SIAS_HUMAN
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 03-AUG-2022, entry version 189.
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.
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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; 74.
DR IntAct; Q9NR45; 22.
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; Q9NR45; -.
DR PeptideAtlas; Q9NR45; -.
DR PRIDE; Q9NR45; -.
DR ProteomicsDB; 82270; -.
DR Antibodypedia; 14440; 226 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 CTD; 54187; -.
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; YRHRVEF; -.
DR OrthoDB; 1117607at2759; -.
DR PhylomeDB; Q9NR45; -.
DR TreeFam; TF324826; -.
DR BioCyc; MetaCyc:HS01818-MON; -.
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; 30 hits in 1075 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 200 other tissues.
DR ExpressionAtlas; Q9NR45; baseline and differential.
DR Genevisible; Q9NR45; HS.
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 Gene3D; 3.20.20.70; -; 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 Pfam; PF03102; NeuB; 1.
DR PRINTS; PR00357; ANTIFREEZIII.
DR SMART; SM00858; SAF; 1.
DR SUPFAM; SSF51269; SSF51269; 1.
DR PROSITE; PS50844; AFP_LIKE; 1.
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
