RT30_HUMAN
ID RT30_HUMAN Reviewed; 439 AA.
AC Q9NP92; Q96I91; Q96Q19; Q9H0P8; Q9NSF9; Q9NZ76;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=39S ribosomal protein S30, mitochondrial;
DE Short=MRP-S30;
DE Short=S30mt;
DE AltName: Full=Mitochondrial large ribosomal subunit protein mL65 {ECO:0000303|PubMed:25278503};
DE AltName: Full=Mitochondrial large ribosomal subunit protein mS30 {ECO:0000303|PubMed:27023846};
DE AltName: Full=Programmed cell death protein 9;
GN Name=MRPS30; Synonyms=PDCD9; ORFNames=BM-047;
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:CAB90810.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT SER-33.
RX PubMed=10640817; DOI=10.1159/000015397;
RA Carim-Todd L., Sumoy L., Nadal M., Estivill X., Escarceller M.;
RT "Cloning, expression, and mapping of PDCD9, the human homolog of Gallus
RT gallus pro-apoptotic protein p52.";
RL Cytogenet. Cell Genet. 87:85-88(1999).
RN [2] {ECO:0000312|EMBL:CAB90810.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-33.
RG The European IMAGE consortium;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT SER-33.
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-439.
RC TISSUE=Bone marrow;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 275-284.
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 [8] {ECO:0000305}
RP IDENTIFICATION.
RX PubMed=11279123; DOI=10.1074/jbc.m100727200;
RA Koc E.C., Burkhart W., Blackburn K., Moseley A., Spremulli L.L.;
RT "The small subunit of the mammalian mitochondrial ribosome: identification
RT of the full complement of ribosomal proteins present.";
RL J. Biol. Chem. 276:19363-19374(2001).
RN [9]
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 [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]
RP NOMENCLATURE.
RX PubMed=27023846; DOI=10.1146/annurev-biochem-060815-014343;
RA Greber B.J., Ban N.;
RT "Structure and function of the mitochondrial ribosome.";
RL Annu. Rev. Biochem. 85:103-132(2016).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS), 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 [13]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.50 ANGSTROMS), 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 [14] {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. mL65 forms a heterodimer with mL37.
CC {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379,
CC ECO:0000269|PubMed:28892042}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:11279123,
CC ECO:0000269|PubMed:28892042}.
CC -!- TISSUE SPECIFICITY: Heart, skeletal muscle, kidney and liver. Lower
CC expression in placenta and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10640817, ECO:0000269|PubMed:11279123}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL65 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67634.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAF67634.1; Type=Miscellaneous discrepancy; Note=Sequencing errors.; Evidence={ECO:0000305};
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DR EMBL; AF146192; AAF65227.1; -; mRNA.
DR EMBL; AL355715; CAB90810.1; -; mRNA.
DR EMBL; AL355716; CAB90811.1; -; mRNA.
DR EMBL; AL136706; CAB66641.1; -; mRNA.
DR EMBL; AK074777; BAC11202.1; -; mRNA.
DR EMBL; BC007735; AAH07735.1; -; mRNA.
DR EMBL; AF217523; AAF67634.1; ALT_SEQ; mRNA.
DR EMBL; AB061211; BAB54961.1; -; Genomic_DNA.
DR CCDS; CCDS3951.1; -.
DR RefSeq; NP_057724.2; NM_016640.3.
DR PDB; 3J7Y; EM; 3.40 A; s=1-439.
DR PDB; 3J9M; EM; 3.50 A; s=1-439.
DR PDB; 5OOL; EM; 3.06 A; s=1-439.
DR PDB; 5OOM; EM; 3.03 A; s=1-439.
DR PDB; 6I9R; EM; 3.90 A; s=1-439.
DR PDB; 6NU2; EM; 3.90 A; s=41-430.
DR PDB; 6NU3; EM; 4.40 A; s=1-439.
DR PDB; 6VLZ; EM; 2.97 A; s=1-439.
DR PDB; 6VMI; EM; 2.96 A; s=1-439.
DR PDB; 6ZM5; EM; 2.89 A; s=1-439.
DR PDB; 6ZM6; EM; 2.59 A; s=1-439.
DR PDB; 6ZS9; EM; 4.00 A; s=1-439.
DR PDB; 6ZSA; EM; 4.00 A; s=1-439.
DR PDB; 6ZSB; EM; 4.50 A; s=1-439.
DR PDB; 6ZSC; EM; 3.50 A; s=1-439.
DR PDB; 6ZSD; EM; 3.70 A; s=1-439.
DR PDB; 6ZSE; EM; 5.00 A; s=1-439.
DR PDB; 6ZSG; EM; 4.00 A; s=1-439.
DR PDB; 7A5F; EM; 4.40 A; s3/t3=1-439.
DR PDB; 7A5G; EM; 4.33 A; s3/t3=1-439.
DR PDB; 7A5H; EM; 3.30 A; s=1-439.
DR PDB; 7A5I; EM; 3.70 A; s3=1-439.
DR PDB; 7A5J; EM; 3.10 A; s=1-439.
DR PDB; 7A5K; EM; 3.70 A; s3=1-439.
DR PDB; 7L08; EM; 3.49 A; s=1-439.
DR PDB; 7L20; EM; 3.15 A; s=1-439.
DR PDB; 7O9K; EM; 3.10 A; s=1-439.
DR PDB; 7O9M; EM; 2.50 A; s=1-439.
DR PDB; 7ODR; EM; 2.90 A; s=1-439.
DR PDB; 7ODS; EM; 3.10 A; s=1-439.
DR PDB; 7ODT; EM; 3.10 A; s=1-439.
DR PDB; 7OF0; EM; 2.20 A; s=1-439.
DR PDB; 7OF2; EM; 2.70 A; s=1-439.
DR PDB; 7OF3; EM; 2.70 A; s=1-439.
DR PDB; 7OF4; EM; 2.70 A; s=1-439.
DR PDB; 7OF5; EM; 2.90 A; s=1-439.
DR PDB; 7OF6; EM; 2.60 A; s=1-439.
DR PDB; 7OF7; EM; 2.50 A; s=1-439.
DR PDB; 7OG4; EM; 3.80 A; s=1-439.
DR PDB; 7OI6; EM; 5.70 A; s=1-439.
DR PDB; 7OI7; EM; 3.50 A; s=1-439.
DR PDB; 7OI8; EM; 3.50 A; s=1-439.
DR PDB; 7OI9; EM; 3.30 A; s=1-439.
DR PDB; 7OIA; EM; 3.20 A; s=1-439.
DR PDB; 7OIB; EM; 3.30 A; s=1-439.
DR PDB; 7OIC; EM; 3.10 A; s=1-439.
DR PDB; 7OID; EM; 3.70 A; s=1-439.
DR PDB; 7OIE; EM; 3.50 A; s=1-439.
DR PDB; 7PD3; EM; 3.40 A; s=1-439.
DR PDB; 7QH6; EM; 3.08 A; s=1-439.
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; Q9NP92; -.
DR SMR; Q9NP92; -.
DR BioGRID; 116091; 206.
DR ComplexPortal; CPX-5226; 39S mitochondrial large ribosomal subunit.
DR CORUM; Q9NP92; -.
DR IntAct; Q9NP92; 83.
DR MINT; Q9NP92; -.
DR STRING; 9606.ENSP00000424328; -.
DR GlyGen; Q9NP92; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NP92; -.
DR PhosphoSitePlus; Q9NP92; -.
DR SwissPalm; Q9NP92; -.
DR BioMuta; MRPS30; -.
DR DMDM; 116242771; -.
DR EPD; Q9NP92; -.
DR jPOST; Q9NP92; -.
DR MassIVE; Q9NP92; -.
DR MaxQB; Q9NP92; -.
DR PaxDb; Q9NP92; -.
DR PeptideAtlas; Q9NP92; -.
DR PRIDE; Q9NP92; -.
DR ProteomicsDB; 81936; -.
DR Antibodypedia; 10864; 138 antibodies from 22 providers.
DR DNASU; 10884; -.
DR Ensembl; ENST00000507110.6; ENSP00000424328.1; ENSG00000112996.11.
DR GeneID; 10884; -.
DR KEGG; hsa:10884; -.
DR MANE-Select; ENST00000507110.6; ENSP00000424328.1; NM_016640.4; NP_057724.2.
DR UCSC; uc003joh.4; human.
DR CTD; 10884; -.
DR DisGeNET; 10884; -.
DR GeneCards; MRPS30; -.
DR HGNC; HGNC:8769; MRPS30.
DR HPA; ENSG00000112996; Low tissue specificity.
DR MIM; 611991; gene.
DR neXtProt; NX_Q9NP92; -.
DR OpenTargets; ENSG00000112996; -.
DR PharmGKB; PA31018; -.
DR VEuPathDB; HostDB:ENSG00000112996; -.
DR eggNOG; KOG4461; Eukaryota.
DR GeneTree; ENSGT00390000001442; -.
DR HOGENOM; CLU_049608_0_0_1; -.
DR InParanoid; Q9NP92; -.
DR OMA; ITDGHFF; -.
DR OrthoDB; 514288at2759; -.
DR PhylomeDB; Q9NP92; -.
DR TreeFam; TF320686; -.
DR PathwayCommons; Q9NP92; -.
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; Q9NP92; -.
DR SIGNOR; Q9NP92; -.
DR BioGRID-ORCS; 10884; 209 hits in 1081 CRISPR screens.
DR ChiTaRS; MRPS30; human.
DR GeneWiki; MRPS30; -.
DR GenomeRNAi; 10884; -.
DR Pharos; Q9NP92; Tbio.
DR PRO; PR:Q9NP92; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; Q9NP92; protein.
DR Bgee; ENSG00000112996; Expressed in adrenal tissue and 202 other tissues.
DR Genevisible; Q9NP92; 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; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
DR GO; GO:0032543; P:mitochondrial translation; IC:ComplexPortal.
DR InterPro; IPR039982; MRPS30.
DR InterPro; IPR010793; Ribosomal_L37/S30.
DR PANTHER; PTHR13014; PTHR13014; 1.
DR Pfam; PF07147; PDCD9; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT CHAIN 1..439
FT /note="39S ribosomal protein S30, mitochondrial"
FT /id="PRO_0000087720"
FT VARIANT 33
FT /note="C -> S (in dbSNP:rs3747479)"
FT /evidence="ECO:0000269|PubMed:10640817,
FT ECO:0000269|PubMed:11230166, ECO:0000269|Ref.2"
FT /id="VAR_028023"
FT VARIANT 102
FT /note="A -> V (in dbSNP:rs35601455)"
FT /id="VAR_052048"
FT CONFLICT 82
FT /note="I -> V (in Ref. 3; CAB66641)"
FT /evidence="ECO:0000305"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 56..72
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 141..154
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:7OIB"
FT HELIX 168..188
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 199..203
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 206..216
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 221..224
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 226..235
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 238..245
FT /evidence="ECO:0007829|PDB:7OF0"
FT TURN 268..272
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7OIA"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 308..314
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 318..343
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:5OOM"
FT STRAND 355..374
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 391..395
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 403..406
FT /evidence="ECO:0007829|PDB:7OF0"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:7OF0"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:7OF0"
SQ SEQUENCE 439 AA; 50365 MW; 2A22DB6170F6D04F CRC64;
MAAARCWRPL LRGPRLSLHT AANAAATATE TTCQDVAATP VARYPPIVAS MTADSKAARL
RRIERWQATV HAAESVDEKL RILTKMQFMK YMVYPQTFAL NADRWYQYFT KTVFLSGLPP
PPAEPEPEPE PEPEPALDLA ALRAVACDCL LQEHFYLRRR RRVHRYEESE VISLPFLDQL
VSTLVGLLSP HNPALAAAAL DYRCPVHFYW VRGEEIIPRG HRRGRIDDLR YQIDDKPNNQ
IRISKQLAEF VPLDYSVPIE IPTIKCKPDK LPLFKRQYEN HIFVGSKTAD PCCYGHTQFH
LLPDKLRRER LLRQNCADQI EVVFRANAIA SLFAWTGAQA MYQGFWSEAD VTRPFVSQAV
ITDGKYFSFF CYQLNTLALT TQADQNNPRK NICWGTQSKP LYETIEDNDV KGFNDDVLLQ
IVHFLLNRPK EEKSQLLEN
