RM04_HUMAN
ID RM04_HUMAN Reviewed; 311 AA.
AC Q9BYD3; A6NNV7; Q9BW07; Q9H4N2; Q9Y317;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=39S ribosomal protein L4, mitochondrial;
DE Short=L4mt;
DE Short=MRP-L4;
DE AltName: Full=Mitochondrial large ribosomal subunit protein uL4m {ECO:0000303|PubMed:25278503};
GN Name=MRPL4; ORFNames=CDABP0091, CGI-28;
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).
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung, and Ovary;
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 20-311 (ISOFORM 1).
RC TISSUE=Leukemia;
RA Zhou J., Yu W., Tang H., Mei G., Tsang Y.T.M., Bouck J., Gibbs R.A.,
RA Margolin J.F.;
RT "Pediatric leukemia cDNA sequencing project.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-147, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
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]
RP INTERACTION WITH MIEF1 UPSTREAM OPEN READING FRAME PROTEIN.
RX PubMed=30215512; DOI=10.1021/acs.biochem.8b00726;
RA Rathore A., Chu Q., Tan D., Martinez T.F., Donaldson C.J., Diedrich J.K.,
RA Yates J.R. III, Saghatelian A.;
RT "MIEF1 microprotein regulates mitochondrial translation.";
RL Biochemistry 57:5564-5575(2018).
RN [11] {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 [12] {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 [13] {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. Interacts with MIEF1 upstream open reading frame
CC protein (PubMed:30215512). {ECO:0000269|PubMed:25278503,
CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042,
CC ECO:0000269|PubMed:30215512}.
CC -!- INTERACTION:
CC Q9BYD3; P49760: CLK2; NbExp=3; IntAct=EBI-721368, EBI-750020;
CC Q9BYD3; Q99732: LITAF; NbExp=3; IntAct=EBI-721368, EBI-725647;
CC Q9BYD3; P36406: TRIM23; NbExp=3; IntAct=EBI-721368, EBI-740098;
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=2;
CC Name=1; Synonyms=isoform a;
CC IsoId=Q9BYD3-1; Sequence=Displayed;
CC Name=2; Synonyms=isoform b;
CC IsoId=Q9BYD3-2; Sequence=VSP_019027, VSP_019028;
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL4 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27737.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAG02005.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB049635; BAB40840.1; -; mRNA.
DR EMBL; AF132962; AAD27737.1; ALT_FRAME; mRNA.
DR EMBL; AC011511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84083.1; -; Genomic_DNA.
DR EMBL; BC000756; AAH00756.1; -; mRNA.
DR EMBL; BC009858; AAH09858.1; -; mRNA.
DR EMBL; AY007152; AAG02005.1; ALT_INIT; mRNA.
DR CCDS; CCDS12230.1; -. [Q9BYD3-1]
DR CCDS; CCDS42499.1; -. [Q9BYD3-2]
DR RefSeq; NP_057040.2; NM_015956.2. [Q9BYD3-1]
DR RefSeq; NP_666499.1; NM_146387.1. [Q9BYD3-1]
DR RefSeq; NP_666500.1; NM_146388.1. [Q9BYD3-2]
DR PDB; 3IY9; EM; 14.10 A; D=97-271.
DR PDB; 3J7Y; EM; 3.40 A; F=1-311.
DR PDB; 3J9M; EM; 3.50 A; F=1-311.
DR PDB; 5OOL; EM; 3.06 A; F=1-311.
DR PDB; 5OOM; EM; 3.03 A; F=1-311.
DR PDB; 6I9R; EM; 3.90 A; F=1-311.
DR PDB; 6NU2; EM; 3.90 A; F=45-294.
DR PDB; 6NU3; EM; 4.40 A; F=1-311.
DR PDB; 6VLZ; EM; 2.97 A; F=1-311.
DR PDB; 6VMI; EM; 2.96 A; F=1-311.
DR PDB; 6ZM5; EM; 2.89 A; F=1-311.
DR PDB; 6ZM6; EM; 2.59 A; F=1-311.
DR PDB; 6ZS9; EM; 4.00 A; XF=1-311.
DR PDB; 6ZSA; EM; 4.00 A; XF=1-311.
DR PDB; 6ZSB; EM; 4.50 A; XF=1-311.
DR PDB; 6ZSC; EM; 3.50 A; XF=1-311.
DR PDB; 6ZSD; EM; 3.70 A; XF=1-311.
DR PDB; 6ZSE; EM; 5.00 A; XF=1-311.
DR PDB; 6ZSG; EM; 4.00 A; XF=1-311.
DR PDB; 7A5F; EM; 4.40 A; F3=1-311.
DR PDB; 7A5G; EM; 4.33 A; F3=1-311.
DR PDB; 7A5H; EM; 3.30 A; F=1-311.
DR PDB; 7A5I; EM; 3.70 A; F3=1-311.
DR PDB; 7A5J; EM; 3.10 A; F=1-311.
DR PDB; 7A5K; EM; 3.70 A; F3=1-311.
DR PDB; 7L08; EM; 3.49 A; F=1-311.
DR PDB; 7L20; EM; 3.15 A; F=1-311.
DR PDB; 7O9K; EM; 3.10 A; F=1-311.
DR PDB; 7O9M; EM; 2.50 A; F=1-311.
DR PDB; 7ODR; EM; 2.90 A; F=1-311.
DR PDB; 7ODS; EM; 3.10 A; F=1-311.
DR PDB; 7ODT; EM; 3.10 A; F=1-311.
DR PDB; 7OF0; EM; 2.20 A; F=1-311.
DR PDB; 7OF2; EM; 2.70 A; F=1-311.
DR PDB; 7OF3; EM; 2.70 A; F=1-311.
DR PDB; 7OF4; EM; 2.70 A; F=1-311.
DR PDB; 7OF5; EM; 2.90 A; F=1-311.
DR PDB; 7OF6; EM; 2.60 A; F=1-311.
DR PDB; 7OF7; EM; 2.50 A; F=1-311.
DR PDB; 7OG4; EM; 3.80 A; XF=1-311.
DR PDB; 7OI6; EM; 5.70 A; F=1-311.
DR PDB; 7OI7; EM; 3.50 A; F=1-311.
DR PDB; 7OI8; EM; 3.50 A; F=1-311.
DR PDB; 7OI9; EM; 3.30 A; F=1-311.
DR PDB; 7OIA; EM; 3.20 A; F=1-311.
DR PDB; 7OIB; EM; 3.30 A; F=1-311.
DR PDB; 7OIC; EM; 3.10 A; F=1-311.
DR PDB; 7OID; EM; 3.70 A; F=1-311.
DR PDB; 7OIE; EM; 3.50 A; F=1-311.
DR PDB; 7PD3; EM; 3.40 A; F=1-311.
DR PDB; 7QH6; EM; 3.08 A; F=1-311.
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; Q9BYD3; -.
DR SMR; Q9BYD3; -.
DR BioGRID; 119264; 262.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9BYD3; -.
DR IntAct; Q9BYD3; 122.
DR MINT; Q9BYD3; -.
DR STRING; 9606.ENSP00000253099; -.
DR GlyGen; Q9BYD3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BYD3; -.
DR PhosphoSitePlus; Q9BYD3; -.
DR BioMuta; MRPL4; -.
DR DMDM; 74733471; -.
DR EPD; Q9BYD3; -.
DR jPOST; Q9BYD3; -.
DR MassIVE; Q9BYD3; -.
DR MaxQB; Q9BYD3; -.
DR PaxDb; Q9BYD3; -.
DR PeptideAtlas; Q9BYD3; -.
DR PRIDE; Q9BYD3; -.
DR ProteomicsDB; 79617; -. [Q9BYD3-1]
DR ProteomicsDB; 79618; -. [Q9BYD3-2]
DR Antibodypedia; 25237; 97 antibodies from 25 providers.
DR DNASU; 51073; -.
DR Ensembl; ENST00000253099.11; ENSP00000253099.5; ENSG00000105364.14. [Q9BYD3-1]
DR Ensembl; ENST00000307422.9; ENSP00000306902.5; ENSG00000105364.14. [Q9BYD3-1]
DR Ensembl; ENST00000590669.5; ENSP00000465143.1; ENSG00000105364.14. [Q9BYD3-2]
DR GeneID; 51073; -.
DR KEGG; hsa:51073; -.
DR MANE-Select; ENST00000253099.11; ENSP00000253099.5; NM_015956.3; NP_057040.2.
DR UCSC; uc002mnm.4; human. [Q9BYD3-1]
DR CTD; 51073; -.
DR DisGeNET; 51073; -.
DR GeneCards; MRPL4; -.
DR HGNC; HGNC:14276; MRPL4.
DR HPA; ENSG00000105364; Low tissue specificity.
DR MIM; 611823; gene.
DR neXtProt; NX_Q9BYD3; -.
DR OpenTargets; ENSG00000105364; -.
DR PharmGKB; PA30971; -.
DR VEuPathDB; HostDB:ENSG00000105364; -.
DR eggNOG; KOG1624; Eukaryota.
DR GeneTree; ENSGT00390000014512; -.
DR InParanoid; Q9BYD3; -.
DR OMA; PQVHILE; -.
DR PhylomeDB; Q9BYD3; -.
DR TreeFam; TF313913; -.
DR PathwayCommons; Q9BYD3; -.
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; Q9BYD3; -.
DR SIGNOR; Q9BYD3; -.
DR BioGRID-ORCS; 51073; 514 hits in 1081 CRISPR screens.
DR ChiTaRS; MRPL4; human.
DR GeneWiki; MRPL4; -.
DR GenomeRNAi; 51073; -.
DR Pharos; Q9BYD3; Tdark.
DR PRO; PR:Q9BYD3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9BYD3; protein.
DR Bgee; ENSG00000105364; Expressed in apex of heart and 194 other tissues.
DR ExpressionAtlas; Q9BYD3; baseline and differential.
DR Genevisible; Q9BYD3; 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:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR Gene3D; 3.40.1370.10; -; 1.
DR HAMAP; MF_01328_B; Ribosomal_L4_B; 1.
DR InterPro; IPR002136; Ribosomal_L4/L1e.
DR InterPro; IPR023574; Ribosomal_L4_dom_sf.
DR InterPro; IPR013005; Ribosomal_uL4/L1e.
DR PANTHER; PTHR10746; PTHR10746; 1.
DR Pfam; PF00573; Ribosomal_L4; 1.
DR SUPFAM; SSF52166; SSF52166; 1.
DR TIGRFAMs; TIGR03953; rplD_bact; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Methylation; Mitochondrion;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1..311
FT /note="39S ribosomal protein L4, mitochondrial"
FT /id="PRO_0000238949"
FT REGION 118..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 147
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 248..263
FT /note="LNVHSMLKHQTLVLTL -> EQRAQAPRVRMCRLRC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019027"
FT VAR_SEQ 264..311
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019028"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 93..106
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 130..135
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:7OIB"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7OI8"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 167..183
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 200..209
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 228..235
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 245..247
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 250..255
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 256..262
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:7OIA"
SQ SEQUENCE 311 AA; 34919 MW; 8267C61C42BFCF07 CRC64;
MLQFVRAGAR AWLRPTGSQG LSSLAEEAAR ATENPEQVAS EGLPEPVLRK VELPVPTHRR
PVQAWVESLR GFEQERVGLA DLHPDVFATA PRLDILHQVA MWQKNFKRIS YAKTKTRAEV
RGGGRKPWPQ KGTGRARHGS IRSPLWRGGG VAHGPRGPTS YYYMLPMKVR ALGLKVALTV
KLAQDDLHIM DSLELPTGDP QYLTELAHYR RWGDSVLLVD LTHEEMPQSI VEATSRLKTF
NLIPAVGLNV HSMLKHQTLV LTLPTVAFLE DKLLWQDSRY RPLYPFSLPY SDFPRPLPHA
TQGPAATPYH C
