ID SAMC_HUMAN Reviewed; 274 AA. AC Q70HW3; A8K758; B3KRZ7; F8WAB8; Q7Z786; Q96E68; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2018, sequence version 2. DT 27-MAR-2024, entry version 149. DE RecName: Full=Mitochondrial S-adenosylmethionine carrier protein {ECO:0000303|PubMed:14674884}; DE Short=SAM carrier {ECO:0000303|PubMed:14674884}; DE AltName: Full=Solute carrier family 25 member 26 {ECO:0000312|HGNC:HGNC:20661}; GN Name=SLC25A26 {ECO:0000312|HGNC:HGNC:20661}; GN Synonyms=SAMC {ECO:0000303|PubMed:14674884}; 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] (ISOFORM 1), FUNCTION, TRANSPORTER ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, SUBCELLULAR LOCATION, RP TISSUE SPECIFICITY, AND VARIANT ASN-41. RX PubMed=14674884; DOI=10.1042/bj20031664; RA Agrimi G., Di Noia M.A., Marobbio C.M.T., Fiermonte G., Lasorsa F.M., RA Palmieri F.; RT "Identification of the human mitochondrial S-adenosylmethionine RT transporter: bacterial expression, reconstitution, functional RT characterization and tissue distribution."; RL Biochem. J. 379:183-190(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS RP ASN-41 AND MET-208. RC TISSUE=Placenta, and Skeletal muscle; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS ASN-41 AND RP MET-208. 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 GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Ovary, and Placenta; 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 [6] RP INVOLVEMENT IN COXPD28, VARIANTS COXPD28 VAL-102; GLY-148 AND LEU-199, RP CHARACTERIZATION OF VARIANTS COXPD28 VAL-102; GLY-148 AND LEU-199, RP FUNCTION, TRANSPORTER ACTIVITY, AND SUBCELLULAR LOCATION. RX PubMed=26522469; DOI=10.1016/j.ajhg.2015.09.013; RA Kishita Y., Pajak A., Bolar N.A., Marobbio C.M., Maffezzini C., RA Miniero D.V., Monne M., Kohda M., Stranneheim H., Murayama K., Naess K., RA Lesko N., Bruhn H., Mourier A., Wibom R., Nennesmo I., Jespers A., RA Govaert P., Ohtake A., Van Laer L., Loeys B.L., Freyer C., Palmieri F., RA Wredenberg A., Okazaki Y., Wedell A.; RT "Intra-mitochondrial methylation deficiency due to mutations in SLC25A26."; RL Am. J. Hum. Genet. 97:761-768(2015). RN [7] RP VARIANTS COXPD28 GLY-135 AND GLN-142, CHARACTERIZATION OF VARIANTS COXPD28 RP GLY-135 AND GLN-142, FUNCTION, AND TRANSPORTER ACTIVITY. RX PubMed=35024855; DOI=10.1093/hmg/ddac002; RA Schober F.A., Tang J.X., Sergeant K., Moedas M.F., Zierz C.M., Moore D., RA Smith C., Lewis D., Guha N., Hopton S., Falkous G., Lam A., Pyle A., RA Poulton J., Gorman G.S., Taylor R.W., Freyer C., Wredenberg A.; RT "Pathogenic SLC25A26 variants impair SAH transport activity causing RT mitochondrial disease."; RL Hum. Mol. Genet. 31:2049-2062(2022). CC -!- FUNCTION: Mitochondrial S-adenosyl-L-methionine/S-adenosyl-L- CC homocysteine antiporter. Mediates the exchange of cytosolic S-adenosyl- CC L-methionine, the predominant methyl-group donor for macromolecule CC methylation processes, for mitochondrial S-adenosylhomocysteine(SAH), a CC by-product of methylation reactions. {ECO:0000269|PubMed:14674884, CC ECO:0000269|PubMed:26522469, ECO:0000269|PubMed:35024855}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-homocysteine(out) + S-adenosyl-L-methionine(in) = CC S-adenosyl-L-homocysteine(in) + S-adenosyl-L-methionine(out); CC Xref=Rhea:RHEA:75479, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; CC Evidence={ECO:0000269|PubMed:14674884, ECO:0000269|PubMed:26522469, CC ECO:0000269|PubMed:35024855}; CC -!- ACTIVITY REGULATION: Strongly inhibited by tannic acid and Bromocresol CC Purple. {ECO:0000269|PubMed:14674884}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=23 uM for S-adenosyl-L-methionine (at 25 degrees Celsius) CC {ECO:0000269|PubMed:14674884}; CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane CC {ECO:0000305|PubMed:14674884, ECO:0000305|PubMed:26522469}; Multi-pass CC membrane protein {ECO:0000255}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q70HW3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q70HW3-2; Sequence=VSP_031062; CC Name=3; CC IsoId=Q70HW3-3; Sequence=VSP_031062, VSP_031063, VSP_031064; CC -!- TISSUE SPECIFICITY: Widely expressed. Highly expressed in testis, with CC moderate expression in brain, heart, kidney, lung, skeletal muscle, CC pancreas, small intestine and liver, and low expression in spleen. CC {ECO:0000269|PubMed:14674884}. CC -!- DISEASE: Combined oxidative phosphorylation deficiency 28 (COXPD28) CC [MIM:616794]: An autosomal recessive mitochondrial disorder CC characterized by decreased activities of respiratory chain enzymes, and CC variable clinical manifestations. Clinical features include episodic CC metabolic decompensation beginning in infancy, mild muscle weakness, CC cardiorespiratory insufficiency, developmental delay, or even death. CC {ECO:0000269|PubMed:26522469, ECO:0000269|PubMed:35024855}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family. CC {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; AJ580932; CAE45652.1; -; mRNA. DR EMBL; AK092495; BAG52559.1; -; mRNA. DR EMBL; AK096876; BAG53388.1; -; mRNA. DR EMBL; AK291873; BAF84562.1; -; mRNA. DR EMBL; AC145425; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC170165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC092034; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC170801; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC235952; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AEKP01024816; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW65449.1; -; Genomic_DNA. DR EMBL; CH471055; EAW65451.1; -; Genomic_DNA. DR EMBL; BC003399; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC012852; AAH12852.2; -; mRNA. DR CCDS; CCDS2905.2; -. [Q70HW3-1] DR CCDS; CCDS54604.1; -. [Q70HW3-2] DR RefSeq; NP_001158268.1; NM_001164796.1. [Q70HW3-2] DR RefSeq; NP_775742.4; NM_173471.3. [Q70HW3-1] DR RefSeq; XP_011531629.1; XM_011533327.2. DR AlphaFoldDB; Q70HW3; -. DR SMR; Q70HW3; -. DR BioGRID; 125423; 9. DR IntAct; Q70HW3; 1. DR STRING; 9606.ENSP00000346955; -. DR TCDB; 2.A.29.18.3; the mitochondrial carrier (mc) family. DR iPTMnet; Q70HW3; -. DR PhosphoSitePlus; Q70HW3; -. DR BioMuta; SLC25A26; -. DR DMDM; 74749739; -. DR EPD; Q70HW3; -. DR jPOST; Q70HW3; -. DR MassIVE; Q70HW3; -. DR MaxQB; Q70HW3; -. DR PaxDb; 9606-ENSP00000346955; -. DR PeptideAtlas; Q70HW3; -. DR ProteomicsDB; 30470; -. DR ProteomicsDB; 68552; -. [Q70HW3-1] DR ProteomicsDB; 68553; -. [Q70HW3-2] DR ProteomicsDB; 68554; -. [Q70HW3-3] DR Pumba; Q70HW3; -. DR Antibodypedia; 15419; 131 antibodies from 19 providers. DR DNASU; 115286; -. DR Ensembl; ENST00000336733.10; ENSP00000336801.5; ENSG00000144741.19. [Q70HW3-2] DR Ensembl; ENST00000354883.11; ENSP00000346955.6; ENSG00000144741.19. [Q70HW3-1] DR Ensembl; ENST00000632575.1; ENSP00000488865.1; ENSG00000282739.1. [Q70HW3-2] DR Ensembl; ENST00000633701.1; ENSP00000488659.1; ENSG00000282739.1. [Q70HW3-1] DR Ensembl; ENST00000676754.1; ENSP00000504323.1; ENSG00000144741.19. [Q70HW3-1] DR Ensembl; ENST00000686511.1; ENSP00000509933.1; ENSG00000144741.19. [Q70HW3-2] DR Ensembl; ENST00000691461.1; ENSP00000510022.1; ENSG00000144741.19. [Q70HW3-2] DR GeneID; 115286; -. DR KEGG; hsa:115286; -. DR MANE-Select; ENST00000354883.11; ENSP00000346955.6; NM_001379210.1; NP_001366139.1. DR UCSC; uc011bfq.2; human. DR UCSC; uc011bfs.3; human. [Q70HW3-1] DR AGR; HGNC:20661; -. DR CTD; 115286; -. DR DisGeNET; 115286; -. DR GeneCards; SLC25A26; -. DR HGNC; HGNC:20661; SLC25A26. DR HPA; ENSG00000144741; Low tissue specificity. DR MalaCards; SLC25A26; -. DR MIM; 611037; gene. DR MIM; 616794; phenotype. DR neXtProt; NX_Q70HW3; -. DR OpenTargets; ENSG00000144741; -. DR Orphanet; 466784; Neonatal severe cardiopulmonary failure due to mitochondrial methylation defect. DR PharmGKB; PA134987831; -. DR VEuPathDB; HostDB:ENSG00000144741; -. DR eggNOG; KOG0768; Eukaryota. DR GeneTree; ENSGT00550000074950; -. DR InParanoid; Q70HW3; -. DR OMA; IGPRTMW; -. DR PhylomeDB; Q70HW3; -. DR TreeFam; TF313186; -. DR PathwayCommons; Q70HW3; -. DR Reactome; R-HSA-425393; Transport of inorganic cations/anions and amino acids/oligopeptides. DR SignaLink; Q70HW3; -. DR BioGRID-ORCS; 115286; 373 hits in 1179 CRISPR screens. DR ChiTaRS; SLC25A26; human. DR GenomeRNAi; 115286; -. DR Pharos; Q70HW3; Tbio. DR PRO; PR:Q70HW3; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q70HW3; Protein. DR Bgee; ENSG00000144741; Expressed in gastrocnemius and 99 other cell types or tissues. DR ExpressionAtlas; Q70HW3; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0000095; F:S-adenosyl-L-methionine transmembrane transporter activity; IMP:UniProtKB. DR GO; GO:0180003; F:S-adenosyl-L-methionine:S-adenosyl-L-homocysteine antiporter activity; IMP:UniProtKB. DR GO; GO:0043414; P:macromolecule methylation; IMP:UniProtKB. DR GO; GO:1990543; P:mitochondrial S-adenosyl-L-methionine transmembrane transport; IMP:UniProtKB. DR GO; GO:0006811; P:monoatomic ion transport; TAS:Reactome. DR GO; GO:0015805; P:S-adenosyl-L-methionine transport; IMP:UniProtKB. DR Gene3D; 1.50.40.10; Mitochondrial carrier domain; 1. DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier. DR InterPro; IPR023395; Mt_carrier_dom_sf. DR PANTHER; PTHR45667; S-ADENOSYLMETHIONINE MITOCHONDRIAL CARRIER PROTEIN; 1. DR PANTHER; PTHR45667:SF9; S-ADENOSYLMETHIONINE MITOCHONDRIAL CARRIER PROTEIN; 1. DR Pfam; PF00153; Mito_carr; 4. DR SUPFAM; SSF103506; Mitochondrial carrier; 1. DR PROSITE; PS50920; SOLCAR; 3. DR Genevisible; Q70HW3; HS. PE 1: Evidence at protein level; KW Alternative splicing; Antiport; Disease variant; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Primary mitochondrial disease; KW Reference proteome; Repeat; S-adenosyl-L-methionine; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1..274 FT /note="Mitochondrial S-adenosylmethionine carrier protein" FT /id="PRO_0000317587" FT TRANSMEM 5..25 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TRANSMEM 49..69 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TRANSMEM 85..105 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TRANSMEM 142..162 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TRANSMEM 182..202 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TRANSMEM 238..258 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT REPEAT 4..77 FT /note="Solcar 1" FT REPEAT 86..168 FT /note="Solcar 2" FT REPEAT 177..265 FT /note="Solcar 3" FT VAR_SEQ 1..88 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334" FT /id="VSP_031062" FT VAR_SEQ 152..154 FT /note="IPF -> EED (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031063" FT VAR_SEQ 155..274 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_031064" FT VARIANT 41 FT /note="S -> N (in dbSNP:rs146159281)" FT /evidence="ECO:0000269|PubMed:14674884, FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3" FT /id="VAR_080244" FT VARIANT 102 FT /note="A -> V (in COXPD28; loss of FT S-adenosyl-L-methionine/S-adenosyl-L-homocysteine FT antiporter activity; dbSNP:rs869025314)" FT /evidence="ECO:0000269|PubMed:26522469" FT /id="VAR_076305" FT VARIANT 135 FT /note="E -> G (in COXPD28; uncertain significance; FT decreased S-adenosyl-L-methionine/S-adenosyl-L-homocysteine FT antiporter activity)" FT /evidence="ECO:0000269|PubMed:35024855" FT /id="VAR_087910" FT VARIANT 142 FT /note="R -> Q (in COXPD28; uncertain significance; FT decreased protein abundance; decreased FT S-adenosyl-L-methionine/S-adenosyl-L-homocysteine FT antiporter activity)" FT /evidence="ECO:0000269|PubMed:35024855" FT /id="VAR_087911" FT VARIANT 148 FT /note="V -> G (in COXPD28; decreased FT S-adenosyl-L-methionine/S-adenosyl-L-homocysteine FT antiporter activity; dbSNP:rs869025313)" FT /evidence="ECO:0000269|PubMed:26522469" FT /id="VAR_076306" FT VARIANT 199 FT /note="P -> L (in COXPD28; loss of FT S-adenosyl-L-methionine/S-adenosyl-L-homocysteine FT antiporter activity; dbSNP:rs869025315)" FT /evidence="ECO:0000269|PubMed:26522469" FT /id="VAR_076307" FT VARIANT 208 FT /note="T -> M (in dbSNP:rs13874)" FT /evidence="ECO:0000269|PubMed:14702039, ECO:0000269|Ref.3" FT /id="VAR_058973" FT CONFLICT 208 FT /note="T -> A (in Ref. 2; BAF84562)" FT /evidence="ECO:0000305" SQ SEQUENCE 274 AA; 29354 MW; 97315DE9CC68D19D CRC64; MDRPGFVAAL VAGGVAGVSV DLILFPLDTI KTRLQSPQGF SKAGGFHGIY AGVPSAAIGS FPNAAAFFIT YEYVKWFLHA DSSSYLTPMK HMLAASAGEV VACLIRVPSE VVKQRAQVSA STRTFQIFSN ILYEEGIQGL YRGYKSTVLR EIPFSLVQFP LWESLKALWS WRQDHVVDSW QSAVCGAFAG GFAAAVTTPL DVAKTRITLA KAGSSTADGN VLSVLHGVWR SQGLAGLFAG VFPRMAAISL GGFIFLGAYD RTHSLLLEVG RKSP //