ID   NADK2_HUMAN             Reviewed;         442 AA.
AC   Q4G0N4; B5MC93; Q6UTX5; Q96NM0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   10-JUN-2026, entry version 146.
DE   RecName: Full=NAD kinase 2, mitochondrial;
DE            EC=2.7.1.23;
DE   AltName: Full=Mitochondrial NAD kinase;
DE   AltName: Full=NAD kinase domain-containing protein 1, mitochondrial;
DE   Flags: Precursor;
GN   Name=NADK2; Synonyms=C5orf33, MNADK, NADKD1;
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 [LARGE SCALE MRNA] (ISOFORM 3).
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 39-442 (ISOFORM 1).
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 164-442 (ISOFORM 2).
RA   Li H., Yu R., Zhou G., Shen C., Xiao W., Li M., Ke R., Zhong G., Lin L.,
RA   Yang S.;
RL   Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN   [5]
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   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, ACTIVITY REGULATION, AND TISSUE SPECIFICITY.
RX   PubMed=23212377; DOI=10.1038/ncomms2262;
RA   Ohashi K., Kawai S., Murata K.;
RT   "Identification and characterization of a human mitochondrial NAD kinase.";
RL   Nat. Commun. 3:1248-1248(2012).
RN   [7]
RP   INVOLVEMENT IN DECRD.
RX   PubMed=24847004; DOI=10.1093/hmg/ddu218;
RA   Houten S.M., Denis S., Te Brinke H., Jongejan A., van Kampen A.H.,
RA   Bradley E.J., Baas F., Hennekam R.C., Millington D.S., Young S.P.,
RA   Frazier D.M., Gucsavas-Calikoglu M., Wanders R.J.;
RT   "Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes
RT   dienoyl-CoA reductase deficiency with hyperlysinemia.";
RL   Hum. Mol. Genet. 23:5009-5016(2014).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-367, AND
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   [9]
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).
CC   -!- FUNCTION: Mitochondrial NAD(+) kinase that phosphorylates NAD(+) to
CC       yield NADP(+). Can use both ATP or inorganic polyphosphate as the
CC       phosphoryl donor. Also has weak NADH kinase activity in vitro; however
CC       NADH kinase activity is much weaker than the NAD(+) kinase activity and
CC       may not be relevant in vivo. {ECO:0000269|PubMed:23212377}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=NAD(+) + ATP = ADP + NADP(+) + H(+); Xref=Rhea:RHEA:18629,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:456216; EC=2.7.1.23;
CC         Evidence={ECO:0000269|PubMed:23212377};
CC   -!- ACTIVITY REGULATION: Inhibited by NADH, NADPH and NADP(+).
CC       {ECO:0000269|PubMed:23212377}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.022 mM for NAD(+) {ECO:0000269|PubMed:23212377};
CC         KM=1.7 mM for ATP {ECO:0000269|PubMed:23212377};
CC         KM=1.2 mM for tetrapolyphosphate {ECO:0000269|PubMed:23212377};
CC         Vmax=0.091 umol/min/mg enzyme {ECO:0000269|PubMed:23212377};
CC   -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:23212377}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:23212377}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q4G0N4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q4G0N4-2; Sequence=VSP_027193;
CC       Name=3;
CC         IsoId=Q4G0N4-3; Sequence=VSP_027192;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:23212377}.
CC   -!- DISEASE: 2,4-dienoyl-CoA reductase deficiency (DECRD) [MIM:616034]: A
CC       rare, autosomal recessive, inborn error of polyunsaturated fatty acids
CC       and lysine metabolism, resulting in mitochondrial dysfunction. Affected
CC       individuals have a severe encephalopathy with neurologic and metabolic
CC       abnormalities beginning in early infancy. Laboratory studies show
CC       increased C10:2 carnitine levels and hyperlysinemia.
CC       {ECO:0000269|PubMed:24847004}. Note=The disease is caused by variants
CC       affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
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DR   EMBL; AK055158; BAB70864.1; -; mRNA.
DR   EMBL; AC008807; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC008942; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC045565; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC062567; AAH62567.1; -; mRNA.
DR   EMBL; AY360463; AAQ62967.1; -; mRNA.
DR   CCDS; CCDS3917.1; -. [Q4G0N4-3]
DR   CCDS; CCDS47197.1; -. [Q4G0N4-1]
DR   RefSeq; NP_001078880.1; NM_001085411.3. [Q4G0N4-1]
DR   RefSeq; NP_001274269.1; NM_001287340.2. [Q4G0N4-3]
DR   RefSeq; NP_001274270.1; NM_001287341.1.
DR   RefSeq; NP_694558.1; NM_153013.5. [Q4G0N4-3]
DR   RefSeq; XP_047272662.1; XM_047416706.1. [Q4G0N4-3]
DR   RefSeq; XP_054207570.1; XM_054351595.1. [Q4G0N4-3]
DR   PDB; 7N29; X-ray; 2.80 A; A/B/C/D=47-442.
DR   PDB; 7R4J; X-ray; 2.95 A; A=61-442.
DR   PDB; 7R4K; X-ray; 3.33 A; A=61-442.
DR   PDB; 7R4L; X-ray; 2.60 A; A=61-442.
DR   PDB; 7R4M; X-ray; 2.29 A; A=61-442.
DR   PDBsum; 7N29; -.
DR   PDBsum; 7R4J; -.
DR   PDBsum; 7R4K; -.
DR   PDBsum; 7R4L; -.
DR   PDBsum; 7R4M; -.
DR   AlphaFoldDB; Q4G0N4; -.
DR   SMR; Q4G0N4; -.
DR   BioGRID; 126369; 74.
DR   FunCoup; Q4G0N4; 2206.
DR   IntAct; Q4G0N4; 12.
DR   MINT; Q4G0N4; -.
DR   STRING; 9606.ENSP00000371362; -.
DR   iPTMnet; Q4G0N4; -.
DR   PhosphoSitePlus; Q4G0N4; -.
DR   SwissPalm; Q4G0N4; -.
DR   BioMuta; NADK2; -.
DR   DMDM; 156630863; -.
DR   jPOST; Q4G0N4; -.
DR   MassIVE; Q4G0N4; -.
DR   PaxDb; 9606-ENSP00000371362; -.
DR   PeptideAtlas; Q4G0N4; -.
DR   ProteomicsDB; 62113; -. [Q4G0N4-1]
DR   ProteomicsDB; 62114; -. [Q4G0N4-2]
DR   ProteomicsDB; 62115; -. [Q4G0N4-3]
DR   Pumba; Q4G0N4; -.
DR   Antibodypedia; 50834; 150 antibodies from 20 providers.
DR   DNASU; 133686; -.
DR   Ensembl; ENST00000282512.7; ENSP00000282512.3; ENSG00000152620.14. [Q4G0N4-3]
DR   Ensembl; ENST00000381937.9; ENSP00000371362.4; ENSG00000152620.14. [Q4G0N4-1]
DR   Ensembl; ENST00000397338.5; ENSP00000380499.1; ENSG00000152620.14. [Q4G0N4-3]
DR   Ensembl; ENST00000514504.5; ENSP00000421029.1; ENSG00000152620.14. [Q4G0N4-2]
DR   GeneID; 133686; -.
DR   KEGG; hsa:133686; -.
DR   MANE-Select; ENST00000381937.9; ENSP00000371362.4; NM_001085411.3; NP_001078880.1.
DR   UCSC; uc003jkf.6; human. [Q4G0N4-1]
DR   AGR; HGNC:26404; -.
DR   ClinPGx; PA162380039; -.
DR   CTD; 133686; -.
DR   DisGeNET; 133686; -.
DR   GeneCards; NADK2; -.
DR   HGNC; HGNC:26404; NADK2.
DR   HPA; ENSG00000152620; Tissue enriched (liver).
DR   MalaCards; NADK2; -.
DR   MIM; 615787; gene.
DR   MIM; 616034; phenotype.
DR   OpenTargets; ENSG00000152620; -.
DR   Orphanet; 431361; Progressive encephalopathy with leukodystrophy due to DECR deficiency.
DR   VEuPathDB; HostDB:ENSG00000152620; -.
DR   eggNOG; KOG4180; Eukaryota.
DR   GeneTree; ENSGT00390000006320; -.
DR   HOGENOM; CLU_039559_0_0_1; -.
DR   InParanoid; Q4G0N4; -.
DR   OMA; WHFNINK; -.
DR   OrthoDB; 185618at2759; -.
DR   PAN-GO; Q4G0N4; 3 GO annotations based on evolutionary models.
DR   PhylomeDB; Q4G0N4; -.
DR   BRENDA; 2.7.1.23; 2681.
DR   PathwayCommons; Q4G0N4; -.
DR   Reactome; R-HSA-196807; Nicotinate metabolism.
DR   Reactome; R-HSA-9837999; Mitochondrial protein degradation.
DR   SABIO-RK; Q4G0N4; -.
DR   SignaLink; Q4G0N4; -.
DR   Agora; ENSG00000152620; -.
DR   BioGRID-ORCS; 133686; 26 hits in 1116 CRISPR screens.
DR   ChiTaRS; NADK2; human.
DR   GenomeRNAi; 133686; -.
DR   Pharos; Q4G0N4; Tbio.
DR   PRO; PR:Q4G0N4; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q4G0N4; protein.
DR   Bgee; ENSG00000152620; Expressed in liver and 198 other cell types or tissues.
DR   ExpressionAtlas; Q4G0N4; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0019674; P:NAD+ metabolic process; IDA:UniProtKB.
DR   GO; GO:0006741; P:NADP+ biosynthetic process; IEA:InterPro.
DR   FunFam; 3.40.50.10330:FF:000021; NAD kinase 2, mitochondrial; 1.
DR   Gene3D; 3.40.50.10330; Probable inorganic polyphosphate/atp-NAD kinase, domain 1; 1.
DR   Gene3D; 2.60.200.30; Probable inorganic polyphosphate/atp-NAD kinase, domain 2; 1.
DR   InterPro; IPR017438; ATP-NAD_kinase_N.
DR   InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_C.
DR   InterPro; IPR016064; NAD/diacylglycerol_kinase_sf.
DR   InterPro; IPR002504; NADK.
DR   InterPro; IPR012355; NADK2_mit.
DR   PANTHER; PTHR13158; -; 1.
DR   PANTHER; PTHR13158:SF5; NAD KINASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01513; NAD_kinase; 1.
DR   PIRSF; PIRSF017565; Kin_ATP-NAD_euk; 1.
DR   SUPFAM; SSF111331; NAD kinase/diacylglycerol kinase-like; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Alternative splicing; ATP-binding; Kinase;
KW   Mitochondrion; NAD; NADP; Nucleotide-binding; Phosphoprotein;
KW   Proteomics identification; Reference proteome; Transferase;
KW   Transit peptide.
FT   TRANSIT         1..62
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           63..442
FT                   /note="NAD kinase 2, mitochondrial"
FT                   /id="PRO_0000296292"
FT   REGION          24..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..36
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         76
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   MOD_RES         76
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   MOD_RES         188
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         302
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   MOD_RES         317
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   MOD_RES         317
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   MOD_RES         367
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         397
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C5H8"
FT   VAR_SEQ         1..163
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334"
FT                   /id="VSP_027192"
FT   VAR_SEQ         288..319
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_027193"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:7N29"
FT   STRAND          69..75
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           76..78
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           79..84
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   TURN            86..91
FT                   /evidence="ECO:0007829|PDB:7N29"
FT   HELIX           95..100
FT                   /evidence="ECO:0007829|PDB:7N29"
FT   STRAND          105..107
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           109..131
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          135..140
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           141..143
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           146..151
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          153..160
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           161..169
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          178..183
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   TURN            185..187
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           196..199
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           202..210
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          214..219
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          232..237
FT                   /evidence="ECO:0007829|PDB:7R4K"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:7N29"
FT   STRAND          265..284
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          289..295
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          301..306
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          308..311
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           314..317
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           319..324
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           325..327
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           328..340
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           350..362
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          373..377
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   TURN            383..385
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          391..402
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          405..411
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   TURN            412..414
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          415..418
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          423..429
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   HELIX           431..433
FT                   /evidence="ECO:0007829|PDB:7R4M"
FT   STRAND          435..439
FT                   /evidence="ECO:0007829|PDB:7R4M"
SQ   SEQUENCE   442 AA;  49433 MW;  289EA16979AF14D8 CRC64;
     MTCYRGFLLG SCCRVAGGRA AALRGPGAGG PAARPRLGGD GGGRRHLGQG QPRELAGCGS
     RADGGFRPSR VVVVAKTTRY EFEQQRYRYA ELSEEDLKQL LALKGSSYSG LLERHHIHTK
     NVEHIIDSLR NEGIEVRLVK RREYDEETVR WADAVIAAGG DGTMLLAASK VLDRLKPVIG
     VNTDPERSEG HLCLPVRYTH SFPEALQKFY RGEFRWLWRQ RIRLYLEGTG INPVPVDLHE
     QQLSLNQHNR ALNIERAHDE RSEASGPQLL PVRALNEVFI GESLSSRASY YEISVDDGPW
     EKQKSSGLNL CTGTGSKAWS FNINRVATQA VEDVLNIAKR QGNLSLPLNR ELVEKVTNEY
     NESLLYSPEE PKILFSIREP IANRVFSSSR QRCFSSKVCV RSRCWDACMV VDGGTSFEFN
     DGAIASMMIN KEDELRTVLL EQ
//