RM46_HUMAN
ID RM46_HUMAN Reviewed; 279 AA.
AC Q9H2W6; B2RD75; Q9HBU8;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=39S ribosomal protein L46, mitochondrial;
DE Short=L46mt;
DE Short=MRP-L46;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL46 {ECO:0000303|PubMed:25278503};
DE AltName: Full=P2ECSL;
DE Flags: Precursor;
GN Name=MRPL46; Synonyms=C15orf4, LIECG2;
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:AAG43507.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11761714; DOI=10.3109/10425170109047561;
RA Carim-Todd L., Sumoy L., Andreu N., Estivill X., Escarceller M.;
RT "Cloning, mapping and expression analysis of C15orf4, a novel human gene
RT with homology to the yeast mitochondrial ribosomal protein Ym130 gene.";
RL DNA Seq. 12:91-96(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAG43507.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zhang K.M., Chen B.S.;
RT "A novel gene identified in vascular endothelial cells.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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] {ECO:0000305, ECO:0000312|EMBL:AAG43507.1}
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 IDENTIFICATION, AND SUBUNIT.
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-230, 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].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
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 [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. mL46 is located at the central protuberance.
CC {ECO:0000269|PubMed:11551941, 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 mitochondrion-specific ribosomal protein
CC mL46 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG33698.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF210056; AAG43507.1; -; mRNA.
DR EMBL; AF205435; AAG33698.1; ALT_INIT; mRNA.
DR EMBL; AK315434; BAG37822.1; -; mRNA.
DR EMBL; CH471101; EAX01995.1; -; Genomic_DNA.
DR EMBL; BC017883; AAH17883.1; -; mRNA.
DR CCDS; CCDS10341.1; -.
DR RefSeq; NP_071446.2; NM_022163.3.
DR PDB; 3J7Y; EM; 3.40 A; e=1-279.
DR PDB; 3J9M; EM; 3.50 A; e=1-279.
DR PDB; 5OOL; EM; 3.06 A; e=1-279.
DR PDB; 5OOM; EM; 3.03 A; e=1-279.
DR PDB; 6I9R; EM; 3.90 A; e=1-279.
DR PDB; 6NU2; EM; 3.90 A; e=43-279.
DR PDB; 6NU3; EM; 4.40 A; e=1-279.
DR PDB; 6VLZ; EM; 2.97 A; e=1-279.
DR PDB; 6VMI; EM; 2.96 A; e=1-279.
DR PDB; 6ZM5; EM; 2.89 A; e=1-279.
DR PDB; 6ZM6; EM; 2.59 A; e=1-279.
DR PDB; 6ZS9; EM; 4.00 A; e=1-279.
DR PDB; 6ZSA; EM; 4.00 A; e=1-279.
DR PDB; 6ZSB; EM; 4.50 A; e=1-279.
DR PDB; 6ZSC; EM; 3.50 A; e=1-279.
DR PDB; 6ZSD; EM; 3.70 A; e=1-279.
DR PDB; 6ZSE; EM; 5.00 A; e=1-279.
DR PDB; 6ZSG; EM; 4.00 A; e=1-279.
DR PDB; 7A5F; EM; 4.40 A; e3=1-279.
DR PDB; 7A5G; EM; 4.33 A; e3=1-279.
DR PDB; 7A5H; EM; 3.30 A; e=1-279.
DR PDB; 7A5I; EM; 3.70 A; e3=1-279.
DR PDB; 7A5J; EM; 3.10 A; e=1-279.
DR PDB; 7A5K; EM; 3.70 A; e3=1-279.
DR PDB; 7L08; EM; 3.49 A; e=1-279.
DR PDB; 7L20; EM; 3.15 A; e=1-279.
DR PDB; 7O9K; EM; 3.10 A; e=1-279.
DR PDB; 7O9M; EM; 2.50 A; e=1-279.
DR PDB; 7ODR; EM; 2.90 A; e=1-279.
DR PDB; 7ODS; EM; 3.10 A; e=1-279.
DR PDB; 7ODT; EM; 3.10 A; e=1-279.
DR PDB; 7OF0; EM; 2.20 A; e=1-279.
DR PDB; 7OF2; EM; 2.70 A; e=1-279.
DR PDB; 7OF3; EM; 2.70 A; e=1-279.
DR PDB; 7OF4; EM; 2.70 A; e=1-279.
DR PDB; 7OF5; EM; 2.90 A; e=1-279.
DR PDB; 7OF6; EM; 2.60 A; e=1-279.
DR PDB; 7OF7; EM; 2.50 A; e=1-279.
DR PDB; 7OG4; EM; 3.80 A; e=1-279.
DR PDB; 7OI7; EM; 3.50 A; e=1-279.
DR PDB; 7OI8; EM; 3.50 A; e=1-279.
DR PDB; 7OI9; EM; 3.30 A; e=1-279.
DR PDB; 7OIA; EM; 3.20 A; e=1-279.
DR PDB; 7OIB; EM; 3.30 A; e=1-279.
DR PDB; 7OIC; EM; 3.10 A; e=1-279.
DR PDB; 7OID; EM; 3.70 A; e=1-279.
DR PDB; 7OIE; EM; 3.50 A; e=1-279.
DR PDB; 7PD3; EM; 3.40 A; e=1-279.
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; 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 AlphaFoldDB; Q9H2W6; -.
DR SMR; Q9H2W6; -.
DR BioGRID; 117757; 179.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9H2W6; -.
DR IntAct; Q9H2W6; 44.
DR MINT; Q9H2W6; -.
DR STRING; 9606.ENSP00000312311; -.
DR GlyGen; Q9H2W6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H2W6; -.
DR MetOSite; Q9H2W6; -.
DR PhosphoSitePlus; Q9H2W6; -.
DR SwissPalm; Q9H2W6; -.
DR BioMuta; MRPL46; -.
DR DMDM; 52783325; -.
DR EPD; Q9H2W6; -.
DR jPOST; Q9H2W6; -.
DR MassIVE; Q9H2W6; -.
DR MaxQB; Q9H2W6; -.
DR PaxDb; Q9H2W6; -.
DR PeptideAtlas; Q9H2W6; -.
DR PRIDE; Q9H2W6; -.
DR ProteomicsDB; 80610; -.
DR Antibodypedia; 58578; 193 antibodies from 27 providers.
DR DNASU; 26589; -.
DR Ensembl; ENST00000312475.5; ENSP00000312311.4; ENSG00000259494.2.
DR GeneID; 26589; -.
DR KEGG; hsa:26589; -.
DR MANE-Select; ENST00000312475.5; ENSP00000312311.4; NM_022163.4; NP_071446.2.
DR UCSC; uc002bmj.3; human.
DR CTD; 26589; -.
DR DisGeNET; 26589; -.
DR GeneCards; MRPL46; -.
DR HGNC; HGNC:1192; MRPL46.
DR HPA; ENSG00000259494; Low tissue specificity.
DR MIM; 611851; gene.
DR neXtProt; NX_Q9H2W6; -.
DR PharmGKB; PA30978; -.
DR VEuPathDB; HostDB:ENSG00000259494; -.
DR eggNOG; KOG4548; Eukaryota.
DR GeneTree; ENSGT00390000015400; -.
DR HOGENOM; CLU_079736_1_0_1; -.
DR InParanoid; Q9H2W6; -.
DR OMA; NNMEAKF; -.
DR OrthoDB; 1527405at2759; -.
DR PhylomeDB; Q9H2W6; -.
DR PathwayCommons; Q9H2W6; -.
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; Q9H2W6; -.
DR SIGNOR; Q9H2W6; -.
DR BioGRID-ORCS; 26589; 321 hits in 1087 CRISPR screens.
DR ChiTaRS; MRPL46; human.
DR GenomeRNAi; 26589; -.
DR Pharos; Q9H2W6; Tdark.
DR PRO; PR:Q9H2W6; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q9H2W6; protein.
DR Bgee; ENSG00000259494; Expressed in adrenal tissue and 97 other tissues.
DR ExpressionAtlas; Q9H2W6; baseline and differential.
DR Genevisible; Q9H2W6; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR CDD; cd04661; MRP_L46; 1.
DR InterPro; IPR033650; MRP_L46_NUDIX.
DR InterPro; IPR040008; MRPL46.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR021757; Ribosomal_L46_N.
DR PANTHER; PTHR13124; PTHR13124; 1.
DR Pfam; PF11788; MRP-L46; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Mitochondrion; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..279
FT /note="39S ribosomal protein L46, mitochondrial"
FT /id="PRO_0000030576"
FT MOD_RES 230
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VARIANT 106
FT /note="H -> Y (in dbSNP:rs16941888)"
FT /id="VAR_052046"
FT CONFLICT 197
FT /note="E -> K (in Ref. 2; AAG33698)"
FT /evidence="ECO:0000305"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 52..55
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 65..81
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 92..103
FT /evidence="ECO:0007829|PDB:5OOM"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 140..142
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 149..151
FT /evidence="ECO:0007829|PDB:7OI7"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:7OIA"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:3J7Y"
FT STRAND 228..233
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 245..247
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 252..255
FT /evidence="ECO:0007829|PDB:3J7Y"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 279 AA; 31705 MW; EDA966D758715378 CRC64;
MAAPVRRTLL GVAGGWRRFE RLWAGSLSSR SLALAAAPSS NGSPWRLLGA LCLQRPPVVS
KPLTPLQEEM ASLLQQIEIE RSLYSDHELR ALDENQRLAK KKADLHDEED EQDILLAQDL
EDMWEQKFLQ FKLGARITEA DEKNDRTSLN RKLDRNLVLL VREKFGDQDV WILPQAEWQP
GETLRGTAER TLATLSENNM EAKFLGNAPC GHYTFKFPQA MRTESNLGAK VFFFKALLLT
GDFSQAGNKG HHVWVTKDEL GDYLKPKYLA QVRRFVSDL
