ID   RM51_HUMAN              Reviewed;         128 AA.
AC   Q4U2R6; Q96Q57; Q9BQ36; Q9P0N7;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   02-OCT-2024, entry version 136.
DE   RecName: Full=Large ribosomal subunit protein mL51 {ECO:0000303|PubMed:25278503};
DE   AltName: Full=39S ribosomal protein L51, mitochondrial;
DE            Short=L51mt;
DE            Short=MRP-L51;
DE   AltName: Full=bMRP-64;
DE            Short=bMRP64;
DE   Flags: Precursor;
GN   Name=MRPL51; Synonyms=MRP64; ORFNames=CDA09, HSPC241;
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=11402041; DOI=10.1074/jbc.m103236200;
RA   Suzuki T., Terasaki M., Takemoto-Hori C., Hanada T., Ueda T., Wada A.,
RA   Watanabe K.;
RT   "Proteomic analysis of the mammalian mitochondrial ribosome. Identification
RT   of protein components in the 28S small subunit.";
RL   J. Biol. Chem. 276:33181-33195(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Pheochromocytoma;
RA   Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.;
RT   "A novel gene expressed in human pheochromocytoma.";
RL   Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Umbilical cord 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, and Testis;
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 42-63.
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.
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   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   [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).
RN   [12] {ECO:0007744|PDB:7QH6, ECO:0007744|PDB:7QH7}
RP   STRUCTURE BY ELECTRON MICROSCOPY (2.9 ANGSTROMS) IN COMPLEX WITH MTLSU, AND
RP   SUBUNIT.
RX   PubMed=35177605; DOI=10.1038/s41467-022-28503-5;
RA   Rebelo-Guiomar P., Pellegrino S., Dent K.C., Sas-Chen A.,
RA   Miller-Fleming L., Garone C., Van Haute L., Rogan J.F., Dinan A.,
RA   Firth A.E., Andrews B., Whitworth A.J., Schwartz S., Warren A.J.,
RA   Minczuk M.;
RT   "A late-stage assembly checkpoint of the human mitochondrial ribosome large
RT   subunit.";
RL   Nat. Commun. 13:929-929(2022).
CC   -!- SUBUNIT: Component of the mitochondrial large ribosomal subunit (mt-
CC       LSU) (PubMed:25278503, PubMed:25838379, PubMed:28892042,
CC       PubMed:35177605). Mature mammalian 55S mitochondrial ribosomes consist
CC       of a small (28S) and a large (39S) subunit. The 28S small subunit
CC       contains a 12S ribosomal RNA (12S mt-rRNA) and 30 different proteins.
CC       The 39S large subunit contains a 16S rRNA (16S mt-rRNA), a copy of
CC       mitochondrial valine transfer RNA (mt-tRNA(Val)), which plays an
CC       integral structural role, and 52 different proteins (PubMed:25278503,
CC       PubMed:25838379). Interacts with OXA1L (By similarity).
CC       {ECO:0000250|UniProtKB:P0C2B6, ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042,
CC       ECO:0000269|PubMed:35177605}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:25278503,
CC       ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
CC   -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC       mL51 family. {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; AB049959; BAB41012.1; -; mRNA.
DR   EMBL; AF212248; AAK14931.1; -; mRNA.
DR   EMBL; AF151075; AAF36161.1; -; mRNA.
DR   EMBL; BC000191; AAH00191.1; -; mRNA.
DR   EMBL; BC014329; AAH14329.1; -; mRNA.
DR   EMBL; AB051355; BAB54944.1; -; Genomic_DNA.
DR   CCDS; CCDS8547.1; -.
DR   RefSeq; NP_057581.2; NM_016497.3.
DR   PDB; 3J7Y; EM; 3.40 A; i=1-128.
DR   PDB; 3J9M; EM; 3.50 A; i=1-128.
DR   PDB; 5OOL; EM; 3.06 A; i=1-128.
DR   PDB; 5OOM; EM; 3.03 A; i=1-128.
DR   PDB; 6I9R; EM; 3.90 A; i=1-128.
DR   PDB; 6NU2; EM; 3.90 A; i=32-128.
DR   PDB; 6NU3; EM; 4.40 A; i=1-128.
DR   PDB; 6VLZ; EM; 2.97 A; i=1-128.
DR   PDB; 6VMI; EM; 2.96 A; i=1-128.
DR   PDB; 6ZM5; EM; 2.89 A; i=1-128.
DR   PDB; 6ZM6; EM; 2.59 A; i=1-128.
DR   PDB; 6ZS9; EM; 4.00 A; i=1-128.
DR   PDB; 6ZSA; EM; 4.00 A; i=1-128.
DR   PDB; 6ZSB; EM; 4.50 A; i=1-128.
DR   PDB; 6ZSC; EM; 3.50 A; i=1-128.
DR   PDB; 6ZSD; EM; 3.70 A; i=1-128.
DR   PDB; 6ZSE; EM; 5.00 A; i=1-128.
DR   PDB; 6ZSG; EM; 4.00 A; i=1-128.
DR   PDB; 7A5F; EM; 4.40 A; i3=1-128.
DR   PDB; 7A5G; EM; 4.33 A; i3=1-128.
DR   PDB; 7A5H; EM; 3.30 A; i=1-128.
DR   PDB; 7A5I; EM; 3.70 A; i3=1-128.
DR   PDB; 7A5J; EM; 3.10 A; i=1-128.
DR   PDB; 7A5K; EM; 3.70 A; i3=1-128.
DR   PDB; 7L08; EM; 3.49 A; i=1-128.
DR   PDB; 7L20; EM; 3.15 A; i=1-128.
DR   PDB; 7O9K; EM; 3.10 A; i=1-128.
DR   PDB; 7O9M; EM; 2.50 A; i=1-128.
DR   PDB; 7ODR; EM; 2.90 A; i=1-128.
DR   PDB; 7ODS; EM; 3.10 A; i=1-128.
DR   PDB; 7ODT; EM; 3.10 A; i=1-128.
DR   PDB; 7OF0; EM; 2.20 A; i=1-128.
DR   PDB; 7OF2; EM; 2.70 A; i=1-128.
DR   PDB; 7OF3; EM; 2.70 A; i=1-128.
DR   PDB; 7OF4; EM; 2.70 A; i=1-128.
DR   PDB; 7OF5; EM; 2.90 A; i=1-128.
DR   PDB; 7OF6; EM; 2.60 A; i=1-128.
DR   PDB; 7OF7; EM; 2.50 A; i=1-128.
DR   PDB; 7OG4; EM; 3.80 A; i=1-128.
DR   PDB; 7OI6; EM; 5.70 A; i=1-128.
DR   PDB; 7OI7; EM; 3.50 A; i=1-128.
DR   PDB; 7OI8; EM; 3.50 A; i=1-128.
DR   PDB; 7OI9; EM; 3.30 A; i=1-128.
DR   PDB; 7OIA; EM; 3.20 A; i=1-128.
DR   PDB; 7OIB; EM; 3.30 A; i=1-128.
DR   PDB; 7OIC; EM; 3.10 A; i=1-128.
DR   PDB; 7OID; EM; 3.70 A; i=1-128.
DR   PDB; 7OIE; EM; 3.50 A; i=1-128.
DR   PDB; 7PD3; EM; 3.40 A; i=1-128.
DR   PDB; 7PO4; EM; 2.56 A; i=1-128.
DR   PDB; 7QH6; EM; 3.08 A; i=1-128.
DR   PDB; 7QH7; EM; 2.89 A; i=32-128.
DR   PDB; 7QI4; EM; 2.21 A; i=1-128.
DR   PDB; 7QI5; EM; 2.63 A; i=1-128.
DR   PDB; 7QI6; EM; 2.98 A; i=1-128.
DR   PDB; 8ANY; EM; 2.85 A; i=1-128.
DR   PDB; 8OIR; EM; 3.10 A; Bz=1-128.
DR   PDB; 8OIT; EM; 2.90 A; Bz=1-128.
DR   PDB; 8PK0; EM; 3.03 A; i=1-128.
DR   PDB; 8QSJ; EM; 3.00 A; i=1-128.
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   PDBsum; 8PK0; -.
DR   PDBsum; 8QSJ; -.
DR   AlphaFoldDB; Q4U2R6; -.
DR   EMDB; EMD-0514; -.
DR   EMDB; EMD-0515; -.
DR   EMDB; EMD-11278; -.
DR   EMDB; EMD-11279; -.
DR   EMDB; EMD-11390; -.
DR   EMDB; EMD-11391; -.
DR   EMDB; EMD-11392; -.
DR   EMDB; EMD-11393; -.
DR   EMDB; EMD-11394; -.
DR   EMDB; EMD-11395; -.
DR   EMDB; EMD-11397; -.
DR   EMDB; EMD-11641; -.
DR   EMDB; EMD-11642; -.
DR   EMDB; EMD-11643; -.
DR   EMDB; EMD-11644; -.
DR   EMDB; EMD-11645; -.
DR   EMDB; EMD-11646; -.
DR   EMDB; EMD-12763; -.
DR   EMDB; EMD-12764; -.
DR   EMDB; EMD-12845; -.
DR   EMDB; EMD-12846; -.
DR   EMDB; EMD-12847; -.
DR   EMDB; EMD-12865; -.
DR   EMDB; EMD-12867; -.
DR   EMDB; EMD-12868; -.
DR   EMDB; EMD-12869; -.
DR   EMDB; EMD-12870; -.
DR   EMDB; EMD-12871; -.
DR   EMDB; EMD-12872; -.
DR   EMDB; EMD-12877; -.
DR   EMDB; EMD-12919; -.
DR   EMDB; EMD-12920; -.
DR   EMDB; EMD-12921; -.
DR   EMDB; EMD-12922; -.
DR   EMDB; EMD-12923; -.
DR   EMDB; EMD-12924; -.
DR   EMDB; EMD-12925; -.
DR   EMDB; EMD-12926; -.
DR   EMDB; EMD-12927; -.
DR   EMDB; EMD-13329; -.
DR   EMDB; EMD-13562; -.
DR   EMDB; EMD-13965; -.
DR   EMDB; EMD-13967; -.
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   EMDB; EMD-17719; -.
DR   EMDB; EMD-21233; -.
DR   EMDB; EMD-21242; -.
DR   EMDB; EMD-23096; -.
DR   EMDB; EMD-23121; -.
DR   EMDB; EMD-3842; -.
DR   EMDB; EMD-3843; -.
DR   EMDB; EMD-4434; -.
DR   SMR; Q4U2R6; -.
DR   BioGRID; 119414; 145.
DR   ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR   CORUM; Q4U2R6; -.
DR   IntAct; Q4U2R6; 102.
DR   MINT; Q4U2R6; -.
DR   STRING; 9606.ENSP00000229238; -.
DR   BioMuta; MRPL51; -.
DR   DMDM; 74762954; -.
DR   jPOST; Q4U2R6; -.
DR   MassIVE; Q4U2R6; -.
DR   PaxDb; 9606-ENSP00000229238; -.
DR   PeptideAtlas; Q4U2R6; -.
DR   ProteomicsDB; 62262; -.
DR   Pumba; Q4U2R6; -.
DR   TopDownProteomics; Q4U2R6; -.
DR   Antibodypedia; 22416; 182 antibodies from 24 providers.
DR   DNASU; 51258; -.
DR   Ensembl; ENST00000229238.5; ENSP00000229238.3; ENSG00000111639.8.
DR   GeneID; 51258; -.
DR   KEGG; hsa:51258; -.
DR   MANE-Select; ENST00000229238.5; ENSP00000229238.3; NM_016497.4; NP_057581.2.
DR   UCSC; uc001qom.3; human.
DR   AGR; HGNC:14044; -.
DR   CTD; 51258; -.
DR   GeneCards; MRPL51; -.
DR   HGNC; HGNC:14044; MRPL51.
DR   HPA; ENSG00000111639; Low tissue specificity.
DR   MIM; 611855; gene.
DR   neXtProt; NX_Q4U2R6; -.
DR   OpenTargets; ENSG00000111639; -.
DR   PharmGKB; PA30984; -.
DR   VEuPathDB; HostDB:ENSG00000111639; -.
DR   eggNOG; KOG4045; Eukaryota.
DR   GeneTree; ENSGT00390000018821; -.
DR   HOGENOM; CLU_150741_0_0_1; -.
DR   InParanoid; Q4U2R6; -.
DR   OMA; VRMHAIP; -.
DR   OrthoDB; 3121045at2759; -.
DR   PhylomeDB; Q4U2R6; -.
DR   TreeFam; TF106130; -.
DR   PathwayCommons; Q4U2R6; -.
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; Q4U2R6; -.
DR   SIGNOR; Q4U2R6; -.
DR   BioGRID-ORCS; 51258; 265 hits in 1162 CRISPR screens.
DR   ChiTaRS; MRPL51; human.
DR   EvolutionaryTrace; Q4U2R6; -.
DR   GenomeRNAi; 51258; -.
DR   Pharos; Q4U2R6; Tdark.
DR   PRO; PR:Q4U2R6; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q4U2R6; protein.
DR   Bgee; ENSG00000111639; Expressed in left ventricle myocardium and 185 other cell types or tissues.
DR   ExpressionAtlas; Q4U2R6; 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:0005761; C:mitochondrial ribosome; IDA:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0003735; F:structural constituent of ribosome; ISS:UniProtKB.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0006412; P:translation; ISS:UniProtKB.
DR   InterPro; IPR019373; Ribosomal_mL51.
DR   PANTHER; PTHR13409:SF0; 39S RIBOSOMAL PROTEIN L51, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13409; MITOCHONDRIAL 39S RIBOSOMAL PROTEIN L51; 1.
DR   Pfam; PF10244; MRP-L51; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Mitochondrion; Proteomics identification; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT   TRANSIT         1..31
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..128
FT                   /note="Large ribosomal subunit protein mL51"
FT                   /id="PRO_0000273082"
FT   VARIANT         102
FT                   /note="M -> I (in dbSNP:rs9526)"
FT                   /id="VAR_030079"
FT   CONFLICT        79
FT                   /note="W -> R (in Ref. 3; AAF36161)"
FT                   /evidence="ECO:0000305"
FT   HELIX           49..52
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            53..59
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           60..63
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   TURN            64..66
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           70..73
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           78..80
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           87..98
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           99..101
FT                   /evidence="ECO:0007829|PDB:7OF0"
FT   HELIX           104..123
FT                   /evidence="ECO:0007829|PDB:7OF0"
SQ   SEQUENCE   128 AA;  15095 MW;  9DB4720D5B387A5D CRC64;
     MAGNLLSGAG RRLWDWVPLA CRSFSLGVPR LIGIRLTLPP PKVVDRWNEK RAMFGVYDNI
     GILGNFEKHP KELIRGPIWL RGWKGNELQR CIRKRKMVGS RMFADDLHNL NKRIRYLYKH
     FNRHGKFR
//