ID RM15_HUMAN Reviewed; 296 AA. AC Q9P015; Q96Q54; Q9H0Y1; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 27-MAR-2024, entry version 168. DE RecName: Full=Large ribosomal subunit protein uL15m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L15, mitochondrial; DE Short=L15mt; DE Short=MRP-L15; DE Flags: Precursor; GN Name=MRPL15; ORFNames=HSPC145; 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]. RC TISSUE=Blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Fetal brain; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cervix; 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 [GENOMIC DNA] OF 259-296. RX PubMed=11543634; DOI=10.1006/geno.2001.6622; RA Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., RA Watanabe K., Tanaka T.; RT "The human mitochondrial ribosomal protein genes: mapping of 54 genes to RT the chromosomes and implications for human disorders."; RL Genomics 77:65-70(2001). RN [6] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [9] {ECO:0007744|PDB:3J7Y} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25278503; DOI=10.1126/science.1258026; RA Brown A., Amunts A., Bai X.C., Sugimoto Y., Edwards P.C., Murshudov G., RA Scheres S.H., Ramakrishnan V.; RT "Structure of the large ribosomal subunit from human mitochondria."; RL Science 346:718-722(2014). RN [10] {ECO:0007744|PDB:3J9M} RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=25838379; DOI=10.1126/science.aaa1193; RA Amunts A., Brown A., Toots J., Scheres S.H., Ramakrishnan V.; RT "Ribosome. The structure of the human mitochondrial ribosome."; RL Science 348:95-98(2015). RN [11] {ECO:0007744|PDB:5OOL, ECO:0007744|PDB:5OOM} RP STRUCTURE BY ELECTRON MICROSCOPY (3.03 ANGSTROMS), SUBCELLULAR LOCATION, RP AND SUBUNIT. RX PubMed=28892042; DOI=10.1038/nsmb.3464; RA Brown A., Rathore S., Kimanius D., Aibara S., Bai X.C., Rorbach J., RA Amunts A., Ramakrishnan V.; RT "Structures of the human mitochondrial ribosome in native states of RT assembly."; RL Nat. Struct. Mol. Biol. 24:866-869(2017). CC -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt- CC LSU) (PubMed:28892042, PubMed:25838379, PubMed:25278503). Mature CC mammalian 55S mitochondrial ribosomes consist of a small (28S) and a CC large (39S) subunit. The 28S small subunit contains a 12S ribosomal RNA CC (12S mt-rRNA) and 30 different proteins. The 39S large subunit contains CC a 16S rRNA (16S mt-rRNA), a copy of mitochondrial valine transfer RNA CC (mt-tRNA(Val)), which plays an integral structural role, and 52 CC different proteins. {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- INTERACTION: CC Q9P015; O95273: CCNDBP1; NbExp=7; IntAct=EBI-2371967, EBI-748961; CC Q9P015; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-2371967, EBI-747225; CC Q9P015; P09012: SNRPA; NbExp=3; IntAct=EBI-2371967, EBI-607085; CC Q9P015; P26368-2: U2AF2; NbExp=3; IntAct=EBI-2371967, EBI-11097439; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL15 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; AF161494; AAF29109.1; -; mRNA. DR EMBL; AL136665; CAB66600.1; -; mRNA. DR EMBL; CR533531; CAG38562.1; -; mRNA. DR EMBL; BC000891; AAH00891.1; -; mRNA. DR EMBL; AB051619; BAB54947.1; -; Genomic_DNA. DR CCDS; CCDS6158.1; -. DR RefSeq; NP_054894.1; NM_014175.3. DR PDB; 3J7Y; EM; 3.40 A; M=1-296. DR PDB; 3J9M; EM; 3.50 A; M=1-296. DR PDB; 5OOL; EM; 3.06 A; M=1-296. DR PDB; 5OOM; EM; 3.03 A; M=1-296. DR PDB; 6I9R; EM; 3.90 A; M=1-296. DR PDB; 6NU2; EM; 3.90 A; M=10-296. DR PDB; 6NU3; EM; 4.40 A; M=1-296. DR PDB; 6VLZ; EM; 2.97 A; M=1-296. DR PDB; 6VMI; EM; 2.96 A; M=1-296. DR PDB; 6ZM5; EM; 2.89 A; M=1-296. DR PDB; 6ZM6; EM; 2.59 A; M=1-296. DR PDB; 6ZS9; EM; 4.00 A; XM=1-296. DR PDB; 6ZSA; EM; 4.00 A; XM=1-296. DR PDB; 6ZSB; EM; 4.50 A; XM=1-296. DR PDB; 6ZSC; EM; 3.50 A; XM=1-296. DR PDB; 6ZSD; EM; 3.70 A; XM=1-296. DR PDB; 6ZSE; EM; 5.00 A; XM=1-296. DR PDB; 6ZSG; EM; 4.00 A; XM=1-296. DR PDB; 7A5F; EM; 4.40 A; M3=1-296. DR PDB; 7A5G; EM; 4.33 A; M3=1-296. DR PDB; 7A5H; EM; 3.30 A; M=1-296. DR PDB; 7A5I; EM; 3.70 A; M3=1-296. DR PDB; 7A5J; EM; 3.10 A; M=1-296. DR PDB; 7A5K; EM; 3.70 A; M3=1-296. DR PDB; 7L08; EM; 3.49 A; M=1-296. DR PDB; 7L20; EM; 3.15 A; M=1-296. DR PDB; 7O9K; EM; 3.10 A; M=1-296. DR PDB; 7O9M; EM; 2.50 A; M=1-296. DR PDB; 7ODR; EM; 2.90 A; M=1-296. DR PDB; 7ODS; EM; 3.10 A; M=1-296. DR PDB; 7ODT; EM; 3.10 A; M=1-296. DR PDB; 7OF0; EM; 2.20 A; M=1-296. DR PDB; 7OF2; EM; 2.70 A; M=1-296. DR PDB; 7OF3; EM; 2.70 A; M=1-296. DR PDB; 7OF4; EM; 2.70 A; M=1-296. DR PDB; 7OF5; EM; 2.90 A; M=1-296. DR PDB; 7OF6; EM; 2.60 A; M=1-296. DR PDB; 7OF7; EM; 2.50 A; M=1-296. DR PDB; 7OG4; EM; 3.80 A; XM=1-296. DR PDB; 7OI6; EM; 5.70 A; M=1-296. DR PDB; 7OI7; EM; 3.50 A; M=1-296. DR PDB; 7OI8; EM; 3.50 A; M=1-296. DR PDB; 7OI9; EM; 3.30 A; M=1-296. DR PDB; 7OIA; EM; 3.20 A; M=1-296. DR PDB; 7OIB; EM; 3.30 A; M=1-296. DR PDB; 7OIC; EM; 3.10 A; M=1-296. DR PDB; 7OID; EM; 3.70 A; M=1-296. DR PDB; 7OIE; EM; 3.50 A; M=1-296. DR PDB; 7PD3; EM; 3.40 A; M=1-296. DR PDB; 7PO4; EM; 2.56 A; M=1-296. DR PDB; 7QH6; EM; 3.08 A; M=1-296. DR PDB; 7QH7; EM; 2.89 A; M=10-296. DR PDB; 7QI4; EM; 2.21 A; M=1-296. DR PDB; 7QI5; EM; 2.63 A; M=1-296. DR PDB; 7QI6; EM; 2.98 A; M=1-296. DR PDB; 8ANY; EM; 2.85 A; M=1-296. DR PDB; 8OIR; EM; 3.10 A; BT=1-296. DR PDB; 8OIT; EM; 2.90 A; BT=1-296. DR PDBsum; 3J7Y; -. DR PDBsum; 3J9M; -. DR PDBsum; 5OOL; -. DR PDBsum; 5OOM; -. DR PDBsum; 6I9R; -. DR PDBsum; 6NU2; -. DR PDBsum; 6NU3; -. DR PDBsum; 6VLZ; -. DR PDBsum; 6VMI; -. DR PDBsum; 6ZM5; -. DR PDBsum; 6ZM6; -. DR PDBsum; 6ZS9; -. DR PDBsum; 6ZSA; -. DR PDBsum; 6ZSB; -. DR PDBsum; 6ZSC; -. DR PDBsum; 6ZSD; -. DR PDBsum; 6ZSE; -. DR PDBsum; 6ZSG; -. DR PDBsum; 7A5F; -. DR PDBsum; 7A5G; -. DR PDBsum; 7A5H; -. DR PDBsum; 7A5I; -. DR PDBsum; 7A5J; -. DR PDBsum; 7A5K; -. DR PDBsum; 7L08; -. DR PDBsum; 7L20; -. DR PDBsum; 7O9K; -. DR PDBsum; 7O9M; -. DR PDBsum; 7ODR; -. DR PDBsum; 7ODS; -. DR PDBsum; 7ODT; -. DR PDBsum; 7OF0; -. DR PDBsum; 7OF2; -. DR PDBsum; 7OF3; -. DR PDBsum; 7OF4; -. DR PDBsum; 7OF5; -. DR PDBsum; 7OF6; -. DR PDBsum; 7OF7; -. DR PDBsum; 7OG4; -. DR PDBsum; 7OI6; -. DR PDBsum; 7OI7; -. DR PDBsum; 7OI8; -. DR PDBsum; 7OI9; -. DR PDBsum; 7OIA; -. DR PDBsum; 7OIB; -. DR PDBsum; 7OIC; -. DR PDBsum; 7OID; -. DR PDBsum; 7OIE; -. DR PDBsum; 7PD3; -. DR PDBsum; 7PO4; -. DR PDBsum; 7QH6; -. DR PDBsum; 7QH7; -. DR PDBsum; 7QI4; -. DR PDBsum; 7QI5; -. DR PDBsum; 7QI6; -. DR PDBsum; 8ANY; -. DR PDBsum; 8OIR; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; Q9P015; -. DR EMDB; EMD-11278; -. DR EMDB; EMD-11279; -. DR EMDB; EMD-11390; -. DR EMDB; EMD-11392; -. DR EMDB; EMD-11393; -. DR EMDB; EMD-11394; -. DR EMDB; EMD-11395; -. DR EMDB; EMD-11397; -. DR EMDB; EMD-12845; -. DR EMDB; EMD-12846; -. DR EMDB; EMD-12847; -. DR EMDB; EMD-13562; -. DR EMDB; EMD-13980; -. DR EMDB; EMD-13981; -. DR EMDB; EMD-13982; -. DR EMDB; EMD-15544; -. DR EMDB; EMD-16897; -. DR EMDB; EMD-16899; -. DR SMR; Q9P015; -. DR BioGRID; 118857; 212. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; Q9P015; -. DR IntAct; Q9P015; 54. DR MINT; Q9P015; -. DR STRING; 9606.ENSP00000260102; -. DR GlyGen; Q9P015; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P015; -. DR PhosphoSitePlus; Q9P015; -. DR SwissPalm; Q9P015; -. DR BioMuta; MRPL15; -. DR DMDM; 74734761; -. DR EPD; Q9P015; -. DR jPOST; Q9P015; -. DR MassIVE; Q9P015; -. DR MaxQB; Q9P015; -. DR PaxDb; 9606-ENSP00000260102; -. DR PeptideAtlas; Q9P015; -. DR ProteomicsDB; 83533; -. DR Pumba; Q9P015; -. DR Antibodypedia; 24498; 217 antibodies from 25 providers. DR DNASU; 29088; -. DR Ensembl; ENST00000260102.9; ENSP00000260102.4; ENSG00000137547.9. DR GeneID; 29088; -. DR KEGG; hsa:29088; -. DR MANE-Select; ENST00000260102.9; ENSP00000260102.4; NM_014175.4; NP_054894.1. DR UCSC; uc003xsa.3; human. DR AGR; HGNC:14054; -. DR CTD; 29088; -. DR GeneCards; MRPL15; -. DR HGNC; HGNC:14054; MRPL15. DR HPA; ENSG00000137547; Tissue enhanced (skeletal muscle, tongue). DR MIM; 611828; gene. DR neXtProt; NX_Q9P015; -. DR OpenTargets; ENSG00000137547; -. DR PharmGKB; PA30944; -. DR VEuPathDB; HostDB:ENSG00000137547; -. DR eggNOG; KOG0846; Eukaryota. DR GeneTree; ENSGT00390000009040; -. DR InParanoid; Q9P015; -. DR OMA; LKRQYPP; -. DR OrthoDB; 166379at2759; -. DR PhylomeDB; Q9P015; -. DR TreeFam; TF105918; -. DR PathwayCommons; Q9P015; -. DR Reactome; R-HSA-5368286; Mitochondrial translation initiation. DR Reactome; R-HSA-5389840; Mitochondrial translation elongation. DR Reactome; R-HSA-5419276; Mitochondrial translation termination. DR SignaLink; Q9P015; -. DR SIGNOR; Q9P015; -. DR BioGRID-ORCS; 29088; 364 hits in 1161 CRISPR screens. DR ChiTaRS; MRPL15; human. DR GeneWiki; MRPL15; -. DR GenomeRNAi; 29088; -. DR Pharos; Q9P015; Tdark. DR PRO; PR:Q9P015; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q9P015; Protein. DR Bgee; ENSG00000137547; Expressed in heart right ventricle and 204 other cell types or tissues. DR ExpressionAtlas; Q9P015; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005762; C:mitochondrial large ribosomal subunit; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEA:Ensembl. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 3.100.10.10; -; 1. DR HAMAP; MF_01341; Ribosomal_uL15; 1. DR InterPro; IPR030878; Ribosomal_uL15. DR InterPro; IPR021131; Ribosomal_uL15/eL18. DR InterPro; IPR036227; Ribosomal_uL15/eL18_sf. DR InterPro; IPR005749; Ribosomal_uL15_bac-type. DR PANTHER; PTHR12934:SF11; 39S RIBOSOMAL PROTEIN L15, MITOCHONDRIAL; 1. DR PANTHER; PTHR12934; 50S RIBOSOMAL PROTEIN L15; 1. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; Ribosomal proteins L15p and L18e; 1. DR Genevisible; Q9P015; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; Transit peptide. FT TRANSIT 1..21 FT /note="Mitochondrion" FT /evidence="ECO:0000250|UniProtKB:Q0VC21" FT CHAIN 22..296 FT /note="Large ribosomal subunit protein uL15m" FT /id="PRO_0000257838" FT REGION 22..66 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 37..58 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT CONFLICT 96 FT /note="L -> M (in Ref. 2; CAB66600 and 3; CAG38562)" FT /evidence="ECO:0000305" FT CONFLICT 137 FT /note="G -> D (in Ref. 2; CAB66600 and 3; CAG38562)" FT /evidence="ECO:0000305" FT HELIX 11..18 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 24..26 FT /evidence="ECO:0007829|PDB:7QH7" FT TURN 31..33 FT /evidence="ECO:0007829|PDB:7QH7" FT TURN 43..45 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 47..50 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 53..55 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 56..59 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:7OI9" FT HELIX 74..77 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:3J7Y" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 92..97 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 98..106 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 108..110 FT /evidence="ECO:0007829|PDB:3J7Y" FT STRAND 112..114 FT /evidence="ECO:0007829|PDB:7QH6" FT HELIX 118..123 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 131..133 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 135..141 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 145..147 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 153..159 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 161..169 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 173..176 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 181..188 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 190..195 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 208..210 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 211..215 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 217..220 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 221..224 FT /evidence="ECO:0007829|PDB:7QH7" FT HELIX 226..228 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 229..240 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 253..257 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 274..276 FT /evidence="ECO:0007829|PDB:7OF0" FT TURN 277..280 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 281..285 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 288..295 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 296 AA; 33420 MW; D7396086F808A72C CRC64; MAGPLQGGGA RALDLLRGLP RVSLANLKPN PGSKKPERRP RGRRRGRKCG RGHKGERQRG TRPRLGFEGG QTPFYIRIPK YGFNEGHSFR RQYKPLSLNR LQYLIDLGRV DPSQPIDLTQ LVNGRGVTIQ PLKRDYGVQL VEEGADTFTA KVNIEVQLAS ELAIAAIEKN GGVVTTAFYD PRSLDIVCKP VPFFLRGQPI PKRMLPPEEL VPYYTDAKNR GYLADPAKFP EARLELARKY GYILPDITKD ELFKMLCTRK DPRQIFFGLA PGWVVNMADK KILKPTDENL LKYYTS //