ID RM19_HUMAN Reviewed; 292 AA. AC P49406; Q53TX9; Q96Q52; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 04-APR-2006, sequence version 2. DT 27-MAR-2024, entry version 193. DE RecName: Full=Large ribosomal subunit protein bL19m {ECO:0000303|PubMed:25278503}; DE AltName: Full=39S ribosomal protein L15, mitochondrial; DE Short=L15mt; DE Short=MRP-L15; DE AltName: Full=39S ribosomal protein L19, mitochondrial; DE Short=L19mt; DE Short=MRP-L19; DE Flags: Precursor; GN Name=MRPL19; Synonyms=KIAA0104, MRPL15; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-292. RC TISSUE=Bone marrow; RX PubMed=7788527; DOI=10.1093/dnares/2.1.37; RA Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., RA Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. III. The RT coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 2:37-43(1995). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-292, AND SUBCELLULAR LOCATION. 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 [5] RP IDENTIFICATION AS A RIBOSOMAL PROTEIN, AND SUBCELLULAR LOCATION. RX PubMed=10600119; DOI=10.1021/bi991543s; RA Graack H.R., Bryant M.L., O'Brien T.W.; RT "Identification of mammalian mitochondrial ribosomal proteins (MRPs) by N- RT terminal sequencing of purified bovine MRPs and comparison to data bank RT sequences: the large subribosomal particle."; RL Biochemistry 38:16569-16577(1999). RN [6] 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-77, AND IDENTIFICATION BY RP 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 [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). 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 -!- INTERACTION: CC P49406; Q5S007: LRRK2; NbExp=3; IntAct=EBI-1188518, EBI-5323863; CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10600119, CC ECO:0000269|PubMed:11543634, ECO:0000269|PubMed:25278503, CC ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}. CC -!- SIMILARITY: Belongs to the bacterial ribosomal protein bL19 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAY14972.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAA03494.1; Type=Erroneous initiation; Evidence={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; AC005034; AAY14972.1; ALT_INIT; Genomic_DNA. DR EMBL; BC030144; AAH30144.2; -; mRNA. DR EMBL; D14660; BAA03494.1; ALT_INIT; mRNA. DR EMBL; AB051621; BAB54949.1; -; Genomic_DNA. DR CCDS; CCDS1960.2; -. DR RefSeq; NP_055578.2; NM_014763.3. DR PDB; 3J7Y; EM; 3.40 A; Q=1-292. DR PDB; 3J9M; EM; 3.50 A; Q=1-292. DR PDB; 5OOL; EM; 3.06 A; Q=1-292. DR PDB; 5OOM; EM; 3.03 A; Q=1-292. DR PDB; 6I9R; EM; 3.90 A; Q=1-292. DR PDB; 6NU2; EM; 3.90 A; Q=74-292. DR PDB; 6NU3; EM; 4.40 A; Q=74-292. DR PDB; 6VLZ; EM; 2.97 A; Q=1-292. DR PDB; 6VMI; EM; 2.96 A; Q=1-292. DR PDB; 6ZM5; EM; 2.89 A; Q=1-292. DR PDB; 6ZM6; EM; 2.59 A; Q=1-292. DR PDB; 6ZS9; EM; 4.00 A; XQ=1-292. DR PDB; 6ZSA; EM; 4.00 A; XQ=1-292. DR PDB; 6ZSB; EM; 4.50 A; XQ=1-292. DR PDB; 6ZSC; EM; 3.50 A; XQ=1-292. DR PDB; 6ZSD; EM; 3.70 A; XQ=1-292. DR PDB; 6ZSE; EM; 5.00 A; XQ=1-292. DR PDB; 6ZSG; EM; 4.00 A; XQ=1-292. DR PDB; 7A5F; EM; 4.40 A; Q3=1-292. DR PDB; 7A5G; EM; 4.33 A; Q3=1-292. DR PDB; 7A5H; EM; 3.30 A; Q=1-292. DR PDB; 7A5I; EM; 3.70 A; Q3=1-292. DR PDB; 7A5J; EM; 3.10 A; Q=1-292. DR PDB; 7A5K; EM; 3.70 A; Q3=1-292. DR PDB; 7L08; EM; 3.49 A; Q=1-292. DR PDB; 7L20; EM; 3.15 A; Q=1-292. DR PDB; 7O9K; EM; 3.10 A; Q=1-292. DR PDB; 7O9M; EM; 2.50 A; Q=1-292. DR PDB; 7ODR; EM; 2.90 A; Q=1-292. DR PDB; 7ODS; EM; 3.10 A; Q=1-292. DR PDB; 7ODT; EM; 3.10 A; Q=1-292. DR PDB; 7OF0; EM; 2.20 A; Q=1-292. DR PDB; 7OF2; EM; 2.70 A; Q=1-292. DR PDB; 7OF3; EM; 2.70 A; Q=1-292. DR PDB; 7OF4; EM; 2.70 A; Q=1-292. DR PDB; 7OF5; EM; 2.90 A; Q=1-292. DR PDB; 7OF6; EM; 2.60 A; Q=1-292. DR PDB; 7OF7; EM; 2.50 A; Q=1-292. DR PDB; 7OG4; EM; 3.80 A; XQ=1-292. DR PDB; 7OI6; EM; 5.70 A; Q=1-292. DR PDB; 7OI7; EM; 3.50 A; Q=1-292. DR PDB; 7OI8; EM; 3.50 A; Q=1-292. DR PDB; 7OI9; EM; 3.30 A; Q=1-292. DR PDB; 7OIA; EM; 3.20 A; Q=1-292. DR PDB; 7OIB; EM; 3.30 A; Q=1-292. DR PDB; 7OIC; EM; 3.10 A; Q=1-292. DR PDB; 7OID; EM; 3.70 A; Q=1-292. DR PDB; 7OIE; EM; 3.50 A; Q=1-292. DR PDB; 7PD3; EM; 3.40 A; Q=1-292. DR PDB; 7PO4; EM; 2.56 A; Q=1-292. DR PDB; 7QH6; EM; 3.08 A; Q=1-292. DR PDB; 7QH7; EM; 2.89 A; Q=74-290. DR PDB; 7QI4; EM; 2.21 A; Q=1-292. DR PDB; 7QI5; EM; 2.63 A; Q=1-292. DR PDB; 7QI6; EM; 2.98 A; Q=1-292. DR PDB; 8ANY; EM; 2.85 A; Q=1-292. DR PDB; 8OIR; EM; 3.10 A; BX=1-292. DR PDB; 8OIS; EM; 3.00 A; BX=1-292. DR PDB; 8OIT; EM; 2.90 A; BX=1-292. 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; 8OIS; -. DR PDBsum; 8OIT; -. DR AlphaFoldDB; P49406; -. 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-16898; -. DR EMDB; EMD-16899; -. 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; P49406; -. DR BioGRID; 115142; 170. DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit. DR CORUM; P49406; -. DR IntAct; P49406; 46. DR MINT; P49406; -. DR STRING; 9606.ENSP00000377486; -. DR ChEMBL; CHEMBL4295771; -. DR GlyCosmos; P49406; 1 site, 1 glycan. DR GlyGen; P49406; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P49406; -. DR MetOSite; P49406; -. DR PhosphoSitePlus; P49406; -. DR SwissPalm; P49406; -. DR BioMuta; MRPL19; -. DR DMDM; 92090636; -. DR EPD; P49406; -. DR jPOST; P49406; -. DR MassIVE; P49406; -. DR MaxQB; P49406; -. DR PaxDb; 9606-ENSP00000377486; -. DR PeptideAtlas; P49406; -. DR ProteomicsDB; 56000; -. DR Pumba; P49406; -. DR Antibodypedia; 31651; 203 antibodies from 23 providers. DR DNASU; 9801; -. DR Ensembl; ENST00000393909.7; ENSP00000377486.2; ENSG00000115364.14. DR Ensembl; ENST00000409374.5; ENSP00000387284.1; ENSG00000115364.14. DR GeneID; 9801; -. DR KEGG; hsa:9801; -. DR MANE-Select; ENST00000393909.7; ENSP00000377486.2; NM_014763.4; NP_055578.2. DR UCSC; uc002snl.4; human. DR AGR; HGNC:14052; -. DR CTD; 9801; -. DR DisGeNET; 9801; -. DR GeneCards; MRPL19; -. DR HGNC; HGNC:14052; MRPL19. DR HPA; ENSG00000115364; Low tissue specificity. DR MIM; 611832; gene. DR neXtProt; NX_P49406; -. DR OpenTargets; ENSG00000115364; -. DR PharmGKB; PA30948; -. DR VEuPathDB; HostDB:ENSG00000115364; -. DR eggNOG; KOG1698; Eukaryota. DR GeneTree; ENSGT00390000009415; -. DR HOGENOM; CLU_076988_1_0_1; -. DR InParanoid; P49406; -. DR OMA; IHEIQVV; -. DR OrthoDB; 2903970at2759; -. DR PhylomeDB; P49406; -. DR TreeFam; TF320270; -. DR PathwayCommons; P49406; -. 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; P49406; -. DR SIGNOR; P49406; -. DR BioGRID-ORCS; 9801; 274 hits in 1179 CRISPR screens. DR ChiTaRS; MRPL19; human. DR GeneWiki; MRPL19; -. DR GenomeRNAi; 9801; -. DR Pharos; P49406; Tbio. DR PRO; PR:P49406; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P49406; Protein. DR Bgee; ENSG00000115364; Expressed in adrenal tissue and 199 other cell types or tissues. DR ExpressionAtlas; P49406; 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:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0032543; P:mitochondrial translation; NAS:ComplexPortal. DR Gene3D; 2.30.30.790; -; 1. DR InterPro; IPR001857; Ribosomal_bL19. DR InterPro; IPR038657; Ribosomal_bL19_sf. DR InterPro; IPR008991; Translation_prot_SH3-like_sf. DR PANTHER; PTHR15680:SF9; 39S RIBOSOMAL PROTEIN L19, MITOCHONDRIAL; 1. DR PANTHER; PTHR15680; RIBOSOMAL PROTEIN L19; 1. DR Pfam; PF01245; Ribosomal_L19; 1. DR PRINTS; PR00061; RIBOSOMALL19. DR SUPFAM; SSF50104; Translation proteins SH3-like domain; 1. DR Genevisible; P49406; HS. PE 1: Evidence at protein level; KW 3D-structure; Mitochondrion; Phosphoprotein; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Transit peptide. FT TRANSIT 1..? FT /note="Mitochondrion" FT /evidence="ECO:0000255" FT CHAIN ?..292 FT /note="Large ribosomal subunit protein bL19m" FT /id="PRO_0000030473" FT MOD_RES 77 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT HELIX 78..80 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 84..87 FT /evidence="ECO:0007829|PDB:7OIA" FT HELIX 89..103 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 116..141 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 144..146 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 148..155 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 158..165 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 171..178 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 181..185 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 188..191 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 195..197 FT /evidence="ECO:0007829|PDB:7OF0" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:5OOM" FT TURN 236..238 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 245..248 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 251..257 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 258..260 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 263..266 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 269..271 FT /evidence="ECO:0007829|PDB:7OF0" FT HELIX 276..289 FT /evidence="ECO:0007829|PDB:7OF0" SQ SEQUENCE 292 AA; 33535 MW; 4056F39694284A9F CRC64; MAACIAAGHW AAMGLGRSFQ AARTLLPPPA SIACRVHAGP VRQQSTGPSE PGAFQPPPKP VIVDKHRPVE PERRFLSPEF IPRRGRTDPL KFQIERKDML ERRKVLHIPE FYVGSILRVT TADPYASGKI SQFLGICIQR SGRGLGATFI LRNVIEGQGV EICFELYNPR VQEIQVVKLE KRLDDSLLYL RDALPEYSTF DVNMKPVVQE PNQKVPVNEL KVKMKPKPWS KRWERPNFNI KGIRFDLCLT EQQMKEAQKW NQPWLEFDMM REYDTSKIEA AIWKEIEASK RS //