NDUA5_HUMAN
ID NDUA5_HUMAN Reviewed; 116 AA.
AC Q16718; B2RD98; Q5H9R2; Q6IRX7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 183.
DE RecName: Full=NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 5;
DE AltName: Full=Complex I subunit B13;
DE AltName: Full=Complex I-13kD-B;
DE Short=CI-13kD-B;
DE AltName: Full=NADH-ubiquinone oxidoreductase 13 kDa-B subunit;
GN Name=NDUFA5;
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=9048877; DOI=10.1016/s0167-4781(96)00208-4;
RA Pata I., Tensing K., Metspalu A.;
RT "A human cDNA encoding the homologue of NADH:ubiquinone oxidoreductase
RT subunit B13.";
RL Biochim. Biophys. Acta 1350:115-118(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9021153; DOI=10.1007/s003359900350;
RA Russell M.W., du Manoir S., Collins F.S., Brody L.C.;
RT "Cloning of the human NADH:ubiquinone oxidoreductase subunit B13:
RT localization to chromosome 7q32 and identification of a pseudogene on
RT 11p15.";
RL Mamm. Genome 8:60-61(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10343126; DOI=10.1159/000015237;
RA Tensing K., Pata I., Wittig I., Wehnert M., Metspalu A.;
RT "Genomic organization of the human complex I 13-kDa subunit gene NDUFA5.";
RL Cytogenet. Cell Genet. 84:125-127(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, Placenta, and Skeletal muscle;
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 [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30 AND LYS-60, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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 [13]
RP IDENTIFICATION BY 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).
RN [14]
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 [15]
RP FUNCTION, AND IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
RX PubMed=27626371; DOI=10.1038/nature19754;
RA Stroud D.A., Surgenor E.E., Formosa L.E., Reljic B., Frazier A.E.,
RA Dibley M.G., Osellame L.D., Stait T., Beilharz T.H., Thorburn D.R.,
RA Salim A., Ryan M.T.;
RT "Accessory subunits are integral for assembly and function of human
RT mitochondrial complex I.";
RL Nature 538:123-126(2016).
CC -!- FUNCTION: Accessory subunit of the mitochondrial membrane respiratory
CC chain NADH dehydrogenase (Complex I), that is believed not to be
CC involved in catalysis. Complex I functions in the transfer of electrons
CC from NADH to the respiratory chain. The immediate electron acceptor for
CC the enzyme is believed to be ubiquinone. {ECO:0000269|PubMed:27626371}.
CC -!- SUBUNIT: Complex I is composed of 45 different subunits.
CC {ECO:0000269|PubMed:12611891, ECO:0000269|PubMed:27626371}.
CC -!- INTERACTION:
CC Q16718; Q92993: KAT5; NbExp=3; IntAct=EBI-746417, EBI-399080;
CC Q16718; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-746417, EBI-11742507;
CC Q16718; O75489: NDUFS3; NbExp=12; IntAct=EBI-746417, EBI-1224896;
CC Q16718; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-746417, EBI-742388;
CC Q16718; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-746417, EBI-9090795;
CC Q16718; P02766: TTR; NbExp=3; IntAct=EBI-746417, EBI-711909;
CC Q16718; P61981: YWHAG; NbExp=3; IntAct=EBI-746417, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:12611891}; Peripheral membrane protein
CC {ECO:0000305}; Matrix side {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q16718-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q16718-2; Sequence=VSP_055164;
CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined with highest
CC levels in heart, skeletal muscle and brain.
CC {ECO:0000269|PubMed:9048877}.
CC -!- SIMILARITY: Belongs to the complex I NDUFA5 subunit family.
CC {ECO:0000305}.
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DR EMBL; U53468; AAB02224.1; -; mRNA.
DR EMBL; U64028; AAB37259.1; -; mRNA.
DR EMBL; AF044418; AAD21526.1; -; Genomic_DNA.
DR EMBL; AF044415; AAD21526.1; JOINED; Genomic_DNA.
DR EMBL; AF044416; AAD21526.1; JOINED; Genomic_DNA.
DR EMBL; AF044417; AAD21526.1; JOINED; Genomic_DNA.
DR EMBL; BT006695; AAP35341.1; -; mRNA.
DR EMBL; AK315458; BAG37845.1; -; mRNA.
DR EMBL; CR933664; CAI45962.1; -; mRNA.
DR EMBL; AC073323; AAQ96854.1; -; Genomic_DNA.
DR EMBL; CH471070; EAW83588.1; -; Genomic_DNA.
DR EMBL; BC000813; AAH00813.1; -; mRNA.
DR EMBL; BC020821; AAH20821.1; -; mRNA.
DR EMBL; BC070236; AAH70236.1; -; mRNA.
DR EMBL; BC070237; AAH70237.1; -; mRNA.
DR CCDS; CCDS5788.1; -. [Q16718-1]
DR CCDS; CCDS64760.1; -. [Q16718-2]
DR PIR; G02526; G02526.
DR RefSeq; NP_001269348.1; NM_001282419.2.
DR RefSeq; NP_001269349.1; NM_001282420.2. [Q16718-2]
DR RefSeq; NP_001269350.1; NM_001282421.2.
DR RefSeq; NP_001269351.1; NM_001282422.2.
DR RefSeq; NP_004991.1; NM_005000.4. [Q16718-1]
DR PDB; 5XTB; EM; 3.40 A; H=5-116.
DR PDB; 5XTD; EM; 3.70 A; H=5-116.
DR PDB; 5XTH; EM; 3.90 A; H=5-116.
DR PDB; 5XTI; EM; 17.40 A; BH/H=5-116.
DR PDBsum; 5XTB; -.
DR PDBsum; 5XTD; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR AlphaFoldDB; Q16718; -.
DR SMR; Q16718; -.
DR BioGRID; 110778; 219.
DR ComplexPortal; CPX-577; Mitochondrial respiratory chain complex I.
DR CORUM; Q16718; -.
DR IntAct; Q16718; 76.
DR MINT; Q16718; -.
DR STRING; 9606.ENSP00000417142; -.
DR BindingDB; Q16718; -.
DR ChEMBL; CHEMBL2363065; -.
DR DrugBank; DB00157; NADH.
DR DrugCentral; Q16718; -.
DR CarbonylDB; Q16718; -.
DR iPTMnet; Q16718; -.
DR PhosphoSitePlus; Q16718; -.
DR SwissPalm; Q16718; -.
DR BioMuta; NDUFA5; -.
DR DMDM; 2499316; -.
DR EPD; Q16718; -.
DR jPOST; Q16718; -.
DR MassIVE; Q16718; -.
DR MaxQB; Q16718; -.
DR PaxDb; Q16718; -.
DR PeptideAtlas; Q16718; -.
DR PRIDE; Q16718; -.
DR ProteomicsDB; 61039; -. [Q16718-1]
DR ProteomicsDB; 62900; -.
DR TopDownProteomics; Q16718-1; -. [Q16718-1]
DR Antibodypedia; 31753; 197 antibodies from 29 providers.
DR DNASU; 4698; -.
DR Ensembl; ENST00000355749.7; ENSP00000347988.2; ENSG00000128609.16. [Q16718-1]
DR Ensembl; ENST00000471770.5; ENSP00000417142.1; ENSG00000128609.16. [Q16718-2]
DR GeneID; 4698; -.
DR KEGG; hsa:4698; -.
DR MANE-Select; ENST00000355749.7; ENSP00000347988.2; NM_005000.5; NP_004991.1.
DR UCSC; uc003vks.4; human. [Q16718-1]
DR CTD; 4698; -.
DR DisGeNET; 4698; -.
DR GeneCards; NDUFA5; -.
DR HGNC; HGNC:7688; NDUFA5.
DR HPA; ENSG00000128609; Tissue enhanced (tongue).
DR MIM; 601677; gene.
DR neXtProt; NX_Q16718; -.
DR OpenTargets; ENSG00000128609; -.
DR PharmGKB; PA31494; -.
DR VEuPathDB; HostDB:ENSG00000128609; -.
DR eggNOG; KOG3365; Eukaryota.
DR GeneTree; ENSGT00390000008099; -.
DR HOGENOM; CLU_099943_2_0_1; -.
DR InParanoid; Q16718; -.
DR OMA; VNEHPHR; -.
DR OrthoDB; 1372253at2759; -.
DR PhylomeDB; Q16718; -.
DR TreeFam; TF313785; -.
DR BioCyc; MetaCyc:HS05206-MON; -.
DR PathwayCommons; Q16718; -.
DR Reactome; R-HSA-611105; Respiratory electron transport.
DR Reactome; R-HSA-6799198; Complex I biogenesis.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q16718; -.
DR SIGNOR; Q16718; -.
DR BioGRID-ORCS; 4698; 173 hits in 1042 CRISPR screens.
DR ChiTaRS; NDUFA5; human.
DR GeneWiki; NDUFA5; -.
DR GenomeRNAi; 4698; -.
DR Pharos; Q16718; Tclin.
DR PRO; PR:Q16718; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q16718; protein.
DR Bgee; ENSG00000128609; Expressed in endothelial cell and 202 other tissues.
DR ExpressionAtlas; Q16718; baseline and differential.
DR Genevisible; Q16718; HS.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:ComplexPortal.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; TAS:ProtInc.
DR GO; GO:0009060; P:aerobic respiration; IC:ComplexPortal.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; NAS: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 GO; GO:0022904; P:respiratory electron transport chain; IBA:GO_Central.
DR InterPro; IPR006806; NDUFA5.
DR PANTHER; PTHR12653; PTHR12653; 1.
DR Pfam; PF04716; ETC_C1_NDUFA5; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Electron transport;
KW Membrane; Mitochondrion; Mitochondrion inner membrane; Reference proteome;
KW Respiratory chain; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P23935"
FT CHAIN 2..116
FT /note="NADH dehydrogenase [ubiquinone] 1 alpha subcomplex
FT subunit 5"
FT /id="PRO_0000118632"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P23935"
FT MOD_RES 30
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 46
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT MOD_RES 60
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 98
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT MOD_RES 98
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9CPP6"
FT VAR_SEQ 1..7
FT /note="MAGVLKK -> MPYRVGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_055164"
FT CONFLICT 52
FT /note="T -> I (in Ref. 9; AAH70236)"
FT /evidence="ECO:0000305"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 20..35
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 43..61
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 65..71
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 80..94
FT /evidence="ECO:0007829|PDB:5XTB"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:5XTB"
FT TURN 109..112
FT /evidence="ECO:0007829|PDB:5XTB"
SQ SEQUENCE 116 AA; 13459 MW; 652339C1127E6F22 CRC64;
MAGVLKKTTG LVGLAVCNTP HERLRILYTK ILDVLEEIPK NAAYRKYTEQ ITNEKLAMVK
AEPDVKKLED QLQGGQLEEV ILQAEHELNL ARKMREWKLW EPLVEEPPAD QWKWPI
