NDUS2_MOUSE
ID NDUS2_MOUSE Reviewed; 463 AA.
AC Q91WD5; Q3TNA8; Q3U5Y9; Q3UJX7; Q99L23;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial;
DE EC=7.1.1.2 {ECO:0000269|PubMed:26437605, ECO:0000269|PubMed:29887397, ECO:0000269|PubMed:31297047};
DE AltName: Full=Complex I-49kD;
DE Short=CI-49kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 49 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufs2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 PROTEIN SEQUENCE OF 57-73; 76-108; 128-138; 158-166; 172-179; 210-216;
RP 255-266; 272-323; 373-421; 424-437 AND 441-463, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT identifies substrates of SIRT3 in metabolic pathways.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
RN [6]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26437605; DOI=10.1016/j.cmet.2015.09.004;
RA Fernandez-Agueera M.C., Gao L., Gonzalez-Rodriguez P., Pintado C.O.,
RA Arias-Mayenco I., Garcia-Flores P., Garcia-Perganeda A., Pascual A.,
RA Ortega-Saenz P., Lopez-Barneo J.;
RT "Oxygen Sensing by Arterial Chemoreceptors Depends on Mitochondrial Complex
RT I Signaling.";
RL Cell Metab. 22:825-837(2015).
RN [7]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29887397; DOI=10.1016/j.cmet.2018.05.009;
RA Arias-Mayenco I., Gonzalez-Rodriguez P., Torres-Torrelo H., Gao L.,
RA Fernandez-Agueera M.C., Bonilla-Henao V., Ortega-Saenz P., Lopez-Barneo J.;
RT "Acute O2 Sensing: Role of Coenzyme QH2/Q Ratio and Mitochondrial ROS
RT Compartmentalization.";
RL Cell Metab. 28:145-158(2018).
RN [8]
RP FUNCTION.
RX PubMed=30922174; DOI=10.1161/circresaha.118.314284;
RA Dunham-Snary K.J., Wu D., Potus F., Sykes E.A., Mewburn J.D., Charles R.L.,
RA Eaton P., Sultanian R.A., Archer S.L.;
RT "Ndufs2, a Core Subunit of Mitochondrial Complex I, Is Essential for Acute
RT Oxygen-Sensing and Hypoxic Pulmonary Vasoconstriction.";
RL Circ. Res. 124:1727-1746(2019).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=31297047; DOI=10.3389/fnins.2019.00664;
RA Cabello-Rivera D., Sarmiento-Soto H., Lopez-Barneo J., Munoz-Cabello A.M.;
RT "Mitochondrial Complex I Function Is Essential for Neural Stem/Progenitor
RT Cells Proliferation and Differentiation.";
RL Front. Neurosci. 13:664-664(2019).
RN [10]
RP INTERACTION WITH CERS2.
RX PubMed=32279995; DOI=10.1016/j.bbrc.2020.02.166;
RA Yang Y., Yang X., Lin Y., Yang G., Li L.;
RT "LASS2 regulates hepatocyte steatosis by interacting with NDUFS2/OXPHOS
RT related proteins.";
RL Biochem. Biophys. Res. Commun. 526:871-879(2020).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC NADH through the respiratory chain, using ubiquinone as an electron
CC acceptor (PubMed:26437605, PubMed:29887397, PubMed:31297047). Essential
CC for the catalytic activity and assembly of complex I (PubMed:26437605,
CC PubMed:29887397, PubMed:31297047). Redox-sensitive, critical component
CC of the oxygen-sensing pathway in the pulmonary vasculature which plays
CC a key role in acute pulmonary oxygen-sensing and hypoxic pulmonary
CC vasoconstriction (PubMed:30922174). Plays an important role in carotid
CC body sensing of hypoxia (PubMed:26437605, PubMed:29887397). Essential
CC for glia-like neural stem and progenitor cell proliferation,
CC differentiation and subsequent oligodendrocyte or neuronal maturation
CC (PubMed:31297047). {ECO:0000269|PubMed:26437605,
CC ECO:0000269|PubMed:29887397, ECO:0000269|PubMed:30922174,
CC ECO:0000269|PubMed:31297047}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC Evidence={ECO:0000269|PubMed:26437605, ECO:0000269|PubMed:29887397,
CC ECO:0000269|PubMed:31297047};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster.;
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits. Component of the iron-
CC sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3. Interacts
CC with NDUFAF7 (By similarity). Interacts with CERS2 (PubMed:32279995).
CC {ECO:0000250|UniProtKB:O75306, ECO:0000269|PubMed:32279995}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:Q641Y2}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q641Y2}; Matrix side
CC {ECO:0000250|UniProtKB:Q641Y2}.
CC -!- PTM: Dimethylation at Arg-118 by NDUFAF7 takes place after NDUFS2
CC assembles into the complex I, leading to stabilize the early
CC intermediate complex. {ECO:0000250|UniProtKB:O75306}.
CC -!- DISRUPTION PHENOTYPE: Knockout mice show early perinatal death and
CC major defects in the CNS, compromising especially the postnatal
CC development of dorsal cortex, corpus callosum, hippocampus and
CC cerebellum (PubMed:31297047). Neonatal neurogenesis and gliogenesis are
CC deeply impaired (PubMed:31297047). {ECO:0000269|PubMed:31297047}.
CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03898.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK078474; BAC37293.1; -; mRNA.
DR EMBL; AK146269; BAE27028.1; -; mRNA.
DR EMBL; AK150431; BAE29554.1; -; mRNA.
DR EMBL; AK151746; BAE30656.1; -; mRNA.
DR EMBL; AK153364; BAE31936.1; -; mRNA.
DR EMBL; AK165426; BAE38181.1; -; mRNA.
DR EMBL; BC003898; AAH03898.1; ALT_INIT; mRNA.
DR EMBL; BC016097; AAH16097.1; -; mRNA.
DR CCDS; CCDS15484.1; -.
DR RefSeq; NP_694704.1; NM_153064.5.
DR PDB; 6G2J; EM; 3.30 A; D=1-463.
DR PDB; 6G72; EM; 3.90 A; D=1-463.
DR PDB; 6ZR2; EM; 3.10 A; D=1-463.
DR PDB; 6ZTQ; EM; 3.00 A; D=1-463.
DR PDB; 7AK5; EM; 3.17 A; D=1-463.
DR PDB; 7AK6; EM; 3.82 A; D=1-463.
DR PDB; 7B93; EM; 3.04 A; D=1-463.
DR PDB; 7PSA; EM; 3.40 A; D=1-463.
DR PDBsum; 6G2J; -.
DR PDBsum; 6G72; -.
DR PDBsum; 6ZR2; -.
DR PDBsum; 6ZTQ; -.
DR PDBsum; 7AK5; -.
DR PDBsum; 7AK6; -.
DR PDBsum; 7B93; -.
DR PDBsum; 7PSA; -.
DR AlphaFoldDB; Q91WD5; -.
DR SMR; Q91WD5; -.
DR BioGRID; 230541; 62.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q91WD5; -.
DR IntAct; Q91WD5; 15.
DR MINT; Q91WD5; -.
DR STRING; 10090.ENSMUSP00000013737; -.
DR iPTMnet; Q91WD5; -.
DR PhosphoSitePlus; Q91WD5; -.
DR SwissPalm; Q91WD5; -.
DR EPD; Q91WD5; -.
DR jPOST; Q91WD5; -.
DR MaxQB; Q91WD5; -.
DR PaxDb; Q91WD5; -.
DR PeptideAtlas; Q91WD5; -.
DR PRIDE; Q91WD5; -.
DR ProteomicsDB; 286170; -.
DR Antibodypedia; 34301; 310 antibodies from 33 providers.
DR DNASU; 226646; -.
DR Ensembl; ENSMUST00000013737; ENSMUSP00000013737; ENSMUSG00000013593.
DR GeneID; 226646; -.
DR KEGG; mmu:226646; -.
DR UCSC; uc007dnm.1; mouse.
DR CTD; 4720; -.
DR MGI; MGI:2385112; Ndufs2.
DR VEuPathDB; HostDB:ENSMUSG00000013593; -.
DR eggNOG; KOG2870; Eukaryota.
DR GeneTree; ENSGT00390000009529; -.
DR HOGENOM; CLU_015134_1_2_1; -.
DR InParanoid; Q91WD5; -.
DR OMA; IMGTSME; -.
DR OrthoDB; 444312at2759; -.
DR PhylomeDB; Q91WD5; -.
DR TreeFam; TF300370; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 226646; 22 hits in 75 CRISPR screens.
DR ChiTaRS; Ndufs2; mouse.
DR PRO; PR:Q91WD5; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q91WD5; protein.
DR Bgee; ENSMUSG00000013593; Expressed in cardiac muscle of left ventricle and 271 other tissues.
DR ExpressionAtlas; Q91WD5; baseline and differential.
DR Genevisible; Q91WD5; MM.
DR GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR GO; GO:0003954; F:NADH dehydrogenase activity; ISO:MGI.
DR GO; GO:0019826; F:oxygen sensor activity; IMP:UniProtKB.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0071453; P:cellular response to oxygen levels; IMP:UniProtKB.
DR GO; GO:0042063; P:gliogenesis; IMP:UniProtKB.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0061351; P:neural precursor cell proliferation; IMP:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR GO; GO:0006979; P:response to oxidative stress; ISS:UniProtKB.
DR Gene3D; 1.10.645.10; -; 1.
DR HAMAP; MF_01358; NDH1_NuoD; 1.
DR InterPro; IPR001135; NADH_Q_OxRdtase_suD.
DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS.
DR InterPro; IPR022885; NDH1_su_D/H.
DR InterPro; IPR029014; NiFe-Hase_large.
DR PANTHER; PTHR11993; PTHR11993; 1.
DR Pfam; PF00346; Complex1_49kDa; 1.
DR SUPFAM; SSF56762; SSF56762; 1.
DR TIGRFAMs; TIGR01962; NuoD; 1.
DR PROSITE; PS00535; COMPLEX1_49K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; Iron; Iron-sulfur; Membrane; Metal-binding;
KW Methylation; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Reference proteome; Respiratory chain; Transit peptide;
KW Translocase; Transport; Ubiquinone.
FT TRANSIT 1..33
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 34..463
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 2, mitochondrial"
FT /id="PRO_0000019982"
FT BINDING 326
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 332
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 347
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 62
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 118
FT /note="Symmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:P17694"
FT CONFLICT 1
FT /note="M -> V (in Ref. 2; AAH03898)"
FT /evidence="ECO:0000305"
FT CONFLICT 2
FT /note="A -> R (in Ref. 1; BAE30656/BAE31936)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="T -> A (in Ref. 1; BAE27028)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="A -> S (in Ref. 1; BAE27028)"
FT /evidence="ECO:0000305"
FT HELIX 41..44
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 49..53
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:7B93"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 80..83
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 98..110
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 120..126
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 133..139
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 144..159
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 165..194
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 198..217
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:6ZR2"
FT HELIX 241..262
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 267..272
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 280..286
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 295..297
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 302..305
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:6G2J"
FT HELIX 328..349
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 361..363
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 375..386
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 395..401
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 403..412
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 429..438
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 439..441
FT /evidence="ECO:0007829|PDB:7B93"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 463 AA; 52626 MW; 989934D73F5C8D27 CRC64;
MAALRALRCL RGVGAPVLRP GSGIRLPSQP SRGARQWQPD IEWAEQFSGA VMYPSKETAH
WKPPPWNDVD ILKEKAVTNM TLNFGPQHPA AHGVLRLVLE LSGEMVRKCD PHIGLLHRGT
EKLIEYKTYL QALPYFDRLD YVSMMCNEQA YSIAVEKLLN IQPPPRAQWI RVLFGEITRI
LNHIMAVTTH ALDIGAMTPF FWMFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL
LDDIYEFSKN FSLRIDEVEE MLTNNRIWRN RTVDIGVVTA EDALNYGFSG VMLRGSGIQW
DLRKTQPYDV YDQVEFDVPI GSRGDCYDRY LCRVEEMRQS LRIIEQCLNK MPPGEIKVDD
AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI EAPKGEFGVY LVSDGSSRPY
RCKIKAPGFA HLAGLDKMSK GHMLADVVAI IGTQDIVFGE IDR
