DENR_HUMAN
ID DENR_HUMAN Reviewed; 198 AA.
AC O43583; Q9H3U6; Q9UKZ0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Density-regulated protein;
DE Short=DRP;
DE AltName: Full=Protein DRP1;
DE AltName: Full=Smooth muscle cell-associated protein 3;
DE Short=SMAP-3;
GN Name=DENR; Synonyms=DRP1; ORFNames=H14;
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], TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9628587; DOI=10.1089/dna.1998.17.437;
RA Deyo J.E., Chiao P.J., Tainsky M.A.;
RT "Drp, a novel protein expressed at high cell density but not during growth
RT arrest.";
RL DNA Cell Biol. 17:437-447(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Nishimoto S., Toyoda H., Tawara J., Aoki T., Komurasaki T.;
RT "Molecular cloning and characterization of human smooth muscle cell
RT associated protein-3 (SMAP-3).";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 49-198, AND INDUCTION BY ERBB2.
RX PubMed=10497265; DOI=10.1093/nar/27.20.4008;
RA Oh J.J., Grosshans D.R., Wong S.G., Slamon D.J.;
RT "Identification of differentially expressed genes associated with HER-2/neu
RT overexpression in human breast cancer cells.";
RL Nucleic Acids Res. 27:4008-4017(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH MCTS1.
RX PubMed=16982740; DOI=10.1158/0008-5472.can-06-1999;
RA Reinert L.S., Shi B., Nandi S., Mazan-Mamczarz K., Vitolo M., Bachman K.E.,
RA He H., Gartenhaus R.B.;
RT "MCT-1 protein interacts with the cap complex and modulates messenger RNA
RT translational profiles.";
RL Cancer Res. 66:8994-9001(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP FUNCTION, AND INDUCTION BY HNRNPD.
RX PubMed=17878526;
RA Mazan-Mamczarz K., Gartenhaus R.B.;
RT "Post-transcriptional control of the MCT-1-associated protein DENR/DRP by
RT RNA-binding protein AUF1.";
RL Cancer Genomics Proteomics 4:233-239(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [12]
RP FUNCTION.
RX PubMed=20713520; DOI=10.1101/gad.1957510;
RA Skabkin M.A., Skabkina O.V., Dhote V., Komar A.A., Hellen C.U.,
RA Pestova T.V.;
RT "Activities of ligatin and MCT-1/DENR in eukaryotic translation initiation
RT and ribosomal recycling.";
RL Genes Dev. 24:1787-1801(2010).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-73 AND THR-86, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: May be involved in the translation of target mRNAs by
CC scanning and recognition of the initiation codon. Involved in
CC translation initiation; promotes recruitmnet of aminoacetyled initiator
CC tRNA to P site of 40S ribosomes. Can promote release of deacylated tRNA
CC and mRNA from recycled 40S subunits following ABCE1-mediated
CC dissociation of post-termination ribosomal complexes into subunits.
CC Plays a role in the modulation of the translational profile of a subset
CC of cancer-related mRNAs when recruited to the translational initiation
CC complex by the oncogene MCTS1. {ECO:0000269|PubMed:16982740,
CC ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:20713520}.
CC -!- SUBUNIT: Interacts with MCTS1. {ECO:0000269|PubMed:16982740}.
CC -!- INTERACTION:
CC O43583; Q9NX47: MARCHF5; NbExp=2; IntAct=EBI-716083, EBI-2341610;
CC O43583; Q9ULC4: MCTS1; NbExp=7; IntAct=EBI-716083, EBI-716076;
CC O43583; Q8WX92: NELFB; NbExp=2; IntAct=EBI-716083, EBI-347721;
CC O43583; P0CG48: UBC; NbExp=3; IntAct=EBI-716083, EBI-3390054;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart and skeletal muscle and
CC moderately expressed in the brain, placenta, liver and pancreas. Weakly
CC expressed in the lung and kidney. {ECO:0000269|PubMed:9628587}.
CC -!- INDUCTION: Up-regulated with increasing cell-density by HNRNPD. Up-
CC regulated in ovarian and breast cancer cells by ERBB2 overexpression.
CC Not induced by TGFB1. {ECO:0000269|PubMed:10497265,
CC ECO:0000269|PubMed:17878526, ECO:0000269|PubMed:9628587}.
CC -!- SIMILARITY: Belongs to the DENR family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC02985.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/DENRID40295ch12q24.html";
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DR EMBL; AF038554; AAC02985.2; ALT_INIT; mRNA.
DR EMBL; AB014731; BAB20268.1; -; mRNA.
DR EMBL; AC026331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC027290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007860; AAH07860.1; -; mRNA.
DR EMBL; AF103800; AAF02420.1; -; mRNA.
DR CCDS; CCDS45003.1; -.
DR RefSeq; NP_003668.2; NM_003677.4.
DR PDB; 5ONS; X-ray; 2.14 A; B=24-51.
DR PDB; 5VYC; X-ray; 6.00 A; l1/l2/l3/l4/l5/l6=1-198.
DR PDB; 6MS4; X-ray; 2.00 A; B=25-70.
DR PDB; 6VPQ; X-ray; 1.74 A; A/B/C/D/E/F=1-198.
DR PDB; 6VPR; X-ray; 2.20 A; A/B=1-198.
DR PDBsum; 5ONS; -.
DR PDBsum; 5VYC; -.
DR PDBsum; 6MS4; -.
DR PDBsum; 6VPQ; -.
DR PDBsum; 6VPR; -.
DR AlphaFoldDB; O43583; -.
DR SMR; O43583; -.
DR BioGRID; 114131; 65.
DR IntAct; O43583; 39.
DR MINT; O43583; -.
DR STRING; 9606.ENSP00000280557; -.
DR GlyGen; O43583; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43583; -.
DR PhosphoSitePlus; O43583; -.
DR SwissPalm; O43583; -.
DR BioMuta; DENR; -.
DR EPD; O43583; -.
DR jPOST; O43583; -.
DR MassIVE; O43583; -.
DR MaxQB; O43583; -.
DR PaxDb; O43583; -.
DR PeptideAtlas; O43583; -.
DR PRIDE; O43583; -.
DR ProteomicsDB; 49063; -.
DR TopDownProteomics; O43583; -.
DR Antibodypedia; 31699; 205 antibodies from 30 providers.
DR DNASU; 8562; -.
DR Ensembl; ENST00000280557.11; ENSP00000280557.6; ENSG00000139726.11.
DR GeneID; 8562; -.
DR KEGG; hsa:8562; -.
DR MANE-Select; ENST00000280557.11; ENSP00000280557.6; NM_003677.5; NP_003668.2.
DR UCSC; uc001uda.4; human.
DR CTD; 8562; -.
DR DisGeNET; 8562; -.
DR GeneCards; DENR; -.
DR HGNC; HGNC:2769; DENR.
DR HPA; ENSG00000139726; Low tissue specificity.
DR MIM; 604550; gene.
DR neXtProt; NX_O43583; -.
DR OpenTargets; ENSG00000139726; -.
DR PharmGKB; PA27252; -.
DR VEuPathDB; HostDB:ENSG00000139726; -.
DR eggNOG; KOG3239; Eukaryota.
DR GeneTree; ENSGT00390000014349; -.
DR HOGENOM; CLU_073511_1_0_1; -.
DR InParanoid; O43583; -.
DR OMA; VIYCGVC; -.
DR OrthoDB; 1490022at2759; -.
DR PhylomeDB; O43583; -.
DR TreeFam; TF105912; -.
DR PathwayCommons; O43583; -.
DR SignaLink; O43583; -.
DR BioGRID-ORCS; 8562; 631 hits in 1057 CRISPR screens.
DR ChiTaRS; DENR; human.
DR GenomeRNAi; 8562; -.
DR Pharos; O43583; Tbio.
DR PRO; PR:O43583; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O43583; protein.
DR Bgee; ENSG00000139726; Expressed in germinal epithelium of ovary and 205 other tissues.
DR ExpressionAtlas; O43583; baseline and differential.
DR Genevisible; O43583; HS.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001731; P:formation of translation preinitiation complex; IDA:UniProtKB.
DR GO; GO:0075522; P:IRES-dependent viral translational initiation; IDA:UniProtKB.
DR GO; GO:0032790; P:ribosome disassembly; IDA:UniProtKB.
DR GO; GO:0002188; P:translation reinitiation; IBA:GO_Central.
DR InterPro; IPR005873; DENR_eukaryotes.
DR InterPro; IPR001950; SUI1.
DR InterPro; IPR036877; SUI1_dom_sf.
DR Pfam; PF01253; SUI1; 1.
DR SUPFAM; SSF55159; SSF55159; 1.
DR TIGRFAMs; TIGR01159; DRP1; 1.
DR PROSITE; PS50296; SUI1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Initiation factor; Phosphoprotein;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..198
FT /note="Density-regulated protein"
FT /id="PRO_0000130600"
FT DOMAIN 115..182
FT /note="SUI1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00200"
FT REGION 72..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 73
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 189
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CQJ6"
FT CONFLICT 49..50
FT /note="DV -> HE (in Ref. 5; AAF02420)"
FT /evidence="ECO:0000305"
FT TURN 35..37
FT /evidence="ECO:0007829|PDB:6MS4"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:6MS4"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:5ONS"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:6MS4"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:6MS4"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:6VPQ"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:6VPQ"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:6VPQ"
FT HELIX 141..152
FT /evidence="ECO:0007829|PDB:6VPQ"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6VPQ"
FT STRAND 163..168
FT /evidence="ECO:0007829|PDB:6VPQ"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:6VPQ"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:6VPQ"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:6VPQ"
FT STRAND 190..192
FT /evidence="ECO:0007829|PDB:6VPQ"
SQ SEQUENCE 198 AA; 22092 MW; 023F70E0C6C0B25D CRC64;
MAADISESSG ADCKGDPRNS AKLDADYPLR VLYCGVCSLP TEYCEYMPDV AKCRQWLEKN
FPNEFAKLTV ENSPKQEAGI SEGQGTAGEE EEKKKQKRGG RGQIKQKKKT VPQKVTIAKI
PRAKKKYVTR VCGLATFEID LKEAQRFFAQ KFSCGASVTG EDEIIIQGDF TDDIIDVIQE
KWPEVDDDSI EDLGEVKK
