NADE_HUMAN
ID NADE_HUMAN Reviewed; 706 AA.
AC Q6IA69; B3KUU4; Q86SN2; Q9HA25; Q9NVM8;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-SEP-2009, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Glutamine-dependent NAD(+) synthetase;
DE EC=6.3.5.1 {ECO:0000269|PubMed:12547821, ECO:0000269|PubMed:31883644};
DE AltName: Full=NAD(+) synthase [glutamine-hydrolyzing];
DE AltName: Full=NAD(+) synthetase;
GN Name=NADSYN1;
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 SUBUNIT, MUTAGENESIS OF CYS-175, BIOPHYSICOCHEMICAL PROPERTIES, AND VARIANT
RP HIS-204.
RC TISSUE=Brain;
RX PubMed=12547821; DOI=10.1074/jbc.m209203200;
RA Hara N., Yamada K., Terashima M., Osago H., Shimoyama M., Tsuchiya M.;
RT "Molecular identification of human glutamine- and ammonia-dependent NAD
RT synthetases. Carbon-nitrogen hydrolase domain confers glutamine
RT dependency.";
RL J. Biol. Chem. 278:10914-10921(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANTS
RP LEU-74 AND HIS-204.
RC TISSUE=Mammary gland, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS LEU-74 AND
RP HIS-204.
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 VARIANTS LEU-74 AND
RP HIS-204.
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 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 [8]
RP INVOLVEMENT IN VCRL3, VARIANTS VCRL3 ARG-49; LEU-132; 245-CYS--ASP-706 DEL;
RP THR-573 AND 613-TYR--ASP-706 DEL, CHARACTERIZATION OF VARIANTS VCRL3
RP ARG-49; LEU-132 AND THR-573, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=31883644; DOI=10.1016/j.ajhg.2019.12.006;
RA Szot J.O., Campagnolo C., Cao Y., Iyer K.R., Cuny H., Drysdale T.,
RA Flores-Daboub J.A., Bi W., Westerfield L., Liu P., Leung T.N., Choy K.W.,
RA Chapman G., Xiao R., Siu V.M., Dunwoodie S.L.;
RT "Bi-allelic mutations in NADSYN1 cause multiple organ defects and expand
RT the genotypic spectrum of congenital NAD deficiency disorders.";
RL Am. J. Hum. Genet. 106:129-136(2020).
CC -!- FUNCTION: Catalyzes the final step of the nicotinamide adenine
CC dinucleotide (NAD) de novo synthesis pathway, the ATP-dependent
CC amidation of deamido-NAD using L-glutamine as a nitrogen source.
CC {ECO:0000269|PubMed:12547821, ECO:0000269|PubMed:31883644}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate +
CC H(+) + L-glutamate + NAD(+); Xref=Rhea:RHEA:24384, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57540, ChEBI:CHEBI:58359,
CC ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.5.1;
CC Evidence={ECO:0000269|PubMed:12547821};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24385;
CC Evidence={ECO:0000305|PubMed:12547821, ECO:0000305|PubMed:31883644};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.49 mM for deamido-NAD(+) {ECO:0000269|PubMed:12547821};
CC KM=0.089 mM for ATP {ECO:0000269|PubMed:12547821};
CC KM=1.44 mM for glutamine {ECO:0000269|PubMed:12547821};
CC KM=13.1 mM for ammonium {ECO:0000269|PubMed:12547821};
CC Vmax=0.99 nmol/min/ug enzyme deamido-NAD(+)
CC {ECO:0000269|PubMed:12547821};
CC Vmax=0.61 nmol/min/ug enzyme ATP {ECO:0000269|PubMed:12547821};
CC Vmax=0.70 nmol/min/ug enzyme glutamine {ECO:0000269|PubMed:12547821};
CC Vmax=1.04 nmol/min/ug enzyme ammonium {ECO:0000269|PubMed:12547821};
CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC deamido-NAD(+) (L-Gln route): step 1/1. {ECO:0000305|PubMed:12547821}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12547821}.
CC -!- INTERACTION:
CC Q6IA69; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-748610, EBI-11954519;
CC Q6IA69; P27658: COL8A1; NbExp=3; IntAct=EBI-748610, EBI-747133;
CC Q6IA69; Q02930-3: CREB5; NbExp=3; IntAct=EBI-748610, EBI-10192698;
CC Q6IA69; Q9NTM9: CUTC; NbExp=4; IntAct=EBI-748610, EBI-714918;
CC Q6IA69; O43559: FRS3; NbExp=3; IntAct=EBI-748610, EBI-725515;
CC Q6IA69; O95872: GPANK1; NbExp=3; IntAct=EBI-748610, EBI-751540;
CC Q6IA69; A0A024R8L2: hCG_1987119; NbExp=6; IntAct=EBI-748610, EBI-14103818;
CC Q6IA69; O14964: HGS; NbExp=3; IntAct=EBI-748610, EBI-740220;
CC Q6IA69; P31273: HOXC8; NbExp=3; IntAct=EBI-748610, EBI-1752118;
CC Q6IA69; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-748610, EBI-12025760;
CC Q6IA69; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-748610, EBI-741158;
CC Q6IA69; Q92734: TFG; NbExp=3; IntAct=EBI-748610, EBI-357061;
CC Q6IA69; Q9H614; NbExp=3; IntAct=EBI-748610, EBI-10249899;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6IA69-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IA69-2; Sequence=VSP_056585, VSP_056586;
CC -!- DISEASE: Vertebral, cardiac, renal, and limb defects syndrome 3 (VCRL3)
CC [MIM:618845]: An autosomal recessive, lethal disorder characterized by
CC severe cardiac and renal anomalies, including hypoplastic or absent
CC left ventricle, transposition of the great arteries, absent pulmonary
CC trunk, and hypoplastic or absent kidneys. Patients also exhibit
CC vertebral segmentation defects and shortening of the proximal long
CC bones or micromelia. Death occurs in early infancy.
CC {ECO:0000269|PubMed:31883644}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD synthetase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AB091316; BAC65148.1; -; mRNA.
DR EMBL; AK001493; BAA91722.1; -; mRNA.
DR EMBL; AK022436; BAB14034.1; -; mRNA.
DR EMBL; AK097946; BAG53556.1; -; mRNA.
DR EMBL; CR457286; CAG33567.1; -; mRNA.
DR EMBL; AP000867; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP002387; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471076; EAW74792.1; -; Genomic_DNA.
DR EMBL; BC003638; AAH03638.1; -; mRNA.
DR EMBL; BC003666; AAH03666.1; -; mRNA.
DR CCDS; CCDS8201.1; -. [Q6IA69-1]
DR RefSeq; NP_060631.2; NM_018161.4. [Q6IA69-1]
DR PDB; 6OFB; X-ray; 2.84 A; A/B=1-706.
DR PDBsum; 6OFB; -.
DR AlphaFoldDB; Q6IA69; -.
DR SMR; Q6IA69; -.
DR BioGRID; 120488; 32.
DR IntAct; Q6IA69; 18.
DR STRING; 9606.ENSP00000326424; -.
DR BindingDB; Q6IA69; -.
DR DrugBank; DB00142; Glutamic acid.
DR DrugBank; DB00130; L-Glutamine.
DR iPTMnet; Q6IA69; -.
DR MetOSite; Q6IA69; -.
DR PhosphoSitePlus; Q6IA69; -.
DR BioMuta; NADSYN1; -.
DR DMDM; 257051045; -.
DR EPD; Q6IA69; -.
DR jPOST; Q6IA69; -.
DR MassIVE; Q6IA69; -.
DR MaxQB; Q6IA69; -.
DR PaxDb; Q6IA69; -.
DR PeptideAtlas; Q6IA69; -.
DR PRIDE; Q6IA69; -.
DR ProteomicsDB; 3734; -.
DR ProteomicsDB; 66358; -. [Q6IA69-1]
DR Antibodypedia; 30728; 73 antibodies from 18 providers.
DR DNASU; 55191; -.
DR Ensembl; ENST00000319023.7; ENSP00000326424.2; ENSG00000172890.13. [Q6IA69-1]
DR GeneID; 55191; -.
DR KEGG; hsa:55191; -.
DR MANE-Select; ENST00000319023.7; ENSP00000326424.2; NM_018161.5; NP_060631.2.
DR UCSC; uc001oqn.4; human. [Q6IA69-1]
DR CTD; 55191; -.
DR DisGeNET; 55191; -.
DR GeneCards; NADSYN1; -.
DR HGNC; HGNC:29832; NADSYN1.
DR HPA; ENSG00000172890; Low tissue specificity.
DR MalaCards; NADSYN1; -.
DR MIM; 608285; gene.
DR MIM; 618845; phenotype.
DR neXtProt; NX_Q6IA69; -.
DR OpenTargets; ENSG00000172890; -.
DR Orphanet; 521438; Congenital vertebral-cardiac-renal anomalies syndrome.
DR PharmGKB; PA142671299; -.
DR VEuPathDB; HostDB:ENSG00000172890; -.
DR eggNOG; KOG2303; Eukaryota.
DR GeneTree; ENSGT00390000010152; -.
DR HOGENOM; CLU_011884_2_0_1; -.
DR InParanoid; Q6IA69; -.
DR OMA; CEDHFYE; -.
DR OrthoDB; 283044at2759; -.
DR PhylomeDB; Q6IA69; -.
DR TreeFam; TF351426; -.
DR BioCyc; MetaCyc:HS10587-MON; -.
DR BRENDA; 6.3.5.1; 2681.
DR PathwayCommons; Q6IA69; -.
DR Reactome; R-HSA-196807; Nicotinate metabolism.
DR SignaLink; Q6IA69; -.
DR UniPathway; UPA00253; UER00334.
DR BioGRID-ORCS; 55191; 6 hits in 1080 CRISPR screens.
DR ChiTaRS; NADSYN1; human.
DR GeneWiki; NADSYN1; -.
DR GenomeRNAi; 55191; -.
DR Pharos; Q6IA69; Tbio.
DR PRO; PR:Q6IA69; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q6IA69; protein.
DR Bgee; ENSG00000172890; Expressed in right uterine tube and 172 other tissues.
DR ExpressionAtlas; Q6IA69; baseline and differential.
DR Genevisible; Q6IA69; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004359; F:glutaminase activity; IBA:GO_Central.
DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IMP:UniProtKB.
DR GO; GO:0034627; P:'de novo' NAD biosynthetic process; IMP:UniProtKB.
DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR CDD; cd00553; NAD_synthase; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR Gene3D; 3.60.110.10; -; 1.
DR HAMAP; MF_02090; NadE_glutamine_dep; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR014445; Gln-dep_NAD_synthase.
DR InterPro; IPR022310; NAD/GMP_synthase.
DR InterPro; IPR003694; NAD_synthase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR23090; PTHR23090; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR Pfam; PF02540; NAD_synthase; 1.
DR PIRSF; PIRSF006630; NADS_GAT; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR00552; nadE; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Disease variant; Ligase;
KW NAD; Nucleotide-binding; Reference proteome.
FT CHAIN 1..706
FT /note="Glutamine-dependent NAD(+) synthetase"
FT /id="PRO_0000237577"
FT DOMAIN 5..275
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT REGION 325..706
FT /note="Ligase"
FT /evidence="ECO:0000250"
FT ACT_SITE 45
FT /note="Proton acceptor; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 114
FT /note="For glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 175
FT /note="Nucleophile; for glutaminase activity"
FT /evidence="ECO:0000250|UniProtKB:P9WJJ3"
FT ACT_SITE 357
FT /evidence="ECO:0000250"
FT BINDING 355..362
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..6
FT /note="MGRKVT -> MGISGQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056585"
FT VAR_SEQ 7..266
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056586"
FT VARIANT 49
FT /note="C -> R (in VCRL3; loss of protein expression)"
FT /evidence="ECO:0000269|PubMed:31883644"
FT /id="VAR_084040"
FT VARIANT 74
FT /note="V -> L (in dbSNP:rs2276360)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|Ref.3"
FT /id="VAR_026497"
FT VARIANT 132
FT /note="W -> L (in VCRL3; decreased protein expression;
FT decreased NAD(+) synthase (glutamine-hydrolyzing) activity;
FT dbSNP:rs189928649)"
FT /evidence="ECO:0000269|PubMed:31883644"
FT /id="VAR_084041"
FT VARIANT 204
FT /note="Q -> H (in dbSNP:rs7950441)"
FT /evidence="ECO:0000269|PubMed:12547821,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.3"
FT /id="VAR_058703"
FT VARIANT 245..706
FT /note="Missing (in VCRL3)"
FT /evidence="ECO:0000269|PubMed:31883644"
FT /id="VAR_084042"
FT VARIANT 297
FT /note="P -> L (in dbSNP:rs7121106)"
FT /id="VAR_056204"
FT VARIANT 573
FT /note="A -> T (in VCRL3; no effect on protein expression;
FT decreased NAD(+) synthase (glutamine-hydrolyzing) activity;
FT dbSNP:rs144139747)"
FT /evidence="ECO:0000269|PubMed:31883644"
FT /id="VAR_084043"
FT VARIANT 591
FT /note="M -> I (in dbSNP:rs35007971)"
FT /id="VAR_056205"
FT VARIANT 613..706
FT /note="Missing (in VCRL3)"
FT /evidence="ECO:0000269|PubMed:31883644"
FT /id="VAR_084044"
FT VARIANT 704
FT /note="G -> S (in dbSNP:rs12282060)"
FT /id="VAR_056206"
FT MUTAGEN 175
FT /note="C->S: Eliminates glutamine-dependent NAD synthetase
FT activity with the ammonia-dependent activity intact."
FT /evidence="ECO:0000269|PubMed:12547821"
FT CONFLICT 102
FT /note="I -> V (in Ref. 1; BAC65148)"
FT /evidence="ECO:0000305"
FT CONFLICT 207
FT /note="R -> H (in Ref. 3; CAG33567)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="W -> R (in Ref. 1; BAC65148)"
FT /evidence="ECO:0000305"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:6OFB"
FT TURN 45..49
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 54..58
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 60..74
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 82..92
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 95..106
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 154..160
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 175..179
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 184..191
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 209..223
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 225..234
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 236..239
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 265..274
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 328..347
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 360..381
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 405..412
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 425..438
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 448..462
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 475..503
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 510..513
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 518..523
FT /evidence="ECO:0007829|PDB:6OFB"
FT STRAND 535..539
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 544..558
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 563..568
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 587..591
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 595..606
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 612..622
FT /evidence="ECO:0007829|PDB:6OFB"
FT TURN 623..626
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 629..646
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 648..651
FT /evidence="ECO:0007829|PDB:6OFB"
FT TURN 666..669
FT /evidence="ECO:0007829|PDB:6OFB"
FT HELIX 681..694
FT /evidence="ECO:0007829|PDB:6OFB"
SQ SEQUENCE 706 AA; 79285 MW; 9788B060F3A1D13B CRC64;
MGRKVTVATC ALNQWALDFE GNLQRILKSI EIAKNRGARY RLGPELEICG YGCWDHYYES
DTLLHSFQVL AALVESPVTQ DIICDVGMPV MHRNVRYNCR VIFLNRKILL IRPKMALANE
GNYRELRWFT PWSRSRHTEE YFLPRMIQDL TKQETVPFGD AVLVTWDTCI GSEICEELWT
PHSPHIDMGL DGVEIITNAS GSHQVLRKAN TRVDLVTMVT SKNGGIYLLA NQKGCDGDRL
YYDGCAMIAM NGSVFAQGSQ FSLDDVEVLT ATLDLEDVRS YRAEISSRNL AASRASPYPR
VKVDFALSCH EDLLAPISEP IEWKYHSPEE EISLGPACWL WDFLRRSQQA GFLLPLSGGV
DSAATACLIY SMCCQVCEAV RSGNEEVLAD VRTIVNQISY TPQDPRDLCG RILTTCYMAS
KNSSQETCTR ARELAQQIGS HHISLNIDPA VKAVMGIFSL VTGKSPLFAA HGGSSRENLA
LQNVQARIRM VLAYLFAQLS LWSRGVHGGL LVLGSANVDE SLLGYLTKYD CSSADINPIG
GISKTDLRAF VQFCIQRFQL PALQSILLAP ATAELEPLAD GQVSQTDEED MGMTYAELSV
YGKLRKVAKM GPYSMFCKLL GMWRHICTPR QVADKVKRFF SKYSMNRHKM TTLTPAYHAE
NYSPEDNRFD LRPFLYNTSW PWQFRCIENQ VLQLERAEPQ SLDGVD
