. RX PubMed=14661163; DOI=10.1086/380999; RA Dumitrescu A.M., Liao X.-H., Best T.B., Brockmann K., Refetoff S.; RT "A novel syndrome combining thyroid and neurological abnormalities is RT associated with mutations in a monocarboxylate transporter gene."; RL Am. J. Hum. Genet. 74:168-175(2004). RN [10] RP ERRATUM. RA Dumitrescu A.M., Liao X.-H., Best T.B., Brockmann K., Refetoff S.; RL Am. J. Hum. Genet. 74:598-598(2004). RN [11] RP IDENTIFICATION OF START CODON. RX PubMed=18398436; DOI=10.1038/ejhg.2008.66; RA Frints S.G., Lenzner S., Bauters M., Jensen L.R., Van Esch H., RA des Portes V., Moog U., Macville M.V., van Roozendaal K., RA Schrander-Stumpel C.T., Tzschach A., Marynen P., Fryns J.P., Hamel B., RA van Bokhoven H., Chelly J., Beldjord C., Turner G., Gecz J., RA Moraine C., Raynaud M., Ropers H.H., Froyen G., Kuss A.W.; RT "MCT8 mutation analysis and identification of the first female with RT Allan-Herndon-Dudley syndrome due to loss of MCT8 expression."; RL Eur. J. Hum. Genet. 16:1029-1037(2008). RN [12] RP VARIANTS MCT8 DEFICIENCY VAL-150 AND PRO-397. RX PubMed=15488219; DOI=10.1016/S0140-6736(04)17226-7; RA Friesema E.C.H., Grueters A., Biebermann H., Krude H., von Moers A., RA Reeser M., Barrett T.G., Mancilla E.E., Svensson J., Kester M.H.A., RA Kuiper G.G.J.M., Balkassmi S., Uitterlinden A.G., Koehrle J., RA Rodien P., Halestrap A.P., Visser T.J.; RT "Association between mutations in a thyroid hormone transporter and RT severe X-linked psychomotor retardation."; RL Lancet 364:1435-1437(2004). RN [13] RP VARIANTS MCT8 DEFICIENCY PHE-120; PHE-156 DEL; MET-161; TRP-360 AND RP PRO-494. RX PubMed=15889350; DOI=10.1086/431313; RA Schwartz C.E., May M.M., Carpenter N.J., Rogers R.C., Martin J., RA Bialer M.G., Ward J., Sanabria J., Marsa S., Lewis J.A., Echeverri R., RA Lubs H.A., Voeller K., Simensen R.J., Stevenson R.E.; RT "Allan-Herndon-Dudley syndrome and the monocarboxylate transporter 8 RT (MCT8) gene."; RL Am. J. Hum. Genet. 77:41-53(2005). RN [14] RP VARIANTS MCT8 DEFICIENCY PHE-427 DEL AND ARG-490, AND POSSIBLE RP PATHOGENIC MECHANISM OF BRAIN DEVELOPMENT. RX PubMed=18636565; DOI=10.1002/humu.20808; RA Visser W.E., Jansen J., Friesema E.C.H., Kester M.H.A., Mancilla E., RA Lundgren J., van der Knaap M.S., Lunsing R.J., Brouwer O.F., RA Visser T.J.; RT "Novel pathogenic mechanism suggested by ex vivo analysis of MCT8 RT (SLC16A2) mutations."; RL Hum. Mutat. 30:29-38(2009). CC -!- FUNCTION: Very active and specific thyroid hormone transporter. CC Stimulates cellular uptake of thyroxine (T4), triiodothyronine CC (T3), reverse triiodothyronine (rT3) and diidothyronine. Does not CC transport Leu, Phe, Trp or Tyr (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19797118}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Highly expressed in liver and heart. CC -!- DISEASE: Monocarboxylate transporter 8 deficiency (MCT8 CC deficiency) [MIM:300523]: Consists of a severe form of X-linked CC psychomotor retardation combined with abnormal thyroid hormone CC (TH) levels. Thyroid hormone deficiency can be caused by defects CC of hormone synthesis and action, but it has also been linked to a CC defect in cellular hormone transport. Affected patients are males CC with abnormal relative concentrations of three circulating CC iodothyronines, as well as severe neurological abnormalities, CC including global developmental delay, central hypotonia, spastic CC quadriplegia, dystonic movements, rotary nystagmus, and impaired CC gaze and hearing. Heterozygous females had a milder thyroid CC phenotype and no neurological defects. CC {ECO:0000269|PubMed:14661163, ECO:0000269|PubMed:15488219, CC ECO:0000269|PubMed:15889350, ECO:0000269|PubMed:18636565, CC ECO:0000269|Ref.8}. Note=The disease is caused by mutations CC affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Abnormal brain development associated with MCT8 CC deficiency may be the consequence of either decreased or increased CC intracellular T3 concentrations. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC Monocarboxylate porter (TC 2.A.1.13) family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB60374.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC Sequence=AAB60375.1; Type=Erroneous gene model prediction; 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; U05321; AAB60375.1; ALT_SEQ; Genomic_DNA. DR EMBL; U05316; AAB60375.1; JOINED; Genomic_DNA. DR EMBL; U05317; AAB60375.1; JOINED; Genomic_DNA. DR EMBL; U05318; AAB60375.1; JOINED; Genomic_DNA. DR EMBL; U05319; AAB60375.1; JOINED; Genomic_DNA. DR EMBL; U05320; AAB60375.1; JOINED; Genomic_DNA. DR EMBL; U05315; AAB60374.1; ALT_INIT; mRNA. DR EMBL; AB085789; BAC76827.1; -; mRNA. DR EMBL; AC004073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL157934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS14426.2; -. DR PIR; I39295; I39295. DR RefSeq; NP_006508.2; NM_006517.4. DR UniGene; Hs.75317; -. DR ProteinModelPortal; P36021; -. DR BioGrid; 112455; 4. DR STRING; 9606.ENSP00000276033; -. DR DrugBank; DB00149; L-Leucine. DR DrugBank; DB00150; L-Tryptophan. DR DrugBank; DB00135; L-Tyrosine. DR DrugBank; DB00451; Levothyroxine. DR DrugBank; DB01583; Liotrix. DR DrugBank; DB00119; Pyruvic acid. DR TCDB; 2.A.1.13.10; the major facilitator superfamily (mfs). DR PhosphoSite; P36021; -. DR DMDM; 114152841; -. DR MaxQB; P36021; -. DR PaxDb; P36021; -. DR PRIDE; P36021; -. DR Ensembl; ENST00000587091; ENSP00000465734; ENSG00000147100. DR GeneID; 6567; -. DR KEGG; hsa:6567; -. DR UCSC; uc031tjy.1; human. DR CTD; 6567; -. DR GeneCards; GC0XP073640; -. DR GeneReviews; SLC16A2; -. DR H-InvDB; HIX0056105; -. DR HGNC; HGNC:10923; SLC16A2. DR MIM; 300095; gene. DR MIM; 300523; phenotype. DR neXtProt; NX_P36021; -. DR Orphanet; 59; Allan-Herndon-Dudley syndrome. DR PharmGKB; PA35814; -. DR eggNOG; NOG321880; -. DR GeneTree; ENSGT00740000115479; -. DR HOVERGEN; HBG006387; -. DR InParanoid; P36021; -. DR KO; K08231; -. DR OrthoDB; EOG7KWSH8; -. DR PhylomeDB; P36021; -. DR TreeFam; TF313792; -. DR ChiTaRS; SLC16A2; human. DR GeneWiki; SLC16A2; -. DR GenomeRNAi; 6567; -. DR NextBio; 25551; -. DR PRO; PR:P36021; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; P36021; -. DR CleanEx; HS_SLC16A2; -. DR Genevestigator; P36021; -. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc. DR GO; GO:0016020; C:membrane; TAS:ProtInc. DR GO; GO:0008028; F:monocarboxylic acid transmembrane transporter activity; TAS:ProtInc. DR GO; GO:0015293; F:symporter activity; IEA:UniProtKB-KW. DR GO; GO:0015349; F:thyroid hormone transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005215; F:transporter activity; TAS:ProtInc. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GO_Central. DR GO; GO:0015718; P:monocarboxylic acid transport; TAS:ProtInc. DR GO; GO:0070327; P:thyroid hormone transport; IBA:GO_Central. DR GO; GO:0006810; P:transport; TAS:ProtInc. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 1: Evidence at protein level; KW Acetylation; Cell membrane; Complete proteome; Disease mutation; KW Membrane; Polymorphism; Reference proteome; Symport; Transmembrane; KW Transmembrane helix; Transport. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:22223895}. FT CHAIN 2 539 Monocarboxylate transporter 8. FT /FTId=PRO_0000211401. FT TOPO_DOM 2 96 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TOPO_DOM 118 143 Extracellular. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TOPO_DOM 165 171 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TOPO_DOM 193 200 Extracellular. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TOPO_DOM 222 229 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 230 250 Helical. {ECO:0000255}. FT TOPO_DOM 251 258 Extracellular. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. FT TOPO_DOM 280 322 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255}. FT TOPO_DOM 344 356 Extracellular. {ECO:0000255}. FT TRANSMEM 357 377 Helical. {ECO:0000255}. FT TOPO_DOM 378 386 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 387 407 Helical. {ECO:0000255}. FT TOPO_DOM 408 409 Extracellular. {ECO:0000255}. FT TRANSMEM 410 430 Helical. {ECO:0000255}. FT TOPO_DOM 431 447 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 448 468 Helical. {ECO:0000255}. FT TOPO_DOM 469 477 Extracellular. {ECO:0000255}. FT TRANSMEM 478 498 Helical. {ECO:0000255}. FT TOPO_DOM 499 539 Cytoplasmic. {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000269|PubMed:19413330, FT ECO:0000269|PubMed:22223895}. FT VARIANT 120 120 S -> F (in MCT8 deficiency). FT {ECO:0000269|PubMed:15889350}. FT /FTId=VAR_059054. FT VARIANT 150 150 A -> V (in MCT8 deficiency). FT {ECO:0000269|PubMed:15488219, FT ECO:0000269|Ref.8}. FT /FTId=VAR_022348. FT VARIANT 156 156 Missing (in MCT8 deficiency). FT {ECO:0000269|PubMed:15889350}. FT /FTId=VAR_059055. FT VARIANT 161 161 V -> M (in MCT8 deficiency). FT {ECO:0000269|PubMed:15889350}. FT /FTId=VAR_059056. FT VARIANT 323 323 I -> L (in dbSNP:rs12849411). FT /FTId=VAR_057723. FT VARIANT 360 360 L -> W (in MCT8 deficiency). FT {ECO:0000269|PubMed:15889350}. FT /FTId=VAR_059057. FT VARIANT 397 397 L -> P (in MCT8 deficiency). FT {ECO:0000269|PubMed:15488219}. FT /FTId=VAR_022349. FT VARIANT 427 427 Missing (in MCT8 deficiency). FT {ECO:0000269|PubMed:18636565}. FT /FTId=VAR_059058. FT VARIANT 438 438 L -> P (in MCT8 deficiency). FT {ECO:0000269|PubMed:14661163}. FT /FTId=VAR_022350. FT VARIANT 490 490 G -> R (in MCT8 deficiency). FT {ECO:0000269|PubMed:18636565}. FT /FTId=VAR_059059. FT VARIANT 494 494 L -> P (in MCT8 deficiency). FT {ECO:0000269|PubMed:15889350}. FT /FTId=VAR_059060. FT MUTAGEN 118 118 H->A: Reduction of thyroid hormone (TH) FT transport. {ECO:0000269|PubMed:23610131}. FT MUTAGEN 186 186 H->A: No effect on thyroid hormone (TH) FT transport. {ECO:0000269|PubMed:23610131}. FT MUTAGEN 376 376 H->A: No effect on thyroid hormone (TH) FT transport. {ECO:0000269|PubMed:23610131}. SQ SEQUENCE 539 AA; 59511 MW; E4DB873D59FA4DD6 CRC64; MALQSQASEE AKGPWQEADQ EQQEPVGSPE PESEPEPEPE PEPVPVPPPE PQPEPQPLPD PAPLPELEFE SERVHEPEPT PTVETRGTAR GFQPPEGGFG WVVVFAATWC NGSIFGIHNS VGILYSMLLE EEKEKNRQVE FQAAWVGALA MGMIFFCSPI VSIFTDRLGC RITATAGAAV AFIGLHTSSF TSSLSLRYFT YGILFGCGCS FAFQPSLVIL GHYFQRRLGL ANGVVSAGSS IFSMSFPFLI RMLGDKIKLA QTFQVLSTFM FVLMLLSLTY RPLLPSSQDT PSKRGVRTLH QRFLAQLRKY FNMRVFRQRT YRIWAFGIAA AALGYFVPYV HLMKYVEEEF SEIKETWVLL VCIGATSGLG RLVSGHISDS IPGLKKIYLQ VLSFLLLGLM SMMIPLCRDF GGLIVVCLFL GLCDGFFITI MAPIAFELVG PMQASQAIGY LLGMMALPMI AGPPIAGLLR NCFGDYHVAF YFAGVPPIIG AVILFFVPLM HQRMFKKEQR DSSKDKMLAP DPDPNGELLP GSPNPEEPI //