ID SIAS_HUMAN Reviewed; 359 AA. AC Q9NR45; B2RE98; Q8WUV9; Q9BWS6; Q9NVD4; DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 27-MAR-2024, entry version 198. DE RecName: Full=Sialic acid synthase; DE AltName: Full=N-acetylneuraminate synthase; DE EC=2.5.1.56 {ECO:0000269|PubMed:10749855, ECO:0000269|PubMed:27213289}; DE AltName: Full=N-acetylneuraminate-9-phosphate synthase; DE EC=2.5.1.57 {ECO:0000269|PubMed:10749855}; DE AltName: Full=N-acetylneuraminic acid phosphate synthase; DE AltName: Full=N-acetylneuraminic acid synthase; GN Name=NANS; Synonyms=SAS; 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], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE RP SPECIFICITY. RC TISSUE=Liver; RX PubMed=10749855; DOI=10.1074/jbc.m000217200; RA Lawrence S.M., Huddleston K.A., Pitts L.R., Nguyen N., Lee Y.C., Vann W.F., RA Coleman T.A., Betenbaugh M.J.; RT "Cloning and expression of the human N-acetylneuraminic acid phosphate RT synthase gene with 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid RT biosynthetic ability."; RL J. Biol. Chem. 275:17869-17877(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta; 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 GENOMIC DNA]. RX PubMed=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). RN [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASP-68. RC TISSUE=Lung, and 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 [6] RP PROTEIN SEQUENCE OF 2-11; 132-145; 150-166; 247-264 AND 299-315, CLEAVAGE RP OF INITIATOR METHIONINE, AND IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Ovarian carcinoma; RA Bienvenut W.V.; RL Submitted (JAN-2010) to UniProtKB. RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-79, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [10] RP IDENTIFICATION BY 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 [11] RP INVOLVEMENT IN SEMDG, VARIANTS SEMDG ASN-29; VAL-133; HIS-151; HIS-188; RP LEU-189; CYS-237 AND ILE-327 INS, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=27213289; DOI=10.1038/ng.3578; RA van Karnebeek C.D., Bonafe L., Wen X.Y., Tarailo-Graovac M., Balzano S., RA Royer-Bertrand B., Ashikov A., Garavelli L., Mammi I., Turolla L., RA Breen C., Donnai D., Cormier V., Heron D., Nishimura G., Uchikawa S., RA Campos-Xavier B., Rossi A., Hennet T., Brand-Arzamendi K., Rozmus J., RA Harshman K., Stevenson B.J., Girardi E., Superti-Furga G., Dewan T., RA Collingridge A., Halparin J., Ross C.J., Van Allen M.I., Rossi A., RA Engelke U.F., Kluijtmans L.A., van der Heeft E., Renkema H., de Brouwer A., RA Huijben K., Zijlstra F., Heisse T., Boltje T., Wasserman W.W., Rivolta C., RA Unger S., Lefeber D.J., Wevers R.A., Superti-Furga A.; RT "NANS-mediated synthesis of sialic acid is required for brain and skeletal RT development."; RL Nat. Genet. 48:777-784(2016). RN [12] RP STRUCTURE BY NMR OF 294-359. RX PubMed=16597820; DOI=10.1110/ps.051700406; RA Hamada T., Ito Y., Abe T., Hayashi F., Guentert P., Inoue M., Kigawa T., RA Terada T., Shirouzu M., Yoshida M., Tanaka A., Sugano S., Yokoyama S., RA Hirota H.; RT "Solution structure of the antifreeze-like domain of human sialic acid RT synthase."; RL Protein Sci. 15:1010-1016(2006). CC -!- FUNCTION: Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy- CC D-glycero-D-galacto-nononic acid (KDN) (PubMed:10749855, CC PubMed:27213289). Can also use N-acetylmannosamine 6-phosphate and CC mannose 6-phosphate as substrates to generate phosphorylated forms of CC Neu5Ac and KDN, respectively (PubMed:10749855). CC {ECO:0000269|PubMed:10749855, ECO:0000269|PubMed:27213289}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-acetyl-D-mannosamine + phosphoenolpyruvate = N- CC acetylneuraminate + phosphate; Xref=Rhea:RHEA:19273, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17122, ChEBI:CHEBI:35418, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=2.5.1.56; CC Evidence={ECO:0000269|PubMed:10749855, ECO:0000269|PubMed:27213289}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19274; CC Evidence={ECO:0000269|PubMed:10749855, ECO:0000269|PubMed:27213289}; CC -!- CATALYTIC ACTIVITY: CC Reaction=an N-acyl-D-mannosamine 6-phosphate + H2O + CC phosphoenolpyruvate = an N-acylneuraminate 9-phosphate + phosphate; CC Xref=Rhea:RHEA:13421, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57537, ChEBI:CHEBI:57666, ChEBI:CHEBI:58702; EC=2.5.1.57; CC Evidence={ECO:0000269|PubMed:10749855}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13422; CC Evidence={ECO:0000269|PubMed:10749855}; CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10749855}. CC -!- DISEASE: Spondyloepimetaphyseal dysplasia, Genevieve type (SEMDG) CC [MIM:610442]: An autosomal recessive disorder characterized by global CC developmental delay with infantile onset, intellectual disability, CC skeletal dysplasia, and short stature. Skeletal findings include flat CC vertebral bodies with irregular vertebral plates, irregular and flared CC metaphyses with vertical striations, small and irregular epiphyses, CC premature carpal ossification and small carpal bones. CC {ECO:0000269|PubMed:27213289}. Note=The disease is caused by variants CC affecting the gene represented in this entry. 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; AF257466; AAF75261.1; -; mRNA. DR EMBL; AK001659; BAA91818.1; -; mRNA. DR EMBL; AK316608; BAG38195.1; -; mRNA. DR EMBL; AL137073; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471105; EAW58867.1; -; Genomic_DNA. DR EMBL; BC000008; AAH00008.1; -; mRNA. DR EMBL; BC019315; AAH19315.1; -; mRNA. DR CCDS; CCDS6733.1; -. DR RefSeq; NP_061819.2; NM_018946.3. DR PDB; 1WVO; NMR; -; A=294-359. DR PDBsum; 1WVO; -. DR AlphaFoldDB; Q9NR45; -. DR SMR; Q9NR45; -. DR BioGRID; 119921; 94. DR IntAct; Q9NR45; 25. DR MINT; Q9NR45; -. DR STRING; 9606.ENSP00000210444; -. DR GlyGen; Q9NR45; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9NR45; -. DR MetOSite; Q9NR45; -. DR PhosphoSitePlus; Q9NR45; -. DR SwissPalm; Q9NR45; -. DR BioMuta; NANS; -. DR DMDM; 20978759; -. DR REPRODUCTION-2DPAGE; IPI00147874; -. DR EPD; Q9NR45; -. DR jPOST; Q9NR45; -. DR MassIVE; Q9NR45; -. DR MaxQB; Q9NR45; -. DR PaxDb; 9606-ENSP00000210444; -. DR PeptideAtlas; Q9NR45; -. DR ProteomicsDB; 82270; -. DR Pumba; Q9NR45; -. DR Antibodypedia; 14440; 245 antibodies from 26 providers. DR DNASU; 54187; -. DR Ensembl; ENST00000210444.6; ENSP00000210444.5; ENSG00000095380.11. DR GeneID; 54187; -. DR KEGG; hsa:54187; -. DR MANE-Select; ENST00000210444.6; ENSP00000210444.5; NM_018946.4; NP_061819.2. DR UCSC; uc004ayc.4; human. DR AGR; HGNC:19237; -. DR DisGeNET; 54187; -. DR GeneCards; NANS; -. DR HGNC; HGNC:19237; NANS. DR HPA; ENSG00000095380; Low tissue specificity. DR MalaCards; NANS; -. DR MIM; 605202; gene. DR MIM; 610442; phenotype. DR neXtProt; NX_Q9NR45; -. DR OpenTargets; ENSG00000095380; -. DR Orphanet; 168454; Spondyloepimetaphyseal dysplasia, Genevieve type. DR PharmGKB; PA134978885; -. DR VEuPathDB; HostDB:ENSG00000095380; -. DR eggNOG; ENOG502QR5J; Eukaryota. DR GeneTree; ENSGT00390000011081; -. DR HOGENOM; CLU_040465_1_0_1; -. DR InParanoid; Q9NR45; -. DR OMA; MTYIDYR; -. DR OrthoDB; 3716025at2759; -. DR PhylomeDB; Q9NR45; -. DR TreeFam; TF324826; -. DR BioCyc; MetaCyc:HS01818-MONOMER; -. DR BRENDA; 2.5.1.132; 2681. DR BRENDA; 2.5.1.56; 2681. DR BRENDA; 2.5.1.57; 2681. DR PathwayCommons; Q9NR45; -. DR Reactome; R-HSA-4085001; Sialic acid metabolism. DR SignaLink; Q9NR45; -. DR BioGRID-ORCS; 54187; 32 hits in 1155 CRISPR screens. DR ChiTaRS; NANS; human. DR EvolutionaryTrace; Q9NR45; -. DR GeneWiki; NANS; -. DR GenomeRNAi; 54187; -. DR Pharos; Q9NR45; Tbio. DR PRO; PR:Q9NR45; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q9NR45; Protein. DR Bgee; ENSG00000095380; Expressed in mucosa of sigmoid colon and 202 other cell types or tissues. DR ExpressionAtlas; Q9NR45; baseline and differential. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0050462; F:N-acetylneuraminate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008781; F:N-acylneuraminate cytidylyltransferase activity; NAS:UniProtKB. DR GO; GO:0047444; F:N-acylneuraminate-9-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro. DR GO; GO:0006055; P:CMP-N-acetylneuraminate biosynthetic process; NAS:UniProtKB. DR GO; GO:0070085; P:glycosylation; IBA:GO_Central. DR CDD; cd11615; SAF_NeuB_like; 1. DR Gene3D; 3.20.20.70; Aldolase class I; 1. DR Gene3D; 3.90.1210.10; Antifreeze-like/N-acetylneuraminic acid synthase C-terminal domain; 1. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR036732; AFP_Neu5c_C_sf. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006013; Antifreeze_III. DR InterPro; IPR013132; Neu5Ac_N. DR InterPro; IPR013974; SAF. DR PANTHER; PTHR42966; N-ACETYLNEURAMINATE SYNTHASE; 1. DR PANTHER; PTHR42966:SF1; SIALIC ACID SYNTHASE; 1. DR Pfam; PF03102; NeuB; 1. DR Pfam; PF08666; SAF; 1. DR PRINTS; PR00357; ANTIFREEZIII. DR SMART; SM00858; SAF; 1. DR SUPFAM; SSF51269; AFP III-like domain; 1. DR SUPFAM; SSF51569; Aldolase; 1. DR PROSITE; PS50844; AFP_LIKE; 1. DR Genevisible; Q9NR45; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Direct protein sequencing; Disease variant; KW Dwarfism; Intellectual disability; Phosphoprotein; Reference proteome; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|Ref.6" FT CHAIN 2..359 FT /note="Sialic acid synthase" FT /id="PRO_0000097750" FT DOMAIN 294..353 FT /note="AFP-like" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00021" FT MOD_RES 61 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99J77" FT MOD_RES 74 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99J77" FT MOD_RES 79 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 275 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q99J77" FT MOD_RES 290 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q99J77" FT VARIANT 29 FT /note="H -> N (in SEMDG; dbSNP:rs1277263564)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076571" FT VARIANT 68 FT /note="E -> D (in dbSNP:rs1058446)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_013308" FT VARIANT 133 FT /note="G -> V (in SEMDG; dbSNP:rs878852980)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076572" FT VARIANT 151 FT /note="R -> H (in SEMDG; dbSNP:rs140402727)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076573" FT VARIANT 188 FT /note="Y -> H (in SEMDG; dbSNP:rs878852981)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076574" FT VARIANT 189 FT /note="P -> L (in SEMDG; dbSNP:rs1024025721)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076575" FT VARIANT 237 FT /note="R -> C (in SEMDG; dbSNP:rs878852982)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076576" FT VARIANT 327 FT /note="I -> II (in SEMDG)" FT /evidence="ECO:0000269|PubMed:27213289" FT /id="VAR_076577" FT CONFLICT 232 FT /note="A -> T (in Ref. 2; BAA91818)" FT /evidence="ECO:0000305" FT CONFLICT 321 FT /note="G -> A (in Ref. 1; AAF75261)" FT /evidence="ECO:0000305" FT STRAND 294..299 FT /evidence="ECO:0007829|PDB:1WVO" FT HELIX 309..311 FT /evidence="ECO:0007829|PDB:1WVO" FT STRAND 312..315 FT /evidence="ECO:0007829|PDB:1WVO" FT STRAND 324..326 FT /evidence="ECO:0007829|PDB:1WVO" FT HELIX 327..330 FT /evidence="ECO:0007829|PDB:1WVO" FT STRAND 334..337 FT /evidence="ECO:0007829|PDB:1WVO" FT HELIX 347..349 FT /evidence="ECO:0007829|PDB:1WVO" FT STRAND 356..358 FT /evidence="ECO:0007829|PDB:1WVO" SQ SEQUENCE 359 AA; 40308 MW; 2E02D47F4F98592F CRC64; MPLELELCPG RWVGGQHPCF IIAEIGQNHQ GDLDVAKRMI RMAKECGADC AKFQKSELEF KFNRKALERP YTSKHSWGKT YGEHKRHLEF SHDQYRELQR YAEEVGIFFT ASGMDEMAVE FLHELNVPFF KVGSGDTNNF PYLEKTAKKG RPMVISSGMQ SMDTMKQVYQ IVKPLNPNFC FLQCTSAYPL QPEDVNLRVI SEYQKLFPDI PIGYSGHETG IAISVAAVAL GAKVLERHIT LDKTWKGSDH SASLEPGELA ELVRSVRLVE RALGSPTKQL LPCEMACNEK LGKSVVAKVK IPEGTILTMD MLTVKVGEPK GYPPEDIFNL VGKKVLVTVE EDDTIMEELV DNHGKKIKS //