RM16_HUMAN
ID RM16_HUMAN Reviewed; 251 AA.
AC Q9NX20; Q9BYD0; Q9HB70;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=39S ribosomal protein L16, mitochondrial;
DE Short=L16mt;
DE Short=MRP-L16;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL16m {ECO:0000303|PubMed:25278503};
DE Flags: Precursor;
GN Name=MRPL16; ORFNames=PNAS-111;
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].
RX PubMed=11279069; DOI=10.1074/jbc.m100432200;
RA Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA Watanabe K.;
RT "Structural compensation for the deficit of rRNA with proteins in the
RT mammalian mitochondrial ribosome. Systematic analysis of protein components
RT of the large ribosomal subunit from mammalian mitochondria.";
RL J. Biol. Chem. 276:21724-21736(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Pheochromocytoma;
RA Peng Y., Li Y., Tu Y., Xu S., Han Z., Fu G., Chen Z.;
RT "A novel gene expressed in human pheochromocytoma.";
RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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].
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-251.
RC TISSUE=Promyelocytic leukemia;
RA Yu W.-Q., Sun B.-Z., Chai Y.-B., Zhu F., Liu X.-S., Li Z., Lu F., Yan W.,
RA Yang H., Zhao Z.-L.;
RT "Human acute promyelocytic leukemia cell line NB4's apoptosis related
RT genes.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=11551941; DOI=10.1074/jbc.m106510200;
RA Koc E.C., Burkhart W., Blackburn K., Moyer M.B., Schlatzer D.M.,
RA Moseley A., Spremulli L.L.;
RT "The large subunit of the mammalian mitochondrial ribosome. Analysis of the
RT complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:43958-43969(2001).
RN [8]
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 [9]
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 [10] {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 [11] {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 [12] {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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL16 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG23818.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB049642; BAB40847.1; -; mRNA.
DR EMBL; AF183428; AAG09697.1; -; mRNA.
DR EMBL; AK000491; BAA91202.1; -; mRNA.
DR EMBL; CR457117; CAG33398.1; -; mRNA.
DR EMBL; BC001040; AAH01040.1; -; mRNA.
DR EMBL; BC019269; AAH19269.1; -; mRNA.
DR EMBL; AF275806; AAG23818.1; ALT_INIT; mRNA.
DR CCDS; CCDS7976.1; -.
DR RefSeq; NP_060310.1; NM_017840.3.
DR PDB; 3IY9; EM; 14.10 A; I=71-188.
DR PDB; 3J7Y; EM; 3.40 A; N=1-251.
DR PDB; 3J9M; EM; 3.50 A; N=1-251.
DR PDB; 5OOL; EM; 3.06 A; N=1-251.
DR PDB; 5OOM; EM; 3.03 A; N=1-251.
DR PDB; 6I9R; EM; 3.90 A; N=1-251.
DR PDB; 6NU2; EM; 3.90 A; N=47-251.
DR PDB; 6NU3; EM; 4.40 A; N=1-251.
DR PDB; 6VLZ; EM; 2.97 A; N=1-251.
DR PDB; 6VMI; EM; 2.96 A; N=1-251.
DR PDB; 6ZM5; EM; 2.89 A; N=1-251.
DR PDB; 6ZM6; EM; 2.59 A; N=1-251.
DR PDB; 6ZS9; EM; 4.00 A; XN=1-251.
DR PDB; 6ZSA; EM; 4.00 A; XN=1-251.
DR PDB; 6ZSB; EM; 4.50 A; XN=1-251.
DR PDB; 6ZSC; EM; 3.50 A; XN=1-251.
DR PDB; 6ZSD; EM; 3.70 A; XN=1-251.
DR PDB; 6ZSE; EM; 5.00 A; XN=1-251.
DR PDB; 6ZSG; EM; 4.00 A; XN=1-251.
DR PDB; 7A5F; EM; 4.40 A; N3=1-251.
DR PDB; 7A5G; EM; 4.33 A; N3=1-251.
DR PDB; 7A5H; EM; 3.30 A; N=1-251.
DR PDB; 7A5I; EM; 3.70 A; N3=1-251.
DR PDB; 7A5J; EM; 3.10 A; N=1-251.
DR PDB; 7A5K; EM; 3.70 A; N3=1-251.
DR PDB; 7L08; EM; 3.49 A; N=1-251.
DR PDB; 7L20; EM; 3.15 A; N=1-251.
DR PDB; 7O9K; EM; 3.10 A; N=1-251.
DR PDB; 7O9M; EM; 2.50 A; N=1-251.
DR PDB; 7ODR; EM; 2.90 A; N=1-251.
DR PDB; 7ODS; EM; 3.10 A; N=1-251.
DR PDB; 7ODT; EM; 3.10 A; N=1-251.
DR PDB; 7OF0; EM; 2.20 A; N=1-251.
DR PDB; 7OF2; EM; 2.70 A; N=1-251.
DR PDB; 7OF3; EM; 2.70 A; N=1-251.
DR PDB; 7OF4; EM; 2.70 A; N=1-251.
DR PDB; 7OF5; EM; 2.90 A; N=1-251.
DR PDB; 7OF6; EM; 2.60 A; N=1-251.
DR PDB; 7OF7; EM; 2.50 A; N=1-251.
DR PDB; 7OG4; EM; 3.80 A; XN=1-251.
DR PDB; 7OI6; EM; 5.70 A; N=1-251.
DR PDB; 7OI7; EM; 3.50 A; N=1-251.
DR PDB; 7OI8; EM; 3.50 A; N=1-251.
DR PDB; 7OI9; EM; 3.30 A; N=1-251.
DR PDB; 7OIA; EM; 3.20 A; N=1-251.
DR PDB; 7OIB; EM; 3.30 A; N=1-251.
DR PDB; 7OIC; EM; 3.10 A; N=1-251.
DR PDB; 7OID; EM; 3.70 A; N=1-251.
DR PDB; 7OIE; EM; 3.50 A; N=1-251.
DR PDB; 7PD3; EM; 3.40 A; N=1-251.
DR PDB; 7QH6; EM; 3.08 A; N=1-251.
DR PDBsum; 3IY9; -.
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; 7QH6; -.
DR AlphaFoldDB; Q9NX20; -.
DR SMR; Q9NX20; -.
DR BioGRID; 120287; 177.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9NX20; -.
DR IntAct; Q9NX20; 50.
DR MINT; Q9NX20; -.
DR STRING; 9606.ENSP00000300151; -.
DR GlyGen; Q9NX20; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NX20; -.
DR PhosphoSitePlus; Q9NX20; -.
DR SwissPalm; Q9NX20; -.
DR BioMuta; MRPL16; -.
DR DMDM; 74734684; -.
DR EPD; Q9NX20; -.
DR jPOST; Q9NX20; -.
DR MassIVE; Q9NX20; -.
DR MaxQB; Q9NX20; -.
DR PaxDb; Q9NX20; -.
DR PeptideAtlas; Q9NX20; -.
DR PRIDE; Q9NX20; -.
DR ProteomicsDB; 83024; -.
DR TopDownProteomics; Q9NX20; -.
DR Antibodypedia; 52764; 115 antibodies from 20 providers.
DR DNASU; 54948; -.
DR Ensembl; ENST00000300151.5; ENSP00000300151.4; ENSG00000166902.5.
DR GeneID; 54948; -.
DR KEGG; hsa:54948; -.
DR MANE-Select; ENST00000300151.5; ENSP00000300151.4; NM_017840.4; NP_060310.1.
DR UCSC; uc001noh.2; human.
DR CTD; 54948; -.
DR DisGeNET; 54948; -.
DR GeneCards; MRPL16; -.
DR HGNC; HGNC:14476; MRPL16.
DR HPA; ENSG00000166902; Low tissue specificity.
DR MIM; 611829; gene.
DR neXtProt; NX_Q9NX20; -.
DR OpenTargets; ENSG00000166902; -.
DR PharmGKB; PA30945; -.
DR VEuPathDB; HostDB:ENSG00000166902; -.
DR eggNOG; KOG3422; Eukaryota.
DR GeneTree; ENSGT00390000002038; -.
DR HOGENOM; CLU_096518_0_0_1; -.
DR InParanoid; Q9NX20; -.
DR OMA; KMNVNTM; -.
DR OrthoDB; 1420525at2759; -.
DR PhylomeDB; Q9NX20; -.
DR TreeFam; TF312969; -.
DR PathwayCommons; Q9NX20; -.
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; Q9NX20; -.
DR SIGNOR; Q9NX20; -.
DR BioGRID-ORCS; 54948; 421 hits in 1082 CRISPR screens.
DR ChiTaRS; MRPL16; human.
DR GenomeRNAi; 54948; -.
DR Pharos; Q9NX20; Tdark.
DR PRO; PR:Q9NX20; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q9NX20; protein.
DR Bgee; ENSG00000166902; Expressed in apex of heart and 196 other tissues.
DR ExpressionAtlas; Q9NX20; baseline and differential.
DR Genevisible; Q9NX20; HS.
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:0019843; F:rRNA binding; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR CDD; cd01433; Ribosomal_L16_L10e; 1.
DR Gene3D; 3.90.1170.10; -; 1.
DR InterPro; IPR016180; Ribosomal_L10e/L16.
DR InterPro; IPR036920; Ribosomal_L10e/L16_sf.
DR InterPro; IPR000114; Ribosomal_L16.
DR PANTHER; PTHR12220; PTHR12220; 1.
DR Pfam; PF00252; Ribosomal_L16; 1.
DR PRINTS; PR00060; RIBOSOMALL16.
DR SUPFAM; SSF54686; SSF54686; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; Transit peptide.
FT TRANSIT 1..29
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:Q3T0J3"
FT CHAIN 30..251
FT /note="39S ribosomal protein L16, mitochondrial"
FT /id="PRO_0000239841"
FT VARIANT 29
FT /note="G -> S (in dbSNP:rs7122468)"
FT /id="VAR_052006"
FT VARIANT 199
FT /note="R -> Q (in dbSNP:rs12787462)"
FT /id="VAR_052007"
FT VARIANT 207
FT /note="R -> C (in dbSNP:rs491671)"
FT /id="VAR_052008"
FT CONFLICT 15
FT /note="V -> L (in Ref. 1; BAB40847)"
FT /evidence="ECO:0000305"
FT HELIX 69..71
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 99..111
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 119..124
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 159..166
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 169..182
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 215..221
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 232..237
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 251 AA; 28449 MW; 8A42A67DA80A6FEF CRC64;
MWRLLARASA PLLRVPLSDS WALLPASAGV KTLLPVPSFE DVSIPEKPKL RFIERAPLVP
KVRREPKNLS DIRGPSTEAT EFTEGNFAIL ALGGGYLHWG HFEMMRLTIN RSMDPKNMFA
IWRVPAPFKP ITRKSVGHRM GGGKGAIDHY VTPVKAGRLV VEMGGRCEFE EVQGFLDQVA
HKLPFAAKAV SRGTLEKMRK DQEERERNNQ NPWTFERIAT ANMLGIRKVL SPYDLTHKGK
YWGKFYMPKR V
