NDUV1_MOUSE
ID NDUV1_MOUSE Reviewed; 464 AA.
AC Q91YT0;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-51kD;
DE Short=CI-51kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit;
DE Flags: Precursor;
GN Name=Ndufv1;
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=C57BL/6J;
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=Kidney;
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 21-29.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=10870971;
RX DOI=10.1002/(sici)1522-2683(20000501)21:9<1853::aid-elps1853>3.0.co;2-y;
RA Tsugita A., Kawakami T., Uchida T., Sakai T., Kamo M., Matsui T.,
RA Watanabe Y., Morimasa T., Hosokawa K., Toda T.;
RT "Proteome analysis of mouse brain: two-dimensional electrophoresis profiles
RT of tissue proteins during the course of aging.";
RL Electrophoresis 21:1853-1871(2000).
RN [4]
RP PROTEIN SEQUENCE OF 29-48; 72-81; 89-126; 138-147; 153-219; 258-267;
RP 275-297; 303-329; 370-375; 387-394 AND 402-449, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
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 [6]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81; LYS-104 AND LYS-375, AND
RP IDENTIFICATION BY MASS 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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-257, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [9]
RP INTERACTION WITH RAB5IF.
RX PubMed=31536960; DOI=10.1016/j.isci.2019.08.057;
RA Moutaoufik M.T., Malty R., Amin S., Zhang Q., Phanse S., Gagarinova A.,
RA Zilocchi M., Hoell L., Minic Z., Gagarinova M., Aoki H., Stockwell J.,
RA Jessulat M., Goebels F., Broderick K., Scott N.E., Vlasblom J., Musso G.,
RA Prasad B., Lamantea E., Garavaglia B., Rajput A., Murayama K., Okazaki Y.,
RA Foster L.J., Bader G.D., Cayabyab F.S., Babu M.;
RT "Rewiring of the Human Mitochondrial Interactome during Neuronal
RT Reprogramming Reveals Regulators of the Respirasome and Neurogenesis.";
RL IScience 19:1114-1132(2019).
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. {ECO:0000250|UniProtKB:P25708}.
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (By similarity). This is
CC a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By
CC similarity). Interacts with RAB5IF (PubMed:31536960).
CC {ECO:0000250|UniProtKB:P49821, ECO:0000269|PubMed:31536960}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P25708}; Matrix side
CC {ECO:0000250|UniProtKB:P25708}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; AK075692; BAC35893.1; -; mRNA.
DR EMBL; BC014818; AAH14818.1; -; mRNA.
DR EMBL; BC041682; AAH41682.1; -; mRNA.
DR CCDS; CCDS29410.1; -.
DR PIR; PC7078; PC7078.
DR RefSeq; NP_598427.1; NM_133666.3.
DR PDB; 6G2J; EM; 3.30 A; F=30-457.
DR PDB; 6G72; EM; 3.90 A; F=1-464.
DR PDB; 6ZR2; EM; 3.10 A; F=1-464.
DR PDB; 6ZTQ; EM; 3.00 A; F=1-464.
DR PDB; 7AK5; EM; 3.17 A; F=1-464.
DR PDB; 7AK6; EM; 3.82 A; F=1-464.
DR PDB; 7B93; EM; 3.04 A; F=1-464.
DR PDB; 7PSA; EM; 3.40 A; F=1-464.
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; Q91YT0; -.
DR SMR; Q91YT0; -.
DR BioGRID; 201719; 69.
DR ComplexPortal; CPX-266; Mitochondrial respiratory chain complex I.
DR CORUM; Q91YT0; -.
DR IntAct; Q91YT0; 7.
DR MINT; Q91YT0; -.
DR STRING; 10090.ENSMUSP00000042967; -.
DR iPTMnet; Q91YT0; -.
DR PhosphoSitePlus; Q91YT0; -.
DR SwissPalm; Q91YT0; -.
DR EPD; Q91YT0; -.
DR jPOST; Q91YT0; -.
DR MaxQB; Q91YT0; -.
DR PaxDb; Q91YT0; -.
DR PeptideAtlas; Q91YT0; -.
DR PRIDE; Q91YT0; -.
DR ProteomicsDB; 287471; -.
DR Antibodypedia; 30465; 265 antibodies from 30 providers.
DR DNASU; 17995; -.
DR Ensembl; ENSMUST00000042497; ENSMUSP00000042967; ENSMUSG00000037916.
DR GeneID; 17995; -.
DR KEGG; mmu:17995; -.
DR UCSC; uc008fye.2; mouse.
DR CTD; 4723; -.
DR MGI; MGI:107851; Ndufv1.
DR VEuPathDB; HostDB:ENSMUSG00000037916; -.
DR eggNOG; KOG2658; Eukaryota.
DR GeneTree; ENSGT00390000010641; -.
DR HOGENOM; CLU_014881_1_0_1; -.
DR InParanoid; Q91YT0; -.
DR OMA; CDDVIMD; -.
DR OrthoDB; 549172at2759; -.
DR PhylomeDB; Q91YT0; -.
DR TreeFam; TF300381; -.
DR Reactome; R-MMU-611105; Respiratory electron transport.
DR Reactome; R-MMU-6799198; Complex I biogenesis.
DR BioGRID-ORCS; 17995; 23 hits in 61 CRISPR screens.
DR ChiTaRS; Ndufv1; mouse.
DR PRO; PR:Q91YT0; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q91YT0; protein.
DR Bgee; ENSMUSG00000037916; Expressed in soleus muscle and 267 other tissues.
DR ExpressionAtlas; Q91YT0; baseline and differential.
DR Genevisible; Q91YT0; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
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; IEA:UniProtKB-EC.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; ISO:MGI.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000269|PubMed:10870971"
FT CHAIN 21..464
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 1,
FT mitochondrial"
FT /id="PRO_0000019978"
FT BINDING 87..96
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250"
FT BINDING 199..247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 81
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 81
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT MOD_RES 257
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23576753"
FT STRAND 37..39
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 41..46
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 73..83
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 95..98
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 112..117
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 126..131
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 135..148
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 163..179
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:7AK5"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 209..217
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:7B93"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 240..244
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 251..257
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 259..264
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 268..284
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 296..302
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 316..324
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 329..331
FT /evidence="ECO:0007829|PDB:6G2J"
FT STRAND 332..334
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 336..338
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 339..344
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 363..376
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 383..401
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 407..420
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT STRAND 422..425
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 427..441
FT /evidence="ECO:0007829|PDB:6ZTQ"
FT HELIX 443..455
FT /evidence="ECO:0007829|PDB:6ZTQ"
SQ SEQUENCE 464 AA; 50834 MW; 611EAB1546D2A630 CRC64;
MLAARHFLGG LVPVRVSVRF SSGTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALRRG
DWYKTKEILL KGPDWILGEM KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
EPGTCKDREI MRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
LIGKNACGSD YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNHPCTVEE EMSVPLKELI
EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS
TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV KGDARPAEID SLWEISKQIE
GHTICALGDG AAWPVQGLIR HFRPELEDRM QRFAQQHRAW QAAS
