ID NSD3_HUMAN Reviewed; 1437 AA. AC Q9BZ95; B7ZL11; D3DSX1; Q1RMD3; Q3B796; Q6ZSA5; Q9BYU8; Q9BYU9; AC Q9H2M8; Q9H9W9; Q9NXA6; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 11-JUN-2014, entry version 125. DE RecName: Full=Histone-lysine N-methyltransferase NSD3; DE EC=2.1.1.43; DE AltName: Full=Nuclear SET domain-containing protein 3; DE AltName: Full=Protein whistle; DE AltName: Full=WHSC1-like 1 isoform 9 with methyltransferase activity to lysine; DE AltName: Full=Wolf-Hirschhorn syndrome candidate 1-like protein 1; DE Short=WHSC1-like protein 1; GN Name=WHSC1L1; Synonyms=NSD3; ORFNames=DC28; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). RX PubMed=11549311; DOI=10.1006/geno.2001.6581; RA Stec I., van Ommen G.-J.B., den Dunnen J.T.; RT "WHSC1L1, on human chromosome 8p11.2, closely resembles WHSC1 and maps RT to a duplicated region shared with 4p16.3."; RL Genomics 76:5-8(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND TISSUE RP SPECIFICITY. RX PubMed=11374904; DOI=10.1006/geno.2001.6524; RA Angrand P.-O., Apiou F., Stewart F., Dutrillaux B., Losson R., RA Chambon P.; RT "NSD3, a new SET domain-containing gene, maps to 8p12 and is amplified RT in human breast cancer cell lines."; RL Genomics 74:79-88(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Dendritic cell; RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.; RT "A novel gene from human dendritic cells."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE RP SEQUENCE [LARGE SCALE MRNA] OF 1-383 (ISOFORM 4). RC TISSUE=Brain, and Teratocarcinoma; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 5). RC TISSUE=Brain, 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP CHROMOSOMAL TRANSLOCATION WITH NUP98. RX PubMed=11986249; DOI=10.1182/blood.V99.10.3857; RA Rosati R., La Starza R., Veronese A., Aventin A., Schwienbacher C., RA Vallespi T., Negrini M., Martelli M.F., Mecucci C.; RT "NUP98 is fused to the NSD3 gene in acute myeloid leukemia associated RT with t(8;11)(p11.2;p15)."; RL Blood 99:3857-3860(2002). RN [9] RP INVOLVEMENT IN NSCLC. RX PubMed=15983384; DOI=10.1073/pnas.0504126102; RA Tonon G., Wong K.-K., Maulik G., Brennan C., Feng B., Zhang Y., RA Khatry D.B., Protopopov A., You M.J., Aguirre A.J., Martin E.S., RA Yang Z., Ji H., Chin L., Depinho R.A.; RT "High-resolution genomic profiles of human lung cancer."; RL Proc. Natl. Acad. Sci. U.S.A. 102:9625-9630(2005). RN [10] RP ENZYME ACTIVITY, AND FUNCTION. RX PubMed=16682010; DOI=10.1016/j.bbrc.2006.04.095; RA Kim S.M., Kee H.J., Eom G.H., Choe N.W., Kim J.Y., Kim Y.S., Kim S.K., RA Kook H., Kook H., Seo S.B.; RT "Characterization of a novel WHSC1-associated SET domain protein with RT H3K4 and H3K27 methyltransferase activity."; RL Biochem. Biophys. Res. Commun. 345:318-323(2006). RN [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-790, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., RA Walther T.C., 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 [12] RP INTERACTION WITH BRD4. RX PubMed=21555454; DOI=10.1128/MCB.01341-10; RA Rahman S., Sowa M.E., Ottinger M., Smith J.A., Shi Y., Harper J.W., RA Howley P.M.; RT "The Brd4 extraterminal domain confers transcription activation RT independent of pTEFb by recruiting multiple proteins, including RT NSD3."; RL Mol. Cell. Biol. 31:2641-2652(2011). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [14] RP STRUCTURE BY NMR OF 957-1053. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of second PWWP domain of WHSC1L1 protein."; RL Submitted (DEC-2005) to the PDB data bank. CC -!- FUNCTION: Histone methyltransferase. Preferentially methylates CC 'Lys-4' and 'Lys-27' of histone H3. H3 'Lys-4' methylation CC represents a specific tag for epigenetic transcriptional CC activation, while 'Lys-27' is a mark for transcriptional CC repression. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + L-lysine-[histone] = CC S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. CC -!- SUBUNIT: Interacts with BRD4. CC -!- INTERACTION: CC Q9UER7:DAXX; NbExp=2; IntAct=EBI-3390132, EBI-77321; CC P09017:HOXC4; NbExp=2; IntAct=EBI-3390132, EBI-3923226; CC P41218:MNDA; NbExp=2; IntAct=EBI-3390132, EBI-2829677; CC O95391:SLU7; NbExp=2; IntAct=EBI-3390132, EBI-750559; CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q9BZ95-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BZ95-2; Sequence=VSP_021430; CC Name=3; CC IsoId=Q9BZ95-3; Sequence=VSP_021428, VSP_021429; CC Name=4; CC IsoId=Q9BZ95-4; Sequence=VSP_021427; CC Note=No experimental confirmation available; CC Name=5; CC IsoId=Q9BZ95-5; Sequence=VSP_054489; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Highly expressed in brain, heart and skeletal CC muscle. Expressed at lower level in liver and lung. CC -!- DISEASE: Note=Defects in WHSC1L1 may be involved in non small cell CC lung carcinomas (NSCLC). Amplified or overexpressed in NSCLC. CC -!- DISEASE: Note=A chromosomal aberration involving WHSC1L1 is found CC in childhood acute myeloid leukemia. Translocation CC t(8;11)(p11.2;p15) with NUP98. CC -!- SIMILARITY: Belongs to the class V-like SAM-binding CC methyltransferase superfamily. Histone-lysine methyltransferase CC family. SET2 subfamily. CC -!- SIMILARITY: Contains 1 AWS domain. CC -!- SIMILARITY: Contains 4 PHD-type zinc fingers. CC -!- SIMILARITY: Contains 1 post-SET domain. CC -!- SIMILARITY: Contains 2 PWWP domains. CC -!- SIMILARITY: Contains 1 SET domain. CC -!- SEQUENCE CAUTION: CC Sequence=AAG44637.1; Type=Frameshift; Positions=Several; CC Sequence=AAI07735.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence; CC Sequence=BAA91110.1; Type=Erroneous initiation; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology CC and Haematology; CC URL="http://atlasgeneticsoncology.org/Genes/WHSC1L1NSD3ID42810ch8p11.html"; 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; AF332468; AAK00354.1; -; mRNA. DR EMBL; AF332469; AAK00355.1; -; mRNA. DR EMBL; AJ295990; CAC28350.1; -; mRNA. DR EMBL; AJ295991; CAC28351.1; -; mRNA. DR EMBL; AJ295992; CAC28352.1; -; mRNA. DR EMBL; AF255649; AAG44637.1; ALT_FRAME; mRNA. DR EMBL; AK000360; BAA91110.1; ALT_INIT; mRNA. DR EMBL; AK022560; BAB14099.1; -; mRNA. DR EMBL; AK127594; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; CH471080; EAW63320.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63321.1; -; Genomic_DNA. DR EMBL; BC012059; AAH12059.1; -; mRNA. DR EMBL; BC062631; AAH62631.1; -; mRNA. DR EMBL; BC101717; AAI01718.1; -; mRNA. DR EMBL; BC107734; AAI07735.1; ALT_SEQ; mRNA. DR EMBL; BC113469; AAI13470.1; -; mRNA. DR EMBL; BC115006; AAI15007.1; -; mRNA. DR EMBL; BC143510; AAI43511.1; -; mRNA. DR EMBL; AC087362; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC087623; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR RefSeq; NP_060248.2; NM_017778.2. [Q9BZ95-3] DR RefSeq; NP_075447.1; NM_023034.1. [Q9BZ95-1] DR RefSeq; XP_005273604.1; XM_005273547.1. DR RefSeq; XP_005273605.1; XM_005273548.1. [Q9BZ95-2] DR UniGene; Hs.434966; -. DR UniGene; Hs.608111; -. DR UniGene; Hs.655314; -. DR PDB; 2DAQ; NMR; -; A=957-1053. DR PDB; 4GND; X-ray; 2.27 A; A/C=1310-1413. DR PDB; 4GNE; X-ray; 1.47 A; A=1310-1413. DR PDB; 4GNF; X-ray; 1.55 A; A=1310-1413. DR PDB; 4GNG; X-ray; 1.73 A; A/D=1310-1413. DR PDBsum; 2DAQ; -. DR PDBsum; 4GND; -. DR PDBsum; 4GNE; -. DR PDBsum; 4GNF; -. DR PDBsum; 4GNG; -. DR ProteinModelPortal; Q9BZ95; -. DR SMR; Q9BZ95; 266-332, 700-834, 919-1285, 1316-1413. DR BioGrid; 120250; 19. DR IntAct; Q9BZ95; 16. DR MINT; MINT-4830664; -. DR PhosphoSite; Q9BZ95; -. DR DMDM; 74761342; -. DR MaxQB; Q9BZ95; -. DR PaxDb; Q9BZ95; -. DR PRIDE; Q9BZ95; -. DR DNASU; 54904; -. DR Ensembl; ENST00000316985; ENSP00000313410; ENSG00000147548. [Q9BZ95-3] DR Ensembl; ENST00000317025; ENSP00000313983; ENSG00000147548. [Q9BZ95-1] DR Ensembl; ENST00000433384; ENSP00000393284; ENSG00000147548. [Q9BZ95-2] DR Ensembl; ENST00000527502; ENSP00000434730; ENSG00000147548. DR GeneID; 54904; -. DR KEGG; hsa:54904; -. DR UCSC; uc003xli.3; human. [Q9BZ95-1] DR UCSC; uc003xlj.3; human. [Q9BZ95-3] DR UCSC; uc010lwe.3; human. [Q9BZ95-2] DR CTD; 54904; -. DR GeneCards; GC08M038151; -. DR HGNC; HGNC:12767; WHSC1L1. DR HPA; CAB013721; -. DR HPA; HPA005659; -. DR HPA; HPA018893; -. DR MIM; 607083; gene. DR neXtProt; NX_Q9BZ95; -. DR PharmGKB; PA37370; -. DR eggNOG; COG2940; -. DR HOVERGEN; HBG079979; -. DR InParanoid; Q9BZ95; -. DR KO; K11425; -. DR OMA; MEKDIHK; -. DR OrthoDB; EOG7Z69BG; -. DR PhylomeDB; Q9BZ95; -. DR TreeFam; TF329088; -. DR ChiTaRS; WHSC1L1; human. DR EvolutionaryTrace; Q9BZ95; -. DR GeneWiki; WHSC1L1; -. DR GenomeRNAi; 54904; -. DR NextBio; 35481221; -. DR PRO; PR:Q9BZ95; -. DR ArrayExpress; Q9BZ95; -. DR Bgee; Q9BZ95; -. DR Genevestigator; Q9BZ95; -. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW. DR GO; GO:0018024; F:histone-lysine N-methyltransferase activity; IEA:InterPro. DR GO; GO:0005515; F:protein binding; IPI:IntAct. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0034968; P:histone lysine methylation; IDA:GOC. DR GO; GO:0016571; P:histone methylation; IDA:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.40.10; -; 3. DR InterPro; IPR006560; AWS. DR InterPro; IPR003616; Post-SET_dom. DR InterPro; IPR000313; PWWP_dom. DR InterPro; IPR001214; SET_dom. DR InterPro; IPR019786; Zinc_finger_PHD-type_CS. DR InterPro; IPR011011; Znf_FYVE_PHD. DR InterPro; IPR001965; Znf_PHD. DR InterPro; IPR019787; Znf_PHD-finger. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR Pfam; PF00855; PWWP; 2. DR Pfam; PF00856; SET; 1. DR SMART; SM00570; AWS; 1. DR SMART; SM00249; PHD; 5. DR SMART; SM00508; PostSET; 1. DR SMART; SM00293; PWWP; 2. DR SMART; SM00184; RING; 2. DR SMART; SM00317; SET; 1. DR SUPFAM; SSF57903; SSF57903; 3. DR PROSITE; PS51215; AWS; 1. DR PROSITE; PS50868; POST_SET; 1. DR PROSITE; PS50812; PWWP; 2. DR PROSITE; PS50280; SET; 1. DR PROSITE; PS01359; ZF_PHD_1; 1. DR PROSITE; PS50016; ZF_PHD_2; 2. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Chromosomal rearrangement; Chromosome; Coiled coil; Complete proteome; KW Metal-binding; Methyltransferase; Nucleus; Phosphoprotein; KW Polymorphism; Proto-oncogene; Reference proteome; Repeat; KW S-adenosyl-L-methionine; Transcription; Transcription regulation; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 1437 Histone-lysine N-methyltransferase NSD3. FT /FTId=PRO_0000259521. FT DOMAIN 270 333 PWWP 1. FT DOMAIN 960 1022 PWWP 2. FT DOMAIN 1093 1143 AWS. FT DOMAIN 1145 1262 SET. FT DOMAIN 1269 1285 Post-SET. FT ZN_FING 701 748 PHD-type 1. FT ZN_FING 749 805 PHD-type 2. FT ZN_FING 862 955 PHD-type 3. FT ZN_FING 1321 1368 PHD-type 4; atypical. FT COILED 1033 1069 Potential. FT MOD_RES 150 150 Phosphoserine. FT MOD_RES 790 790 N6-acetyllysine. FT VAR_SEQ 67 129 Missing (in isoform 4). FT /FTId=VSP_021427. FT VAR_SEQ 620 645 ASEISDSCKPLKKRSRASTDVEMTSS -> SADRGVQGSVR FT FSDSSVSAAIEETVD (in isoform 3). FT /FTId=VSP_021428. FT VAR_SEQ 646 1437 Missing (in isoform 3). FT /FTId=VSP_021429. FT VAR_SEQ 871 919 Missing (in isoform 2). FT /FTId=VSP_021430. FT VAR_SEQ 1196 1206 Missing (in isoform 5). FT /FTId=VSP_054489. FT VARIANT 186 186 T -> M (in dbSNP:rs13034). FT /FTId=VAR_061215. FT VARIANT 383 383 R -> P (in dbSNP:rs2234552). FT /FTId=VAR_028950. FT CONFLICT 436 436 G -> R (in Ref. 7; AAI15007). FT CONFLICT 578 578 R -> G (in Ref. 7; AAI15007). FT CONFLICT 829 829 G -> E (in Ref. 2; CAC28350/CAC28351). FT CONFLICT 926 926 C -> R (in Ref. 7; AAI15007). FT CONFLICT 1308 1308 K -> R (in Ref. 7; AAI15007). FT CONFLICT 1430 1430 D -> G (in Ref. 7; AAI15007). FT STRAND 960 967 FT STRAND 969 971 FT STRAND 973 978 FT TURN 981 983 FT HELIX 986 989 FT STRAND 998 1002 FT TURN 1003 1006 FT STRAND 1007 1011 FT STRAND 1013 1018 FT STRAND 1025 1027 FT HELIX 1036 1052 FT TURN 1325 1327 FT STRAND 1331 1335 FT HELIX 1348 1350 FT STRAND 1357 1359 FT HELIX 1363 1365 FT TURN 1368 1370 FT STRAND 1375 1377 FT STRAND 1379 1382 FT TURN 1387 1389 FT TURN 1391 1393 FT TURN 1398 1401 SQ SEQUENCE 1437 AA; 161613 MW; 87E54997A996F7CC CRC64; MDFSFSFMQG IMGNTIQQPP QLIDSANIRQ EDAFDNNSDI AEDGGQTPYE ATLQQGFQYP ATTEDLPPLT NGYPSSISVY ETQTKYQSYN QYPNGSANGF GAVRNFSPTD YYHSEIPNTR PHEILEKPSP PQPPPPPSVP QTVIPKKTGS PEIKLKITKT IQNGRELFES SLCGDLLNEV QASEHTKSKH ESRKEKRKKS NKHDSSRSEE RKSHKIPKLE PEEQNRPNER VDTVSEKPRE EPVLKEEAPV QPILSSVPTT EVSTGVKFQV GDLVWSKVGT YPWWPCMVSS DPQLEVHTKI NTRGAREYHV QFFSNQPERA WVHEKRVREY KGHKQYEELL AEATKQASNH SEKQKIRKPR PQRERAQWDI GIAHAEKALK MTREERIEQY TFIYIDKQPE EALSQAKKSV ASKTEVKKTR RPRSVLNTQP EQTNAGEVAS SLSSTEIRRH SQRRHTSAEE EEPPPVKIAW KTAAARKSLP ASITMHKGSL DLQKCNMSPV VKIEQVFALQ NATGDGKFID QFVYSTKGIG NKTEISVRGQ DRLIISTPNQ RNEKPTQSVS SPEATSGSTG SVEKKQQRRS IRTRSESEKS TEVVPKKKIK KEQVETVPQA TVKTGLQKGA SEISDSCKPL KKRSRASTDV EMTSSAYRDT SDSDSRGLSD LQVGFGKQVD SPSATADADV SDVQSMDSSL SRRGTGMSKK DTVCQICESS GDSLIPCEGE CCKHFHLECL GLASLPDSKF ICMECKTGQH PCFSCKVSGK DVKRCSVGAC GKFYHEACVR KFPTAIFESK GFRCPQHCCS ACSMEKDIHK ASKGRMMRCL RCPVAYHSGD ACIAAGSMLV SSYILICSNH SKRSSNSSAV NVGFCFVCAR GLIVQDHSDP MFSSYAYKSH YLLNESNRAE LMKLPMIPSS SASKKKCEKG GRLLCCESCP ASFHPECLSI EMPEGCWNCN DCKAGKKLHY KQIVWVKLGN YRWWPAEICN PRSVPLNIQG LKHDLGDFPV FFFGSHDYYW VHQGRVFPYV EGDKSFAEGQ TSINKTFKKA LEEAAKRFQE LKAQRESKEA LEIEKNSRKP PPYKHIKANK VIGKVQIQVA DLSEIPRCNC KPADENPCGL ESECLNRMLQ YECHPQVCPA GDRCQNQCFT KRLYPDAEII KTERRGWGLR TKRSIKKGEF VNEYVGELID EEECRLRIKR AHENSVTNFY MLTVTKDRII DAGPKGNYSR FMNHSCNPNC ETQKWTVNGD VRVGLFALCD IPAGMELTFN YNLDCLGNGR TECHCGADNC SGFLGVRPKS ACASTNEEKA KNAKLKQKRR KIKTEPKQMH EDYCFQCGDG GELVMCDKKD CPKAYHLLCL NLTQPPYGKW ECPWHQCDEC SSAAVSFCEF CPHSFCKDHE KGALVPSALE GRLCCSEHDP MAPVSPEYWS KIKCKWESQD HGEEVKE //