OGFD1_HUMAN
ID OGFD1_HUMAN Reviewed; 542 AA.
AC Q8N543; H3BUQ2; Q9H7U5; Q9H9J9; Q9HA87; Q9HCG0; Q9NVB6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Prolyl 3-hydroxylase OGFOD1;
DE EC=1.14.11.-;
DE AltName: Full=2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1;
DE AltName: Full=Termination and polyadenylation 1 homolog;
DE AltName: Full=uS12 prolyl 3-hydroxylase {ECO:0000303|PubMed:25728928};
GN Name=OGFOD1; Synonyms=KIAA1612, TPA1;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:273-281(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
RP SER-173.
RC TISSUE=Embryo, Ovary, and 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND IDENTIFICATION.
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 SUBCELLULAR LOCATION, AND MUTAGENESIS OF HIS-155.
RX PubMed=20579638; DOI=10.1016/j.febslet.2010.06.015;
RA Saito K., Adachi N., Koyama H., Matsushita M.;
RT "OGFOD1, a member of the 2-oxoglutarate and iron dependent dioxygenase
RT family, functions in ischemic signaling.";
RL FEBS Lett. 584:3340-3347(2010).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20154146; DOI=10.1128/mcb.01350-09;
RA Wehner K.A., Schutz S., Sarnow P.;
RT "OGFOD1, a novel modulator of eukaryotic translation initiation factor
RT 2alpha phosphorylation and the cellular response to stress.";
RL Mol. Cell. Biol. 30:2006-2016(2010).
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 SUBCELLULAR LOCATION.
RX PubMed=22002106; DOI=10.1074/mcp.m111.013680;
RA Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I.;
RT "Systematic analysis of protein pools, isoforms, and modifications
RT affecting turnover and subcellular localization.";
RL Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24550462; DOI=10.1073/pnas.1311750111;
RA Loenarz C., Sekirnik R., Thalhammer A., Ge W., Spivakovsky E.,
RA Mackeen M.M., McDonough M.A., Cockman M.E., Kessler B.M., Ratcliffe P.J.,
RA Wolf A., Schofield C.J.;
RT "Hydroxylation of the eukaryotic ribosomal decoding center affects
RT translational accuracy.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4019-4024(2014).
RN [10]
RP FUNCTION, AND MUTAGENESIS OF ASP-157.
RX PubMed=24550447; DOI=10.1073/pnas.1314482111;
RA Singleton R.S., Liu-Yi P., Formenti F., Ge W., Sekirnik R., Fischer R.,
RA Adam J., Pollard P.J., Wolf A., Thalhammer A., Loenarz C., Flashman E.,
RA Yamamoto A., Coleman M.L., Kessler B.M., Wappner P., Schofield C.J.,
RA Ratcliffe P.J., Cockman M.E.;
RT "OGFOD1 catalyzes prolyl hydroxylation of RPS23 and is involved in
RT translation control and stress granule formation.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:4031-4036(2014).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH INHIBITORS, AND
RP SUBUNIT.
RX PubMed=25728928; DOI=10.1016/j.str.2015.01.014;
RA Horita S., Scotti J.S., Thinnes C., Mottaghi-Taromsari Y.S., Thalhammer A.,
RA Ge W., Aik W., Loenarz C., Schofield C.J., McDonough M.A.;
RT "Structure of the ribosomal oxygenase OGFOD1 provides insights into the
RT regio- and stereoselectivity of prolyl hydroxylases.";
RL Structure 23:639-652(2015).
CC -!- FUNCTION: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-
CC 62' of small ribosomal subunit uS12 (RPS23), thereby regulating protein
CC translation termination efficiency. Involved in stress granule
CC formation. {ECO:0000269|PubMed:20154146, ECO:0000269|PubMed:24550447,
CC ECO:0000269|PubMed:24550462}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + [ribosomal protein uS12]-L-proline + O2 =
CC [ribosomal protein uS12]-(3S)-3-hydroxy-L-proline + CO2 + succinate;
CC Xref=Rhea:RHEA:54156, Rhea:RHEA-COMP:13816, Rhea:RHEA-COMP:13818,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:50342, ChEBI:CHEBI:85428;
CC Evidence={ECO:0000269|PubMed:24550462, ECO:0000305|PubMed:25728928};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- COFACTOR:
CC Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:25728928}.
CC -!- INTERACTION:
CC Q8N543; Q9BSK4: FEM1A; NbExp=3; IntAct=EBI-13327083, EBI-2515349;
CC Q8N543; P62266: RPS23; NbExp=3; IntAct=EBI-13327083, EBI-353072;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Nucleus. Note=Mainly
CC nuclear. A portion relocalizes to cytoplasmic stress granules upon
CC stress.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N543-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N543-2; Sequence=VSP_025852;
CC -!- SIMILARITY: Belongs to the TPA1 family. {ECO:0000305}.
CC -!- CAUTION: According to a report, it is incorporated into stress granules
CC upon arsenite-induced stress and associates with heme-regulated kinase
CC and eIF-2-alpha (EIF2S1) in regulating eIF-2-alpha phosphorylation
CC (PubMed:20154146). However, no effect in eIF-2-alpha phosphorylation
CC have been observed by another study (PubMed:24550447).
CC {ECO:0000305|PubMed:20154146, ECO:0000305|PubMed:24550447}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13438.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14880.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB046832; BAB13438.1; ALT_INIT; mRNA.
DR EMBL; AK001688; BAA91838.1; -; mRNA.
DR EMBL; AK022130; BAB13967.1; -; mRNA.
DR EMBL; AK022752; BAB14226.1; -; mRNA.
DR EMBL; AK024314; BAB14880.1; ALT_INIT; mRNA.
DR EMBL; AC092140; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032919; AAH32919.1; -; mRNA.
DR CCDS; CCDS10761.2; -. [Q8N543-1]
DR RefSeq; NP_001311291.1; NM_001324362.1. [Q8N543-2]
DR RefSeq; NP_060703.3; NM_018233.3. [Q8N543-1]
DR PDB; 4NHX; X-ray; 2.10 A; A=1-542.
DR PDB; 4NHY; X-ray; 2.60 A; A/B/C/D=1-542.
DR PDBsum; 4NHX; -.
DR PDBsum; 4NHY; -.
DR AlphaFoldDB; Q8N543; -.
DR SMR; Q8N543; -.
DR BioGRID; 120532; 53.
DR IntAct; Q8N543; 3.
DR STRING; 9606.ENSP00000457258; -.
DR BindingDB; Q8N543; -.
DR ChEMBL; CHEMBL4523398; -.
DR DrugBank; DB00126; Ascorbic acid.
DR GlyGen; Q8N543; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N543; -.
DR MetOSite; Q8N543; -.
DR PhosphoSitePlus; Q8N543; -.
DR BioMuta; OGFOD1; -.
DR DMDM; 74728942; -.
DR EPD; Q8N543; -.
DR jPOST; Q8N543; -.
DR MassIVE; Q8N543; -.
DR MaxQB; Q8N543; -.
DR PaxDb; Q8N543; -.
DR PeptideAtlas; Q8N543; -.
DR PRIDE; Q8N543; -.
DR ProteomicsDB; 42995; -.
DR ProteomicsDB; 72000; -. [Q8N543-1]
DR ProteomicsDB; 72001; -. [Q8N543-2]
DR Antibodypedia; 756; 208 antibodies from 26 providers.
DR DNASU; 55239; -.
DR Ensembl; ENST00000566157.6; ENSP00000457258.1; ENSG00000087263.17. [Q8N543-1]
DR GeneID; 55239; -.
DR KEGG; hsa:55239; -.
DR MANE-Select; ENST00000566157.6; ENSP00000457258.1; NM_018233.4; NP_060703.3.
DR UCSC; uc002ejb.4; human. [Q8N543-1]
DR CTD; 55239; -.
DR DisGeNET; 55239; -.
DR GeneCards; OGFOD1; -.
DR HGNC; HGNC:25585; OGFOD1.
DR HPA; ENSG00000087263; Low tissue specificity.
DR MIM; 615857; gene.
DR neXtProt; NX_Q8N543; -.
DR OpenTargets; ENSG00000087263; -.
DR PharmGKB; PA143485568; -.
DR VEuPathDB; HostDB:ENSG00000087263; -.
DR eggNOG; KOG3844; Eukaryota.
DR GeneTree; ENSGT00390000002349; -.
DR HOGENOM; CLU_027679_0_0_1; -.
DR InParanoid; Q8N543; -.
DR OMA; YTDALLC; -.
DR OrthoDB; 623539at2759; -.
DR PhylomeDB; Q8N543; -.
DR TreeFam; TF105920; -.
DR PathwayCommons; Q8N543; -.
DR SignaLink; Q8N543; -.
DR BioGRID-ORCS; 55239; 91 hits in 1087 CRISPR screens.
DR ChiTaRS; OGFOD1; human.
DR GeneWiki; OGFOD1; -.
DR GenomeRNAi; 55239; -.
DR Pharos; Q8N543; Tbio.
DR PRO; PR:Q8N543; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8N543; protein.
DR Bgee; ENSG00000087263; Expressed in adrenal tissue and 195 other tissues.
DR ExpressionAtlas; Q8N543; baseline and differential.
DR Genevisible; Q8N543; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0010494; C:cytoplasmic stress granule; IMP:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR GO; GO:0031544; F:peptidyl-proline 3-dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0031543; F:peptidyl-proline dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IMP:UniProtKB.
DR GO; GO:0019511; P:peptidyl-proline hydroxylation; IDA:CACAO.
DR GO; GO:0018126; P:protein hydroxylation; IDA:UniProtKB.
DR GO; GO:0006449; P:regulation of translational termination; IMP:UniProtKB.
DR GO; GO:0034063; P:stress granule assembly; IMP:UniProtKB.
DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
DR InterPro; IPR019601; Oxoglutarate/Fe-dep_Oase_C.
DR InterPro; IPR006620; Pro_4_hyd_alph.
DR InterPro; IPR039558; TPA1/OFD1_N.
DR Pfam; PF13661; 2OG-FeII_Oxy_4; 1.
DR Pfam; PF10637; Ofd1_CTDD; 1.
DR SMART; SM00702; P4Hc; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Dioxygenase; Iron;
KW Metal-binding; Nucleus; Oxidoreductase; Reference proteome; Vitamin C.
FT CHAIN 1..542
FT /note="Prolyl 3-hydroxylase OGFOD1"
FT /id="PRO_0000288974"
FT DOMAIN 134..239
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT REGION 373..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 4..20
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 373..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 155
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:25728928"
FT BINDING 157
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:25728928"
FT BINDING 169
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000305|PubMed:25728928"
FT BINDING 218
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000269|PubMed:25728928"
FT BINDING 230
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805,
FT ECO:0000305|PubMed:25728928"
FT VAR_SEQ 1..140
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_025852"
FT VARIANT 173
FT /note="P -> S (in dbSNP:rs34883368)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_032545"
FT MUTAGEN 155
FT /note="H->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:20579638"
FT MUTAGEN 157
FT /note="D->A: Loss of function."
FT /evidence="ECO:0000269|PubMed:24550447"
FT CONFLICT 50
FT /note="S -> G (in Ref. 2; BAB13967)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="I -> V (in Ref. 2; BAB14226)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="E -> G (in Ref. 2; BAB14880)"
FT /evidence="ECO:0000305"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 33..44
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 73..84
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 88..102
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:4NHY"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 122..131
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 162..169
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 182..187
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 193..200
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 266..269
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 272..275
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 277..290
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 301..313
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:4NHX"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 339..349
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 459..467
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 479..483
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 500..505
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 509..513
FT /evidence="ECO:0007829|PDB:4NHX"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:4NHX"
FT STRAND 532..541
FT /evidence="ECO:0007829|PDB:4NHX"
SQ SEQUENCE 542 AA; 63246 MW; 8834BB200D5D8D85 CRC64;
MNGKRPAEPG PARVGKKGKK EVMAEFSDAV TEETLKKQVA EAWSRRTPFS HEVIVMDMDP
FLHCVIPNFI QSQDFLEGLQ KELMNLDFHE KYNDLYKFQQ SDDLKKRREP HISTLRKILF
EDFRSWLSDI SKIDLESTID MSCAKYEFTD ALLCHDDELE GRRIAFILYL VPPWDRSMGG
TLDLYSIDEH FQPKQIVKSL IPSWNKLVFF EVSPVSFHQV SEVLSEEKSR LSISGWFHGP
SLTRPPNYFE PPIPRSPHIP QDHEILYDWI NPTYLDMDYQ VQIQEEFEES SEILLKEFLK
PEKFTKVCEA LEHGHVEWSS RGPPNKRFYE KAEESKLPEI LKECMKLFRS EALFLLLSNF
TGLKLHFLAP SEEDEMNDKK EAETTDITEE GTSHSPPEPE NNQMAISNNS QQSNEQTDPE
PEENETKKES SVPMCQGELR HWKTGHYTLI HDHSKAEFAL DLILYCGCEG WEPEYGGFTS
YIAKGEDEEL LTVNPESNSL ALVYRDRETL KFVKHINHRS LEQKKTFPNR TGFWDFSFIY
YE
