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   27-MAR-2024, entry version 176.
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,
RC   Pancreas, 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-BMAL1 heterodimer from
CC       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; 23.
DR   DIP; DIP-29217N; -.
DR   IntAct; Q99KQ4; 1.
DR   STRING; 10090.ENSMUSP00000020886; -.
DR   BindingDB; Q99KQ4; -.
DR   ChEMBL; CHEMBL3259474; -.
DR   GlyGen; Q99KQ4; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q99KQ4; -.
DR   PhosphoSitePlus; Q99KQ4; -.
DR   SwissPalm; Q99KQ4; -.
DR   EPD; Q99KQ4; -.
DR   jPOST; Q99KQ4; -.
DR   MaxQB; Q99KQ4; -.
DR   PaxDb; 10090-ENSMUSP00000020886; -.
DR   PeptideAtlas; Q99KQ4; -.
DR   ProteomicsDB; 293629; -.
DR   Pumba; Q99KQ4; -.
DR   Antibodypedia; 17123; 1123 antibodies from 44 providers.
DR   DNASU; 59027; -.
DR   Ensembl; ENSMUST00000020886.9; ENSMUSP00000020886.8; ENSMUSG00000020572.9.
DR   GeneID; 59027; -.
DR   KEGG; mmu:59027; -.
DR   UCSC; uc007nif.2; mouse.
DR   AGR; MGI:1929865; -.
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; 312306at2759; -.
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 82 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 279 other cell types or tissues.
DR   ExpressionAtlas; Q99KQ4; baseline and differential.
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: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: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; Aldolase class I; 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; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR43816:SF1; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF18127; NAMPT_N; 1.
DR   Pfam; PF04095; NAPRTase; 1.
DR   PIRSF; PIRSF005943; NMPRT; 1.
DR   SUPFAM; SSF51690; Nicotinate/Quinolinate PRTase C-terminal domain-like; 1.
DR   Genevisible; Q99KQ4; MM.
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
//