NDUS7_HUMAN
ID NDUS7_HUMAN Reviewed; 213 AA.
AC O75251; B3KRI2; Q2T9H7; Q9BV17;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 3.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=NADH dehydrogenase [ubiquinone] iron-sulfur protein 7, mitochondrial;
DE EC=7.1.1.2 {ECO:0000269|PubMed:17275378};
DE AltName: Full=Complex I-20kD;
DE Short=CI-20kD;
DE AltName: Full=NADH-ubiquinone oxidoreductase 20 kDa subunit;
DE AltName: Full=PSST subunit {ECO:0000303|PubMed:8938450};
DE Flags: Precursor;
GN Name=NDUFS7;
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] (ISOFORM 1).
RX PubMed=8938450; DOI=10.1006/geno.1996.0572;
RA Hyslop S.J., Duncan A.M.V., Pitkanen S., Robinson B.H.;
RT "Assignment of the PSST subunit gene of human mitochondrial complex I to
RT chromosome 19p13.";
RL Genomics 37:375-380(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LEU-23.
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 IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX,
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=12611891; DOI=10.1074/jbc.c300064200;
RA Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F.,
RA Ghosh S.S., Capaldi R.A.;
RT "The subunit composition of the human NADH dehydrogenase obtained by rapid
RT one-step immunopurification.";
RL J. Biol. Chem. 278:13619-13622(2003).
RN [6]
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 [7]
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 [8]
RP HYDROXYLATION AT ARG-111.
RX PubMed=27226634; DOI=10.1074/jbc.m116.734970;
RA Rhein V.F., Carroll J., Ding S., Fearnley I.M., Walker J.E.;
RT "NDUFAF5 hydroxylates NDUFS7 at an early stage in the assembly of human
RT complex I.";
RL J. Biol. Chem. 291:14851-14860(2016).
RN [9]
RP INVOLVEMENT IN MC1DN3, AND VARIANT MC1DN3 MET-122.
RX PubMed=10360771;
RX DOI=10.1002/1531-8249(199906)45:6<787::aid-ana13>3.0.co;2-6;
RA Triepels R.H., van den Heuvel L., Loeffen J.L.C.M., Buskens C.A.F.,
RA Smeets R.J.P., Rubio Gozalbo M.E., Budde S.M., Mariman E.C.M.,
RA Wijburg F.A., Barth P.G., Trijbels J.M.F., Smeitink J.A.M.;
RT "Leigh syndrome associated with a mutation in the NDUFS7 (PSST) nuclear
RT encoded subunit of complex I.";
RL Ann. Neurol. 45:787-790(1999).
RN [10]
RP INVOLVEMENT IN MC1DN3, AND VARIANT MC1DN3 MET-122.
RX PubMed=10330338; DOI=10.1086/302432;
RA Smeitink J., van den Heuvel L.;
RT "Human mitochondrial complex I in health and disease.";
RL Am. J. Hum. Genet. 64:1505-1510(1999).
RN [11]
RP VARIANT HIS-145, CHARACTERIZATION OF VARIANT HIS-145, FUNCTION, AND
RP CATALYTIC ACTIVITY.
RX PubMed=17275378; DOI=10.1016/j.ymgme.2006.12.007;
RA Lebon S., Rodriguez D., Bridoux D., Zerrad A., Roetig A., Munnich A.,
RA Legrand A., Slama A.;
RT "A novel mutation in the human complex I NDUFS7 subunit associated with
RT Leigh syndrome.";
RL Mol. Genet. Metab. 90:379-382(2007).
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:17275378). Essential for the catalytic activity of
CC complex I (PubMed:17275378). {ECO:0000269|PubMed:17275378}.
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:17275378};
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 (PubMed:12611891). This
CC is a component of the iron-sulfur (IP) fragment of the enzyme (By
CC similarity). {ECO:0000250|UniProtKB:P42026,
CC ECO:0000269|PubMed:12611891}.
CC -!- INTERACTION:
CC O75251; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-719652, EBI-1055254;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P42026}; Matrix side
CC {ECO:0000250|UniProtKB:P42026}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75251-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75251-2; Sequence=VSP_057067;
CC -!- PTM: Hydroxylated ar Arg-111 by NDUFAF5 early in the pathway of
CC assembly of complex I, before the formation of the juncture between
CC peripheral and membrane arms. {ECO:0000269|PubMed:27226634}.
CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 3 (MC1DN3)
CC [MIM:618224]: A form of mitochondrial complex I deficiency, the most
CC common biochemical signature of mitochondrial disorders, a group of
CC highly heterogeneous conditions characterized by defective oxidative
CC phosphorylation, which collectively affects 1 in 5-10000 live births.
CC Clinical disorders have variable severity, ranging from lethal neonatal
CC disease to adult-onset neurodegenerative disorders. Phenotypes include
CC macrocephaly with progressive leukodystrophy, non-specific
CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh
CC syndrome, Leber hereditary optic neuropathy, and some forms of
CC Parkinson disease. MC1DN3 transmission pattern is consistent with
CC autosomal recessive inheritance. {ECO:0000269|PubMed:10330338,
CC ECO:0000269|PubMed:10360771}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC27669.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK091623; BAG52394.1; -; mRNA.
DR EMBL; AC005329; AAC27669.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC001715; AAH01715.2; -; mRNA.
DR EMBL; BC005954; AAH05954.1; -; mRNA.
DR EMBL; BC111517; AAI11518.1; -; mRNA.
DR CCDS; CCDS12063.1; -. [O75251-1]
DR RefSeq; NP_077718.3; NM_024407.4. [O75251-1]
DR PDB; 5XTB; EM; 3.40 A; C=58-213.
DR PDB; 5XTD; EM; 3.70 A; C=58-213.
DR PDB; 5XTH; EM; 3.90 A; C=58-213.
DR PDB; 5XTI; EM; 17.40 A; BC/C=58-213.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; O75251; -.
DR SMR; O75251; -.
DR BioGRID; 131889; 299.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; O75251; -.
DR IntAct; O75251; 99.
DR MINT; O75251; -.
DR STRING; 9606.ENSP00000233627; -.
DR BindingDB; O75251; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00997; Doxorubicin.
DR DrugBank; DB00157; NADH.
DR DrugCentral; O75251; -.
DR GlyGen; O75251; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75251; -.
DR MetOSite; O75251; -.
DR PhosphoSitePlus; O75251; -.
DR SwissPalm; O75251; -.
DR BioMuta; NDUFS7; -.
DR EPD; O75251; -.
DR jPOST; O75251; -.
DR MassIVE; O75251; -.
DR MaxQB; O75251; -.
DR PaxDb; O75251; -.
DR PeptideAtlas; O75251; -.
DR PRIDE; O75251; -.
DR ProteomicsDB; 3604; -.
DR ProteomicsDB; 49873; -. [O75251-1]
DR TopDownProteomics; O75251-1; -. [O75251-1]
DR Antibodypedia; 22663; 167 antibodies from 31 providers.
DR DNASU; 374291; -.
DR Ensembl; ENST00000233627.14; ENSP00000233627.9; ENSG00000115286.21. [O75251-1]
DR Ensembl; ENST00000313408.11; ENSP00000364262.5; ENSG00000115286.21. [O75251-2]
DR Ensembl; ENST00000546283.5; ENSP00000440348.1; ENSG00000115286.21. [O75251-2]
DR GeneID; 374291; -.
DR KEGG; hsa:374291; -.
DR MANE-Select; ENST00000233627.14; ENSP00000233627.9; NM_024407.5; NP_077718.3.
DR UCSC; uc060qzv.1; human. [O75251-1]
DR CTD; 374291; -.
DR DisGeNET; 374291; -.
DR GeneCards; NDUFS7; -.
DR GeneReviews; NDUFS7; -.
DR HGNC; HGNC:7714; NDUFS7.
DR HPA; ENSG00000115286; Tissue enriched (skeletal).
DR MalaCards; NDUFS7; -.
DR MIM; 601825; gene.
DR MIM; 618224; phenotype.
DR neXtProt; NX_O75251; -.
DR OpenTargets; ENSG00000115286; -.
DR Orphanet; 2609; Isolated complex I deficiency.
DR Orphanet; 255241; Leigh syndrome with leukodystrophy.
DR PharmGKB; PA31524; -.
DR VEuPathDB; HostDB:ENSG00000115286; -.
DR eggNOG; KOG1687; Eukaryota.
DR GeneTree; ENSGT00390000006565; -.
DR HOGENOM; CLU_055737_1_2_1; -.
DR InParanoid; O75251; -.
DR OMA; AGWVRKS; -.
DR PhylomeDB; O75251; -.
DR TreeFam; TF312859; -.
DR BioCyc; MetaCyc:HS03864-MON; -.
DR PathwayCommons; O75251; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR SignaLink; O75251; -.
DR SIGNOR; O75251; -.
DR BioGRID-ORCS; 374291; 172 hits in 1081 CRISPR screens.
DR ChiTaRS; NDUFS7; human.
DR GeneWiki; NDUFS7; -.
DR GenomeRNAi; 374291; -.
DR Pharos; O75251; Tclin.
DR PRO; PR:O75251; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O75251; protein.
DR Bgee; ENSG00000115286; Expressed in hindlimb stylopod muscle and 190 other tissues.
DR ExpressionAtlas; O75251; baseline and differential.
DR Genevisible; O75251; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IEA:Ensembl.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0097060; C:synaptic membrane; IEA:Ensembl.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IMP:UniProtKB.
DR GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; NAS:UniProtKB.
DR GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR GO; GO:0009060; P:aerobic respiration; IBA:GO_Central.
DR GO; GO:0015990; P:electron transport coupled proton transport; IBA:GO_Central.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IMP:UniProtKB.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IMP:UniProtKB.
DR GO; GO:0042776; P:proton motive force-driven mitochondrial ATP synthesis; IC:ComplexPortal.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Alternative splicing; Disease variant;
KW Electron transport; Hydroxylation; Iron; Iron-sulfur; Leigh syndrome;
KW Membrane; Metal-binding; Mitochondrion; Mitochondrion inner membrane; NAD;
KW Oxidoreductase; Primary mitochondrial disease; Reference proteome;
KW Respiratory chain; Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..38
FT /note="Mitochondrion"
FT /evidence="ECO:0000250|UniProtKB:P42026"
FT CHAIN 39..213
FT /note="NADH dehydrogenase [ubiquinone] iron-sulfur protein
FT 7, mitochondrial"
FT /id="PRO_0000020027"
FT REGION 31..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 88
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 153
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 183
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 111
FT /note="Hydroxyarginine"
FT /evidence="ECO:0000250|UniProtKB:P42026"
FT VAR_SEQ 183..213
FT /note="CPPTAEALLYGILQLQRKIKRERRLQIWYRR -> RAGTAPPTRELETGPAP
FT HGARRPL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057067"
FT VARIANT 23
FT /note="P -> L (in dbSNP:rs1142530)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_014482"
FT VARIANT 122
FT /note="V -> M (in MC1DN3; dbSNP:rs104894705)"
FT /evidence="ECO:0000269|PubMed:10330338,
FT ECO:0000269|PubMed:10360771"
FT /id="VAR_008848"
FT VARIANT 145
FT /note="R -> H (found in a patient with Leigh syndrome;
FT unknown pathological significance; decrease in enzyme
FT activity; dbSNP:rs121434479)"
FT /evidence="ECO:0000269|PubMed:17275378"
FT /id="VAR_084360"
FT HELIX 60..76
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 128..130
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 131..140
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 151..156
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5XTB"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 187..202
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 206..211
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 213 AA; 23564 MW; B3547EA24643C1B0 CRC64;
MAVLSAPGLR GFRILGLRSS VGPAVQARGV HQSVATDGPS STQPALPKAR AVAPKPSSRG
EYVVAKLDDL VNWARRSSLW PMTFGLACCA VEMMHMAAPR YDMDRFGVVF RASPRQSDVM
IVAGTLTNKM APALRKVYDQ MPEPRYVVSM GSCANGGGYY HYSYSVVRGC DRIVPVDIYI
PGCPPTAEAL LYGILQLQRK IKRERRLQIW YRR
