PNCB_HUMAN
ID PNCB_HUMAN Reviewed; 538 AA.
AC Q6XQN6; A7BFI3; Q6PJL1; Q6XQN4; Q6XQN5; Q8N5E8; Q9BRG0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Nicotinate phosphoribosyltransferase;
DE Short=NAPRTase;
DE EC=6.3.4.21 {ECO:0000269|PubMed:17604275, ECO:0000269|PubMed:21742010, ECO:0000269|PubMed:26042198};
DE AltName: Full=FHA-HIT-interacting protein;
DE AltName: Full=Nicotinate phosphoribosyltransferase domain-containing protein 1;
GN Name=NAPRT; Synonyms=FHIP, NAPRT1;
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), FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, AND PATHWAY.
RX PubMed=17604275; DOI=10.1074/jbc.m610357200;
RA Hara N., Yamada K., Shibata T., Osago H., Hashimoto T., Tsuchiya M.;
RT "Elevation of cellular NAD levels by nicotinic acid and involvement of
RT nicotinic acid phosphoribosyltransferase in human cells.";
RL J. Biol. Chem. 282:24574-24582(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
RA Huang C.-H., Chen H., Chen Y.;
RT "Identification of nicotinate phosphoribosyltransferase as a novel FHA-HIT
RT interaction protein (FHIP).";
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, AND IDENTIFICATION BY
RP 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 CATALYTIC ACTIVITY, FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, 3D-STRUCTURE MODELING, PATHWAY, AND MUTAGENESIS OF ASP-19; TYR-21;
RP GLY-169; GLY-209; HIS-213; ASP-288; ARG-318; ASN-357; GLY-379; THR-380 AND
RP SER-381.
RX PubMed=21742010; DOI=10.1016/j.biochi.2011.06.033;
RA Galassi L., Di Stefano M., Brunetti L., Orsomando G., Amici A.,
RA Ruggieri S., Magni G.;
RT "Characterization of human nicotinate phosphoribosyltransferase: Kinetic
RT studies, structure prediction and functional analysis by site-directed
RT mutagenesis.";
RL Biochimie 94:300-309(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-537, 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] {ECO:0007744|PDB:4YUB}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP PATHWAY, AND SUBUNIT.
RX PubMed=26042198; DOI=10.1016/j.fob.2015.05.002;
RA Marletta A.S., Massarotti A., Orsomando G., Magni G., Rizzi M.,
RA Garavaglia S.;
RT "Crystal structure of human nicotinic acid phosphoribosyltransferase.";
RL FEBS Open Bio 5:419-428(2015).
CC -!- FUNCTION: Catalyzes the first step in the biosynthesis of NAD from
CC nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-
CC ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate
CC (PubMed:17604275, PubMed:21742010, PubMed:26042198). Helps prevent
CC cellular oxidative stress via its role in NAD biosynthesis
CC (PubMed:17604275). {ECO:0000269|PubMed:17604275,
CC ECO:0000269|PubMed:21742010, ECO:0000269|PubMed:26042198}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O +
CC nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide +
CC phosphate; Xref=Rhea:RHEA:36163, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32544, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57502, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:456216; EC=6.3.4.21;
CC Evidence={ECO:0000269|PubMed:17604275, ECO:0000269|PubMed:21742010,
CC ECO:0000269|PubMed:26042198};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21742010};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:21742010};
CC Note=Activity is highest with Mn(2+). {ECO:0000269|PubMed:21742010};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44.3 uM for nicotinic acid (in the presence of 3 mM ATP)
CC {ECO:0000269|PubMed:21742010};
CC KM=22.1 uM for 5-phosphoribosyl-1-pyrophosphate (in the presence of 3
CC mM ATP) {ECO:0000269|PubMed:21742010};
CC KM=27.3 uM for nicotinic acid (in the presence of inorganic
CC phosphate) {ECO:0000269|PubMed:21742010};
CC KM=38.2 uM for 5-phosphoribosyl-1-pyrophosphate (in the presence of
CC inorganic phosphate) {ECO:0000269|PubMed:21742010};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-
CC ribonucleotide from nicotinate: step 1/1. {ECO:0000269|PubMed:17604275,
CC ECO:0000269|PubMed:21742010, ECO:0000269|PubMed:26042198}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:26042198,
CC ECO:0000305|PubMed:21742010}.
CC -!- INTERACTION:
CC Q6XQN6; Q96HH9: GRAMD2B; NbExp=3; IntAct=EBI-10254872, EBI-2832937;
CC Q6XQN6; Q93062: RBPMS; NbExp=3; IntAct=EBI-10254872, EBI-740322;
CC Q6XQN6-2; Q2TAC2: CCDC57; NbExp=3; IntAct=EBI-10254820, EBI-2808286;
CC Q6XQN6-2; A2ABF9: EHMT2; NbExp=3; IntAct=EBI-10254820, EBI-10174566;
CC Q6XQN6-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-10254820, EBI-10171697;
CC Q6XQN6-2; Q93062: RBPMS; NbExp=3; IntAct=EBI-10254820, EBI-740322;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17604275}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6XQN6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6XQN6-2; Sequence=VSP_030612;
CC Name=3;
CC IsoId=Q6XQN6-3; Sequence=VSP_030610;
CC -!- PTM: Transiently phosphorylated on a His residue during the reaction
CC cycle. Phosphorylation strongly increases the affinity for substrates
CC and increases the rate of nicotinate D-ribonucleotide production.
CC Dephosphorylation regenerates the low-affinity form of the enzyme,
CC leading to product release. {ECO:0000250|UniProtKB:P22253}.
CC -!- SIMILARITY: Belongs to the NAPRTase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH06284.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH32466.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB242230; BAF75377.1; -; mRNA.
DR EMBL; AY214325; AAP69603.1; -; mRNA.
DR EMBL; AY214326; AAP69604.1; -; mRNA.
DR EMBL; AY214327; AAP69605.1; -; mRNA.
DR EMBL; BC006284; AAH06284.2; ALT_INIT; mRNA.
DR EMBL; BC032466; AAH32466.1; ALT_INIT; mRNA.
DR CCDS; CCDS6403.2; -. [Q6XQN6-1]
DR CCDS; CCDS69555.1; -. [Q6XQN6-3]
DR RefSeq; NP_001273758.1; NM_001286829.1. [Q6XQN6-3]
DR RefSeq; NP_660202.3; NM_145201.5. [Q6XQN6-1]
DR RefSeq; XP_016869469.1; XM_017013980.1.
DR PDB; 4YUB; X-ray; 2.90 A; A/B=1-538.
DR PDBsum; 4YUB; -.
DR AlphaFoldDB; Q6XQN6; -.
DR SMR; Q6XQN6; -.
DR BioGRID; 125001; 43.
DR IntAct; Q6XQN6; 9.
DR STRING; 9606.ENSP00000401508; -.
DR ChEMBL; CHEMBL4523354; -.
DR iPTMnet; Q6XQN6; -.
DR PhosphoSitePlus; Q6XQN6; -.
DR BioMuta; NAPRT; -.
DR DMDM; 166221824; -.
DR EPD; Q6XQN6; -.
DR jPOST; Q6XQN6; -.
DR MassIVE; Q6XQN6; -.
DR MaxQB; Q6XQN6; -.
DR PaxDb; Q6XQN6; -.
DR PeptideAtlas; Q6XQN6; -.
DR PRIDE; Q6XQN6; -.
DR ProteomicsDB; 67810; -. [Q6XQN6-1]
DR ProteomicsDB; 67811; -. [Q6XQN6-2]
DR ProteomicsDB; 67812; -. [Q6XQN6-3]
DR Antibodypedia; 14617; 195 antibodies from 27 providers.
DR DNASU; 93100; -.
DR Ensembl; ENST00000426292.7; ENSP00000390949.3; ENSG00000147813.16. [Q6XQN6-3]
DR Ensembl; ENST00000449291.7; ENSP00000401508.2; ENSG00000147813.16. [Q6XQN6-1]
DR Ensembl; ENST00000621955.1; ENSP00000480017.1; ENSG00000278488.2. [Q6XQN6-1]
DR Ensembl; ENST00000632139.1; ENSP00000488794.1; ENSG00000278488.2. [Q6XQN6-3]
DR GeneID; 93100; -.
DR KEGG; hsa:93100; -.
DR MANE-Select; ENST00000449291.7; ENSP00000401508.2; NM_145201.6; NP_660202.3.
DR UCSC; uc003yym.6; human. [Q6XQN6-1]
DR CTD; 93100; -.
DR DisGeNET; 93100; -.
DR GeneCards; NAPRT; -.
DR HGNC; HGNC:30450; NAPRT.
DR HPA; ENSG00000147813; Tissue enhanced (intestine, liver).
DR MIM; 611552; gene.
DR neXtProt; NX_Q6XQN6; -.
DR OpenTargets; ENSG00000147813; -.
DR PharmGKB; PA142671293; -.
DR VEuPathDB; HostDB:ENSG00000147813; -.
DR eggNOG; KOG2511; Eukaryota.
DR GeneTree; ENSGT00940000153456; -.
DR InParanoid; Q6XQN6; -.
DR OMA; VYFPGSP; -.
DR OrthoDB; 577034at2759; -.
DR PhylomeDB; Q6XQN6; -.
DR TreeFam; TF314732; -.
DR BRENDA; 6.3.4.21; 2681.
DR PathwayCommons; Q6XQN6; -.
DR Reactome; R-HSA-197264; Nicotinamide salvaging.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SABIO-RK; Q6XQN6; -.
DR SignaLink; Q6XQN6; -.
DR UniPathway; UPA00253; UER00457.
DR BioGRID-ORCS; 93100; 14 hits in 1079 CRISPR screens.
DR ChiTaRS; NAPRT; human.
DR GenomeRNAi; 93100; -.
DR Pharos; Q6XQN6; Tchem.
DR PRO; PR:Q6XQN6; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q6XQN6; protein.
DR Bgee; ENSG00000147813; Expressed in mucosa of transverse colon and 92 other tissues.
DR ExpressionAtlas; Q6XQN6; baseline and differential.
DR Genevisible; Q6XQN6; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004516; F:nicotinate phosphoribosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IEA:InterPro.
DR GO; GO:0034355; P:NAD salvage; IBA:GO_Central.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR041619; NAPRTase_C.
DR InterPro; IPR040727; NAPRTase_N.
DR InterPro; IPR007229; Nic_PRibTrfase-Fam.
DR InterPro; IPR006405; Nic_PRibTrfase_pncB.
DR InterPro; IPR036068; Nicotinate_pribotase-like_C.
DR PANTHER; PTHR11098; PTHR11098; 1.
DR Pfam; PF17956; NAPRTase_C; 1.
DR Pfam; PF17767; NAPRTase_N; 1.
DR PIRSF; PIRSF000484; NAPRT; 1.
DR SUPFAM; SSF51690; SSF51690; 1.
DR TIGRFAMs; TIGR01513; NAPRTase_put; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Ligase; Magnesium;
KW Manganese; Metal-binding; Phosphoprotein; Pyridine nucleotide biosynthesis;
KW Reference proteome; Transferase.
FT CHAIN 1..538
FT /note="Nicotinate phosphoribosyltransferase"
FT /id="PRO_0000315681"
FT BINDING 21
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 210
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 318
FT /ligand="nicotinate"
FT /ligand_id="ChEBI:CHEBI:32544"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT BINDING 380
FT /ligand="5-phospho-alpha-D-ribose 1-diphosphate"
FT /ligand_id="ChEBI:CHEBI:58017"
FT /evidence="ECO:0000250|UniProtKB:Q9HJ28"
FT MOD_RES 213
FT /note="Phosphohistidine"
FT /evidence="ECO:0000250|UniProtKB:P22253"
FT MOD_RES 537
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 469..481
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_030610"
FT VAR_SEQ 517
FT /note="Y -> YQVGGGGPPCHSALCAPALTLPTAPVLCSL (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_030612"
FT VARIANT 57
FT /note="A -> V (in dbSNP:rs896950)"
FT /id="VAR_038275"
FT MUTAGEN 19
FT /note="D->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 21
FT /note="Y->A: Partial loss of activity in the presence of
FT ATP, complete loss in the absence of ATP."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 169
FT /note="G->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 209
FT /note="G->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 213
FT /note="H->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 288
FT /note="D->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 318
FT /note="R->A: Partial loss of activity in the presence of
FT ATP, almost complete loss in the absence of ATP."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 357
FT /note="N->A: Small loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 379
FT /note="G->A: Complete loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 380
FT /note="T->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT MUTAGEN 381
FT /note="S->A: Partial loss of activity."
FT /evidence="ECO:0000269|PubMed:21742010"
FT CONFLICT 155
FT /note="L -> V (in Ref. 2; AAP69603/AAP69604/AAP69605)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="V -> A (in Ref. 1; BAF75377)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="A -> T (in Ref. 1; BAF75377)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="V -> A (in Ref. 1; BAF75377)"
FT /evidence="ECO:0000305"
FT HELIX 20..31
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 35..44
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 49..51
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 60..66
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 74..79
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 121..127
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 135..159
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 178..189
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 197..203
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 213..216
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 242..257
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 266..278
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 280..282
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 283..286
FT /evidence="ECO:0007829|PDB:4YUB"
FT TURN 292..295
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 296..306
FT /evidence="ECO:0007829|PDB:4YUB"
FT TURN 307..310
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 324..342
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 345..348
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 351..354
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 360..366
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 421..427
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 451..454
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 468..472
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 475..479
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 490..503
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 506..509
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:4YUB"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:4YUB"
FT HELIX 523..529
FT /evidence="ECO:0007829|PDB:4YUB"
SQ SEQUENCE 538 AA; 57578 MW; 26DF39885CBB1C9B CRC64;
MAAEQDPEAR AAARPLLTDL YQATMALGYW RAGRARDAAE FELFFRRCPF GGAFALAAGL
RDCVRFLRAF RLRDADVQFL ASVLPPDTDP AFFEHLRALD CSEVTVRALP EGSLAFPGVP
LLQVSGPLLV VQLLETPLLC LVSYASLVAT NAARLRLIAG PEKRLLEMGL RRAQGPDGGL
TASTYSYLGG FDSSSNVLAG QLRGVPVAGT LAHSFVTSFS GSEVPPDPML APAAGEGPGV
DLAAKAQVWL EQVCAHLGLG VQEPHPGERA AFVAYALAFP RAFQGLLDTY SVWRSGLPNF
LAVALALGEL GYRAVGVRLD SGDLLQQAQE IRKVFRAAAA QFQVPWLESV LIVVSNNIDE
EALARLAQEG SEVNVIGIGT SVVTCPQQPS LGGVYKLVAV GGQPRMKLTE DPEKQTLPGS
KAAFRLLGSD GSPLMDMLQL AEEPVPQAGQ ELRVWPPGAQ EPCTVRPAQV EPLLRLCLQQ
GQLCEPLPSL AESRALAQLS LSRLSPEHRR LRSPAQYQVV LSERLQALVN SLCAGQSP
