NAMPT_MOUSE
ID NAMPT_MOUSE Reviewed; 491 AA.
AC Q99KQ4; Q8C3B5; Q9JKM0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Nicotinamide phosphoribosyltransferase;
DE Short=NAmPRTase;
DE Short=Nampt;
DE EC=2.4.2.12 {ECO:0000269|PubMed:12555668, ECO:0000269|PubMed:15381699};
DE AltName: Full=Pre-B-cell colony-enhancing factor 1 homolog;
DE Short=PBEF;
DE AltName: Full=Visfatin;
GN Name=Nampt; Synonyms=Pbef1;
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 [MRNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell;
RX PubMed=12555668;
RX DOI=10.1002/1521-4141(200211)32:11<3225::aid-immu3225>3.0.co;2-l;
RA Rongvaux A., Shea R.J., Mulks M.H., Gigot D., Urbain J., Leo O., Andris F.;
RT "Pre-B-cell colony-enhancing factor, whose expression is up-regulated in
RT activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a
RT cytosolic enzyme involved in NAD biosynthesis.";
RL Eur. J. Immunol. 32:3225-3234(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND FUNCTION.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=15381699; DOI=10.1074/jbc.m408388200;
RA Revollo J.R., Grimm A.A., Imai S.;
RT "The NAD biosynthesis pathway mediated by nicotinamide
RT phosphoribosyltransferase regulates Sir2 activity in mammalian cells.";
RL J. Biol. Chem. 279:50754-50763(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Samal B.B., Sun N., Sun Y.;
RT "Mus musculus pre-B-cell colony-enhancing factor (PBEF) mRNA.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-368.
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=19299583; DOI=10.1126/science.1171641;
RA Ramsey K.M., Yoshino J., Brace C.S., Abrassart D., Kobayashi Y.,
RA Marcheva B., Hong H.K., Chong J.L., Buhr E.D., Lee C., Takahashi J.S.,
RA Imai S., Bass J.;
RT "Circadian clock feedback cycle through NAMPT-mediated NAD+ biosynthesis.";
RL Science 324:651-654(2009).
RN [7]
RP FUNCTION.
RX PubMed=19286518; DOI=10.1126/science.1170803;
RA Nakahata Y., Sahar S., Astarita G., Kaluzova M., Sassone-Corsi P.;
RT "Circadian control of the NAD+ salvage pathway by CLOCK-SIRT1.";
RL Science 324:654-657(2009).
RN [8]
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 [9]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=16783377; DOI=10.1038/nsmb1105;
RA Khan J.A., Tao X., Tong L.;
RT "Molecular basis for the inhibition of human NMPRTase, a novel target for
RT anticancer agents.";
RL Nat. Struct. Mol. Biol. 13:582-588(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH NICOTINAMIDE
RP MONONUCLEOTIDE, AND SUBUNIT.
RX PubMed=16783373; DOI=10.1038/nsmb1114;
RA Wang T., Zhang X., Bheda P., Revollo J.R., Imai S., Wolberger C.;
RT "Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme.";
RL Nat. Struct. Mol. Biol. 13:661-662(2006).
CC -!- FUNCTION: The secreted form behaves both as a cytokine with
CC immunomodulating properties and an adipokine with anti-diabetic
CC properties, it has no enzymatic activity, partly because of lack of
CC activation by ATP, which has a low level in extracellular space and
CC plasma (By similarity). Catalyzes the condensation of nicotinamide with
CC 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide,
CC an intermediate in the biosynthesis of NAD. It is the rate limiting
CC component in the mammalian NAD biosynthesis pathway. Plays a role in
CC the modulation of circadian clock function. NAMPT-dependent oscillatory
CC production of NAD regulates oscillation of clock target gene expression
CC by releasing the core clock component: CLOCK-ARNTL/BMAL1 heterodimer
CC from NAD-dependent SIRT1-mediated suppression.
CC {ECO:0000250|UniProtKB:P43490, ECO:0000269|PubMed:12555668,
CC ECO:0000269|PubMed:15381699, ECO:0000269|PubMed:19286518,
CC ECO:0000269|PubMed:19299583}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16149, ChEBI:CHEBI:14649, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017; EC=2.4.2.12;
CC Evidence={ECO:0000269|PubMed:12555668, ECO:0000269|PubMed:15381699};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:16151;
CC Evidence={ECO:0000269|PubMed:12555668, ECO:0000269|PubMed:15381699};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.92 uM for nicotinamide {ECO:0000269|PubMed:12555668,
CC ECO:0000269|PubMed:15381699};
CC Vmax=0.021 umol/min/mg enzyme {ECO:0000269|PubMed:12555668,
CC ECO:0000269|PubMed:15381699};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-
CC ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and
CC nicotinamide: step 1/1.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16783373,
CC ECO:0000269|PubMed:16783377}.
CC -!- INTERACTION:
CC Q99KQ4; Q99KQ4: Nampt; NbExp=4; IntAct=EBI-8316571, EBI-8316571;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P43490}. Cytoplasm
CC {ECO:0000269|PubMed:12555668}. Secreted {ECO:0000250|UniProtKB:P43490}.
CC Note=Under non-inflammatory conditions, visfatin predominantly exhibits
CC a granular pattern within the nucleus. Secreted by endothelial cells
CC upon IL-1beta stimulation. Abundantly secreted in milk, reaching 100-
CC fold higher concentrations compared to maternal serum.
CC {ECO:0000250|UniProtKB:P43490}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in lymphoid and non-lymphoid
CC tissues. {ECO:0000269|PubMed:12555668}.
CC -!- INDUCTION: Expression shows a diurnal pattern of oscillation across the
CC 24-hour light-dark cycle in liver, with a reduction in levels before
CC the onset of the dark period (at protein level). Expression shows a
CC diurnal pattern of oscillation in white adipose tissue (WAT), peaking
CC at the beginning of the dark period. Up-regulated during polyclonal
CC immune responses. {ECO:0000269|PubMed:12555668,
CC ECO:0000269|PubMed:19299583}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
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DR EMBL; AY679720; AAT72933.1; -; mRNA.
DR EMBL; AF234625; AAF43208.1; -; mRNA.
DR EMBL; BC004059; AAH04059.1; -; mRNA.
DR EMBL; BC018358; AAH18358.1; -; mRNA.
DR EMBL; AK086415; BAC39664.1; -; mRNA.
DR CCDS; CCDS25871.1; -.
DR RefSeq; NP_067499.2; NM_021524.2.
DR PDB; 2GVL; X-ray; 2.10 A; A/B=1-491.
DR PDB; 2H3B; X-ray; 1.95 A; A/B=1-491.
DR PDB; 2H3D; X-ray; 2.10 A; A/B=1-491.
DR PDB; 7Q8T; X-ray; 2.15 A; A/B=1-491.
DR PDBsum; 2GVL; -.
DR PDBsum; 2H3B; -.
DR PDBsum; 2H3D; -.
DR PDBsum; 7Q8T; -.
DR AlphaFoldDB; Q99KQ4; -.
DR SMR; Q99KQ4; -.
DR BioGRID; 208494; 21.
DR DIP; DIP-29217N; -.
DR IntAct; Q99KQ4; 1.
DR STRING; 10090.ENSMUSP00000020886; -.
DR BindingDB; Q99KQ4; -.
DR ChEMBL; CHEMBL3259474; -.
DR iPTMnet; Q99KQ4; -.
DR PhosphoSitePlus; Q99KQ4; -.
DR SwissPalm; Q99KQ4; -.
DR EPD; Q99KQ4; -.
DR jPOST; Q99KQ4; -.
DR MaxQB; Q99KQ4; -.
DR PaxDb; Q99KQ4; -.
DR PeptideAtlas; Q99KQ4; -.
DR PRIDE; Q99KQ4; -.
DR ProteomicsDB; 293629; -.
DR Antibodypedia; 17123; 991 antibodies from 44 providers.
DR DNASU; 59027; -.
DR Ensembl; ENSMUST00000020886; ENSMUSP00000020886; ENSMUSG00000020572.
DR GeneID; 59027; -.
DR KEGG; mmu:59027; -.
DR UCSC; uc007nif.2; mouse.
DR CTD; 10135; -.
DR MGI; MGI:1929865; Nampt.
DR VEuPathDB; HostDB:ENSMUSG00000020572; -.
DR eggNOG; ENOG502QSGN; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR HOGENOM; CLU_012550_2_0_1; -.
DR InParanoid; Q99KQ4; -.
DR OMA; TFGFAMK; -.
DR OrthoDB; 446086at2759; -.
DR PhylomeDB; Q99KQ4; -.
DR TreeFam; TF333530; -.
DR BRENDA; 2.4.2.12; 3474.
DR Reactome; R-MMU-197264; Nicotinamide salvaging.
DR SABIO-RK; Q99KQ4; -.
DR UniPathway; UPA00253; UER00890.
DR BioGRID-ORCS; 59027; 22 hits in 77 CRISPR screens.
DR ChiTaRS; Nampt; mouse.
DR EvolutionaryTrace; Q99KQ4; -.
DR PRO; PR:Q99KQ4; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q99KQ4; protein.
DR Bgee; ENSMUSG00000020572; Expressed in gastrula and 275 other tissues.
DR ExpressionAtlas; Q99KQ4; baseline and differential.
DR Genevisible; Q99KQ4; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005125; F:cytokine activity; ISO:MGI.
DR GO; GO:1901363; F:heterocyclic compound binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0047280; F:nicotinamide phosphoribosyltransferase activity; IDA:MGI.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; ISO:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0007623; P:circadian rhythm; IEP:UniProtKB.
DR GO; GO:0001774; P:microglial cell activation; ISO:MGI.
DR GO; GO:0009435; P:NAD biosynthetic process; IDA:MGI.
DR GO; GO:0010507; P:negative regulation of autophagy; ISO:MGI.
DR GO; GO:2000773; P:negative regulation of cellular senescence; ISO:MGI.
DR GO; GO:0051770; P:positive regulation of nitric-oxide synthase biosynthetic process; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0014916; P:regulation of lung blood pressure; ISO:MGI.
DR CDD; cd01569; PBEF_like; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041529; DUF5598.
DR InterPro; IPR041525; N/Namide_PRibTrfase.
DR InterPro; IPR016471; Nicotinamide_PRibTrfase.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR43816; PTHR43816; 1.
DR Pfam; PF18127; NAMPT_N; 1.
DR Pfam; PF04095; NAPRTase; 1.
DR PIRSF; PIRSF005943; NMPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Biological rhythms; Cytokine; Cytoplasm;
KW Glycosyltransferase; Nucleus; Phosphoprotein;
KW Pyridine nucleotide biosynthesis; Reference proteome; Secreted;
KW Transferase.
FT CHAIN 1..491
FT /note="Nicotinamide phosphoribosyltransferase"
FT /id="PRO_0000205864"
FT BINDING 196
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 219
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 247
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 311..313
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 311
FT /ligand="diphosphate"
FT /ligand_id="ChEBI:CHEBI:33019"
FT /evidence="ECO:0000250"
FT BINDING 353..354
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 384
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT BINDING 392
FT /ligand="beta-nicotinamide D-ribonucleotide"
FT /ligand_id="ChEBI:CHEBI:14649"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
FT MOD_RES 188
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P43490"
FT CONFLICT 170
FT /note="K -> R (in Ref. 3; AAF43208)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="F -> S (in Ref. 3; AAF43208)"
FT /evidence="ECO:0000305"
FT CONFLICT 215
FT /note="F -> L (in Ref. 3; AAF43208)"
FT /evidence="ECO:0000305"
FT HELIX 11..13
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2H3D"
FT HELIX 17..24
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 62..69
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 77..91
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 98..108
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 139..143
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 149..153
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 156..180
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 189..192
FT /evidence="ECO:0007829|PDB:2H3B"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:2H3B"
FT TURN 212..214
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:2H3D"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 247..251
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 283..288
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 296..299
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 317..331
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 358..370
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 378..383
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 384..387
FT /evidence="ECO:0007829|PDB:2H3B"
FT TURN 392..396
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 397..406
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 409..412
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 440..443
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 447..450
FT /evidence="ECO:0007829|PDB:2H3B"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:2GVL"
FT STRAND 459..463
FT /evidence="ECO:0007829|PDB:2H3B"
FT HELIX 473..479
FT /evidence="ECO:0007829|PDB:2H3B"
SQ SEQUENCE 491 AA; 55447 MW; D3E522A1841297E6 CRC64;
MNAAAEAEFN ILLATDSYKV THYKQYPPNT SKVYSYFECR EKKTENSKVR KVKYEETVFY
GLQYILNKYL KGKVVTKEKI QEAKEVYREH FQDDVFNERG WNYILEKYDG HLPIEVKAVP
EGSVIPRGNV LFTVENTDPE CYWLTNWIET ILVQSWYPIT VATNSREQKK ILAKYLLETS
GNLDGLEYKL HDFGYRGVSS QETAGIGASA HLVNFKGTDT VAGIALIKKY YGTKDPVPGY
SVPAAEHSTI TAWGKDHEKD AFEHIVTQFS SVPVSVVSDS YDIYNACEKI WGEDLRHLIV
SRSTEAPLII RPDSGNPLDT VLKVLDILGK KFPVTENSKG YKLLPPYLRV IQGDGVDINT
LQEIVEGMKQ KKWSIENVSF GSGGALLQKL TRDLLNCSFK CSYVVTNGLG VNVFKDPVAD
PNKRSKKGRL SLHRTPAGNF VTLEEGKGDL EEYGHDLLHT VFKNGKVTKS YSFDEVRKNA
QLNIEQDVAP H
