RM47_HUMAN
ID RM47_HUMAN Reviewed; 250 AA.
AC Q9HD33; Q6XRG1; Q8N5D1;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 04-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=39S ribosomal protein L47, mitochondrial;
DE Short=L47mt;
DE Short=MRP-L47;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL29m {ECO:0000303|PubMed:25278503};
DE AltName: Full=Nasopharyngeal carcinoma metastasis-related protein 1;
DE Flags: Precursor;
GN Name=MRPL47; Synonyms=NCM1; ORFNames=CGI-204;
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 {ECO:0000312|EMBL:AAG01157.1};
RN [1]
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 [2] {ECO:0000305, ECO:0000312|EMBL:AAG01157.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Lymph;
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 [4] {ECO:0000305, ECO:0000312|EMBL:AAG01157.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-250 (ISOFORM 1).
RA Zhu L.P., Jin Y.L.;
RT "Nasopharyngeal carcinoma metastasis-related gene 1.";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 36-250 (ISOFORMS 1/2).
RX PubMed=11342225; DOI=10.1016/s0167-4781(00)00295-5;
RA Lai C.-H., Chiu J.-Y., Lin W.-C.;
RT "Identification of the human crooked neck gene by comparative gene
RT identification.";
RL Biochim. Biophys. Acta 1517:449-454(2001).
RN [6]
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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-144, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9HD33-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HD33-2; Sequence=VSP_035650;
CC Name=3;
CC IsoId=Q9HD33-3; Sequence=VSP_035649;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL29 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG01157.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. Seems to include a portion of the orthologous murine sequence.; Evidence={ECO:0000305};
CC Sequence=AAO92749.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC090425; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471052; EAW78395.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78396.1; -; Genomic_DNA.
DR EMBL; BC021575; AAH21575.1; -; mRNA.
DR EMBL; BC032522; AAH32522.1; -; mRNA.
DR EMBL; AY212270; AAO92749.1; ALT_INIT; mRNA.
DR EMBL; AF285120; AAG01157.1; ALT_SEQ; mRNA.
DR CCDS; CCDS3232.1; -. [Q9HD33-1]
DR CCDS; CCDS3233.1; -. [Q9HD33-3]
DR RefSeq; NP_065142.2; NM_020409.2. [Q9HD33-1]
DR RefSeq; NP_817125.1; NM_177988.1. [Q9HD33-3]
DR PDB; 3J7Y; EM; 3.40 A; Y=1-250.
DR PDB; 3J9M; EM; 3.50 A; Y=1-250.
DR PDB; 5OOL; EM; 3.06 A; Y=1-250.
DR PDB; 5OOM; EM; 3.03 A; Y=1-250.
DR PDB; 6I9R; EM; 3.90 A; Y=1-250.
DR PDB; 6NU2; EM; 3.90 A; Y=63-238.
DR PDB; 6NU3; EM; 4.40 A; Y=1-250.
DR PDB; 6VLZ; EM; 2.97 A; Y=1-250.
DR PDB; 6VMI; EM; 2.96 A; Y=1-250.
DR PDB; 6ZM5; EM; 2.89 A; Y=1-250.
DR PDB; 6ZM6; EM; 2.59 A; Y=1-250.
DR PDB; 6ZS9; EM; 4.00 A; XY=1-250.
DR PDB; 6ZSA; EM; 4.00 A; XY=1-250.
DR PDB; 6ZSB; EM; 4.50 A; XY=1-250.
DR PDB; 6ZSC; EM; 3.50 A; XY=1-250.
DR PDB; 6ZSD; EM; 3.70 A; XY=1-250.
DR PDB; 6ZSE; EM; 5.00 A; XY=1-250.
DR PDB; 6ZSG; EM; 4.00 A; XY=1-250.
DR PDB; 7A5F; EM; 4.40 A; Y3=1-250.
DR PDB; 7A5G; EM; 4.33 A; Y3=1-250.
DR PDB; 7A5H; EM; 3.30 A; Y=1-250.
DR PDB; 7A5I; EM; 3.70 A; Y3=1-250.
DR PDB; 7A5J; EM; 3.10 A; Y=1-250.
DR PDB; 7A5K; EM; 3.70 A; Y3=1-250.
DR PDB; 7L08; EM; 3.49 A; Y=1-250.
DR PDB; 7L20; EM; 3.15 A; Y=1-250.
DR PDB; 7O9K; EM; 3.10 A; Y=1-250.
DR PDB; 7O9M; EM; 2.50 A; Y=1-250.
DR PDB; 7ODR; EM; 2.90 A; Y=1-250.
DR PDB; 7ODS; EM; 3.10 A; Y=1-250.
DR PDB; 7ODT; EM; 3.10 A; Y=1-250.
DR PDB; 7OF0; EM; 2.20 A; Y=1-250.
DR PDB; 7OF2; EM; 2.70 A; Y=1-250.
DR PDB; 7OF3; EM; 2.70 A; Y=1-250.
DR PDB; 7OF4; EM; 2.70 A; Y=1-250.
DR PDB; 7OF5; EM; 2.90 A; Y=1-250.
DR PDB; 7OF6; EM; 2.60 A; Y=1-250.
DR PDB; 7OF7; EM; 2.50 A; Y=1-250.
DR PDB; 7OG4; EM; 3.80 A; XY=1-250.
DR PDB; 7OI6; EM; 5.70 A; Y=1-250.
DR PDB; 7OI7; EM; 3.50 A; Y=1-250.
DR PDB; 7OI8; EM; 3.50 A; Y=1-250.
DR PDB; 7OI9; EM; 3.30 A; Y=1-250.
DR PDB; 7OIA; EM; 3.20 A; Y=1-250.
DR PDB; 7OIB; EM; 3.30 A; Y=1-250.
DR PDB; 7OIC; EM; 3.10 A; Y=1-250.
DR PDB; 7OID; EM; 3.70 A; Y=1-250.
DR PDB; 7OIE; EM; 3.50 A; Y=1-250.
DR PDB; 7PD3; EM; 3.40 A; Y=1-250.
DR PDB; 7QH6; EM; 3.08 A; Y=1-250.
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; Q9HD33; -.
DR SMR; Q9HD33; -.
DR BioGRID; 121392; 194.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9HD33; -.
DR IntAct; Q9HD33; 93.
DR MINT; Q9HD33; -.
DR STRING; 9606.ENSP00000417602; -.
DR iPTMnet; Q9HD33; -.
DR PhosphoSitePlus; Q9HD33; -.
DR BioMuta; MRPL47; -.
DR DMDM; 212276461; -.
DR EPD; Q9HD33; -.
DR jPOST; Q9HD33; -.
DR MassIVE; Q9HD33; -.
DR MaxQB; Q9HD33; -.
DR PaxDb; Q9HD33; -.
DR PeptideAtlas; Q9HD33; -.
DR PRIDE; Q9HD33; -.
DR ProteomicsDB; 81820; -. [Q9HD33-1]
DR ProteomicsDB; 81821; -. [Q9HD33-2]
DR ProteomicsDB; 81822; -. [Q9HD33-3]
DR Antibodypedia; 50126; 78 antibodies from 22 providers.
DR DNASU; 57129; -.
DR Ensembl; ENST00000259038.6; ENSP00000259038.2; ENSG00000136522.14. [Q9HD33-2]
DR Ensembl; ENST00000392659.2; ENSP00000376427.2; ENSG00000136522.14. [Q9HD33-3]
DR Ensembl; ENST00000476781.6; ENSP00000417602.1; ENSG00000136522.14. [Q9HD33-1]
DR GeneID; 57129; -.
DR KEGG; hsa:57129; -.
DR MANE-Select; ENST00000476781.6; ENSP00000417602.1; NM_020409.3; NP_065142.2.
DR UCSC; uc003fjz.5; human. [Q9HD33-1]
DR CTD; 57129; -.
DR DisGeNET; 57129; -.
DR GeneCards; MRPL47; -.
DR HGNC; HGNC:16652; MRPL47.
DR HPA; ENSG00000136522; Low tissue specificity.
DR MIM; 611852; gene.
DR neXtProt; NX_Q9HD33; -.
DR OpenTargets; ENSG00000136522; -.
DR PharmGKB; PA30979; -.
DR VEuPathDB; HostDB:ENSG00000136522; -.
DR eggNOG; KOG3331; Eukaryota.
DR GeneTree; ENSGT00390000002837; -.
DR InParanoid; Q9HD33; -.
DR OMA; LTMEHEC; -.
DR OrthoDB; 1072631at2759; -.
DR PhylomeDB; Q9HD33; -.
DR TreeFam; TF314327; -.
DR PathwayCommons; Q9HD33; -.
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; Q9HD33; -.
DR SIGNOR; Q9HD33; -.
DR BioGRID-ORCS; 57129; 267 hits in 1084 CRISPR screens.
DR ChiTaRS; MRPL47; human.
DR GenomeRNAi; 57129; -.
DR Pharos; Q9HD33; Tbio.
DR PRO; PR:Q9HD33; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9HD33; protein.
DR Bgee; ENSG00000136522; Expressed in left ventricle myocardium and 191 other tissues.
DR Genevisible; Q9HD33; 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:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IBA:GO_Central.
DR Gene3D; 6.10.330.20; -; 1.
DR InterPro; IPR038340; MRP-L47_sf.
DR InterPro; IPR010729; Ribosomal_L47_mit.
DR PANTHER; PTHR21183; PTHR21183; 1.
DR Pfam; PF06984; MRP-L47; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..250
FT /note="39S ribosomal protein L47, mitochondrial"
FT /id="PRO_0000030567"
FT MOD_RES 144
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035649"
FT VAR_SEQ 34..53
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035650"
FT VARIANT 10
FT /note="C -> G (in dbSNP:rs2339844)"
FT /id="VAR_052042"
FT VARIANT 213
FT /note="R -> H (in dbSNP:rs10513762)"
FT /id="VAR_052043"
FT CONFLICT 2..5
FT /note="AAAG -> DATY (in Ref. 4; AAO92749)"
FT /evidence="ECO:0000305"
FT HELIX 64..67
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:7OI9"
FT HELIX 87..91
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 95..122
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 130..158
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 188..190
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 203..205
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 206..237
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 250 AA; 29450 MW; 53EE4FF6E6BF5645 CRC64;
MAAAGLALLC RRVSSALKSS RSLITPQVPA CTGFFLSLLP KSTPNVTSFH QYRLLHTTLS
RKGLEEFFDD PKNWGQEKVK SGAAWTCQQL RNKSNEDLHK LWYVLLKERN MLLTLEQEAK
RQRLPMPSPE RLDKVVDSMD ALDKVVQERE DALRLLQTGQ ERARPGAWRR DIFGRIIWHK
FKQWVIPWHL NKRYNRKRFF ALPYVDHFLR LEREKRARIK ARKENLERKK AKILLKKFPH
LAEAQKSSLV
