NADK_HUMAN
ID NADK_HUMAN Reviewed; 446 AA.
AC O95544; A6NNN3; A8K296; B7Z434; F5GXR5; Q5QPS4; Q9H2P2; Q9H931;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=NAD kinase;
DE EC=2.7.1.23;
DE AltName: Full=Poly(P)/ATP NAD kinase;
GN Name=NADK;
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), CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND VARIANT LYS-262.
RC TISSUE=Fibroblast;
RX PubMed=11594753; DOI=10.1006/bbrc.2001.5735;
RA Lerner F., Niere M., Ludwig A., Ziegler M.;
RT "Structural and functional characterization of human NAD kinase.";
RL Biochem. Biophys. Res. Commun. 288:69-74(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Hypothalamus;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT LYS-262.
RC TISSUE=Lymph;
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48; SER-50 AND
RP SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46 AND SER-48, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-48; SER-50; SER-55
RP AND SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP 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 [12]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 68-426.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human NAD kinase.";
RL Submitted (NOV-2010) to the PDB data bank.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + NAD(+) = ADP + H(+) + NADP(+); 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:11594753};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:11594753};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.3 mM for ATP {ECO:0000269|PubMed:11594753};
CC KM=0.54 mM for NAD {ECO:0000269|PubMed:11594753};
CC Vmax=6.7 umol/min/mg enzyme {ECO:0000269|PubMed:11594753};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11594753};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:11594753};
CC -!- INTERACTION:
CC O95544; Q49AN0: CRY2; NbExp=3; IntAct=EBI-743949, EBI-2212355;
CC O95544; Q9H5Z6-2: FAM124B; NbExp=3; IntAct=EBI-743949, EBI-11986315;
CC O95544; Q8TBB1: LNX1; NbExp=5; IntAct=EBI-743949, EBI-739832;
CC O95544; O00560: SDCBP; NbExp=7; IntAct=EBI-743949, EBI-727004;
CC O95544; P63104: YWHAZ; NbExp=2; IntAct=EBI-743949, EBI-347088;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O95544-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95544-2; Sequence=VSP_047313, VSP_047314;
CC Name=3;
CC IsoId=O95544-3; Sequence=VSP_047312;
CC -!- TISSUE SPECIFICITY: Widely expressed but not detected in skeletal
CC muscle. {ECO:0000269|PubMed:11594753}.
CC -!- SIMILARITY: Belongs to the NAD kinase family. {ECO:0000305}.
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DR EMBL; AY090771; AAM01195.1; -; mRNA.
DR EMBL; AF250320; AAG44568.1; -; mRNA.
DR EMBL; AK023114; BAB14412.1; -; mRNA.
DR EMBL; AK290161; BAF82850.1; -; mRNA.
DR EMBL; AK296722; BAH12420.1; -; mRNA.
DR EMBL; AL031282; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471183; EAW56151.1; -; Genomic_DNA.
DR EMBL; CH471183; EAW56152.1; -; Genomic_DNA.
DR EMBL; BC001709; AAH01709.1; -; mRNA.
DR CCDS; CCDS30565.1; -. [O95544-1]
DR CCDS; CCDS55562.1; -. [O95544-2]
DR RefSeq; NP_001185922.1; NM_001198993.1. [O95544-1]
DR RefSeq; NP_001185923.1; NM_001198994.1. [O95544-2]
DR RefSeq; NP_001185924.1; NM_001198995.1.
DR RefSeq; NP_075394.3; NM_023018.4. [O95544-1]
DR RefSeq; XP_005244835.1; XM_005244778.2.
DR RefSeq; XP_006710900.1; XM_006710837.2.
DR PDB; 3PFN; X-ray; 2.70 A; A/B/C/D=68-426.
DR PDBsum; 3PFN; -.
DR AlphaFoldDB; O95544; -.
DR SMR; O95544; -.
DR BioGRID; 122408; 74.
DR IntAct; O95544; 14.
DR MINT; O95544; -.
DR BindingDB; O95544; -.
DR ChEMBL; CHEMBL6177; -.
DR iPTMnet; O95544; -.
DR MetOSite; O95544; -.
DR PhosphoSitePlus; O95544; -.
DR BioMuta; NADK; -.
DR EPD; O95544; -.
DR jPOST; O95544; -.
DR MassIVE; O95544; -.
DR MaxQB; O95544; -.
DR PaxDb; O95544; -.
DR PeptideAtlas; O95544; -.
DR PRIDE; O95544; -.
DR ProteomicsDB; 24500; -.
DR ProteomicsDB; 50936; -. [O95544-1]
DR ProteomicsDB; 63692; -.
DR Antibodypedia; 26587; 158 antibodies from 24 providers.
DR DNASU; 65220; -.
DR Ensembl; ENST00000341426.9; ENSP00000341679.5; ENSG00000008130.15. [O95544-1]
DR Ensembl; ENST00000341991.7; ENSP00000344340.3; ENSG00000008130.15. [O95544-1]
DR Ensembl; ENST00000378625.5; ENSP00000367890.1; ENSG00000008130.15. [O95544-2]
DR GeneID; 65220; -.
DR KEGG; hsa:65220; -.
DR MANE-Select; ENST00000341426.9; ENSP00000341679.5; NM_023018.5; NP_075394.3.
DR UCSC; uc001aic.3; human. [O95544-1]
DR CTD; 65220; -.
DR DisGeNET; 65220; -.
DR GeneCards; NADK; -.
DR HGNC; HGNC:29831; NADK.
DR HPA; ENSG00000008130; Low tissue specificity.
DR MIM; 611616; gene.
DR neXtProt; NX_O95544; -.
DR OpenTargets; ENSG00000008130; -.
DR PharmGKB; PA142671298; -.
DR VEuPathDB; HostDB:ENSG00000008130; -.
DR eggNOG; KOG2178; Eukaryota.
DR GeneTree; ENSGT00390000013792; -.
DR HOGENOM; CLU_008831_10_3_1; -.
DR InParanoid; O95544; -.
DR OrthoDB; 1263874at2759; -.
DR PhylomeDB; O95544; -.
DR TreeFam; TF324076; -.
DR BioCyc; MetaCyc:HS00233-MON; -.
DR BRENDA; 2.7.1.23; 2681.
DR PathwayCommons; O95544; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SABIO-RK; O95544; -.
DR SignaLink; O95544; -.
DR BioGRID-ORCS; 65220; 32 hits in 1087 CRISPR screens.
DR ChiTaRS; NADK; human.
DR EvolutionaryTrace; O95544; -.
DR GeneWiki; NAD%2B_kinase; -.
DR GenomeRNAi; 65220; -.
DR Pharos; O95544; Tbio.
DR PRO; PR:O95544; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95544; protein.
DR Bgee; ENSG00000008130; Expressed in blood and 200 other tissues.
DR ExpressionAtlas; O95544; baseline and differential.
DR Genevisible; O95544; HS.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB.
DR GO; GO:0046034; P:ATP metabolic process; NAS:UniProtKB.
DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro.
DR GO; GO:0006741; P:NADP biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; NAS:UniProtKB.
DR Gene3D; 2.60.200.30; -; 1.
DR Gene3D; 3.40.50.10330; -; 1.
DR HAMAP; MF_00361; NAD_kinase; 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 Pfam; PF01513; NAD_kinase; 1.
DR SUPFAM; SSF111331; SSF111331; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Kinase; Metal-binding;
KW NAD; NADP; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW Transferase.
FT CHAIN 1..446
FT /note="NAD kinase"
FT /id="PRO_0000120713"
FT MOD_RES 46
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 55
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 11..87
FT /note="NKELSPDAAAYCCSACHGDETWSYNHPIRGRAKSRSLSASPALGSTKEFRRT
FT RSLHGPCPVTTFGPKACVLQNPQTI -> GRPRVRQAWPGCCGHTGRLPAGRGYLASHM
FT CDPAGAELIGDGMSDPTPPSNACT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047312"
FT VAR_SEQ 88
FT /note="M -> IATPLSLASQLLPSPAVSHSGQGGVTGQVHVLPQPSDQGVLSGPRAA
FT RGQTAPQEEAVTQEEVEALVCGHTQRWVPGPVYDAAAGGSGWAQLSLRAGMGVGQATG
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047313"
FT VAR_SEQ 131
FT /note="E -> EARGAGGKGAWGAHGVGGASIHITAPRVGSAGGMSRLALCFQ (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047314"
FT VARIANT 262
FT /note="N -> K (in dbSNP:rs4751)"
FT /evidence="ECO:0000269|PubMed:11594753,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_034119"
FT CONFLICT 363
FT /note="Missing (in Ref. 2; AAG44568)"
FT /evidence="ECO:0000305"
FT CONFLICT 445
FT /note="E -> EE (in Ref. 2; BAB14412)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="G -> EG (in Ref. 3; BAH12420)"
FT /evidence="ECO:0000305"
FT TURN 75..77
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 78..80
FT /evidence="ECO:0007829|PDB:3PFN"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3PFN"
FT TURN 93..95
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 97..102
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 116..118
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 119..131
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:3PFN"
FT TURN 166..168
FT /evidence="ECO:0007829|PDB:3PFN"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 176..183
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:3PFN"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 220..229
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 277..289
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 299..303
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 306..311
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 313..319
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 321..325
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 327..330
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:3PFN"
FT STRAND 405..408
FT /evidence="ECO:0007829|PDB:3PFN"
FT HELIX 413..424
FT /evidence="ECO:0007829|PDB:3PFN"
SQ SEQUENCE 446 AA; 49228 MW; 48CE7AF05EDD7E8B CRC64;
MEMEQEKMTM NKELSPDAAA YCCSACHGDE TWSYNHPIRG RAKSRSLSAS PALGSTKEFR
RTRSLHGPCP VTTFGPKACV LQNPQTIMHI QDPASQRLTW NKSPKSVLVI KKMRDASLLQ
PFKELCTHLM EENMIVYVEK KVLEDPAIAS DESFGAVKKK FCTFREDYDD ISNQIDFIIC
LGGDGTLLYA SSLFQGSVPP VMAFHLGSLG FLTPFSFENF QSQVTQVIEG NAAVVLRSRL
KVRVVKELRG KKTAVHNGLG ENGSQAAGLD MDVGKQAMQY QVLNEVVIDR GPSSYLSNVD
VYLDGHLITT VQGDGVIVST PTGSTAYAAA AGASMIHPNV PAIMITPICP HSLSFRPIVV
PAGVELKIML SPEARNTAWV SFDGRKRQEI RHGDSISITT SCYPLPSICV RDPVSDWFES
LAQCLHWNVR KKQAHFEEEE EEEEEG
