ID H2AY_HUMAN Reviewed; 372 AA. AC O75367; O75377; Q503A8; Q7Z5E3; Q96D41; Q9H8P3; Q9UP96; DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 05-OCT-2010, entry version 113. DE RecName: Full=Core histone macro-H2A.1; DE Short=Histone macroH2A1; DE Short=mH2A1; DE AltName: Full=Histone H2A.y; DE Short=H2A/y; DE AltName: Full=Medulloblastoma antigen MU-MB-50.205; GN Name=H2AFY; Synonyms=MACROH2A1; 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 2), AND TISSUE SPECIFICITY. RC TISSUE=Liver; RX MEDLINE=98390273; PubMed=9714746; DOI=10.1016/S0167-4781(98)00098-0; RA Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y., RA Lee K.S., Choe I.S.; RT "Isolation of cDNA clones encoding human histone macroH2A1 subtypes."; RL Biochim. Biophys. Acta 1399:73-77(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Umbilical cord blood; RX MEDLINE=98318631; PubMed=9653160; DOI=10.1073/pnas.95.14.8175; RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., RA Wang Y.-X., Chen S.-J., Chen Z.; RT "Identification of genes expressed in human CD34(+) hematopoietic RT stem/progenitor cells by expressed sequence tags and efficient full- RT length cDNA cloning."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Ovary; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Bone marrow, 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 [6] RP NUCLEOTIDE SEQUENCE [MRNA] OF 6-372 (ISOFORM 3). RC TISSUE=Medulloblastoma; RX MEDLINE=22683448; PubMed=12800201; DOI=10.1002/ijc.11208; RA Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., RA Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., RA Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., RA Asmuss H.-P., Bise K., Mautner J.; RT "Novel tumor antigens identified by autologous antibody screening of RT childhood medulloblastoma cDNA libraries."; RL Int. J. Cancer 106:244-251(2003). RN [7] RP SUBCELLULAR LOCATION. RX PubMed=9634239; DOI=10.1038/31275; RA Costanzi C., Pehrson J.R.; RT "Histone macroH2A1 is concentrated in the inactive X chromosome of RT female mammals."; RL Nature 393:599-601(1998). RN [8] RP FUNCTION. RX PubMed=12718888; DOI=10.1016/S1097-2765(03)00100-X; RA Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S., RA Bouvet P., Dimitrov S.; RT "The histone variant macroH2A interferes with transcription factor RT binding and SWI/SNF nucleosome remodeling."; RL Mol. Cell 11:1033-1041(2003). RN [9] RP UBIQUITINATION AT LYS-116 AND LYS-117, AND MASS SPECTROMETRY. RX PubMed=16129414; DOI=10.1016/j.bbrc.2005.08.046; RA Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.; RT "Histone variant macroH2A1.2 is mono-ubiquitinated at its histone RT domain."; RL Biochem. Biophys. Res. Commun. 336:204-209(2005). RN [10] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=15621527; DOI=10.1016/j.devcel.2004.10.019; RA Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., RA Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., RA Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.; RT "Formation of MacroH2A-containing senescence-associated RT heterochromatin foci and senescence driven by ASF1a and HIRA."; RL Dev. Cell 8:19-30(2005). RN [11] RP BINDING TO ADP-RIBOSE (ISOFORM 1). RX PubMed=15902274; DOI=10.1038/sj.emboj.7600664; RA Karras G.I., Kustatscher G., Buhecha H.R., Allen M.D., Pugieux C., RA Sait F., Bycroft M., Ladurner A.G.; RT "The macro domain is an ADP-ribose binding module."; RL EMBO J. 24:1911-1920(2005). RN [12] RP IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION, RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=15897469; DOI=10.1073/pnas.0408918102; RA Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., RA Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., RA van Lohuizen M.; RT "Stable X chromosome inactivation involves the PRC1 Polycomb complex RT and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 RT ligase."; RL Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, AND RP MASS SPECTROMETRY. 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [14] RP FUNCTION. RX PubMed=16428466; DOI=10.1128/MCB.26.3.1156-1164.2006; RA Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F., RA Studitsky V.M., Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.; RT "Mechanism of polymerase II transcription repression by the histone RT variant macroH2A."; RL Mol. Cell. Biol. 26:1156-1164(2006). RN [15] RP METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, AND RP MASS SPECTROMETRY. RX PubMed=16210244; DOI=10.1074/mcp.M500285-MCP200; RA Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., RA Burlingame A.L.; RT "Mapping post-translational modifications of the histone variant RT MacroH2A1 using tandem mass spectrometry."; RL Mol. Cell. Proteomics 5:194-203(2006). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 RP AND THR-174, AND MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=19007248; DOI=10.1021/ac801708p; RA Wang B., Malik R., Nigg E.A., Korner R.; RT "Evaluation of the low-specificity protease elastase for large-scale RT phosphoproteome analysis."; RL Anal. Chem. 80:9526-9533(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 RP AND THR-178, AND MASS SPECTROMETRY. 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 [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170 AND RP SER-173, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE RP NUCLEOSOME CORE PARTICLE, AND FUNCTION. RX PubMed=16107708; DOI=10.1128/MCB.25.17.7616-7624.2005; RA Chakravarthy S., Gundimella S.K., Caron C., Perche P.-Y., RA Pehrson J.R., Khochbin S., Luger K.; RT "Structural characterization of the histone variant macroH2A."; RL Mol. Cell. Biol. 25:7616-7624(2005). RN [21] RP X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 162-372 (ISOFORM 1), X-RAY RP CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 161-372 (ISOFORM 2), AND BINDING RP TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1). RX PubMed=15965484; DOI=10.1038/nsmb956; RA Kustatscher G., Hothorn M., Pugieux C., Scheffzek K., Ladurner A.G.; RT "Splicing regulates NAD metabolite binding to histone macroH2A."; RL Nat. Struct. Mol. Biol. 12:624-625(2005). CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a CC subset of nucleosomes where it represses transcription. CC Nucleosomes wrap and compact DNA into chromatin, limiting DNA CC accessibility to the cellular machineries which require DNA as a CC template. Histones thereby play a central role in transcription CC regulation, DNA repair, DNA replication and chromosomal stability. CC DNA accessibility is regulated via a complex set of post- CC translational modifications of histones, also called histone code, CC and nucleosome remodeling. Involved in stable X chromosome CC inactivation. Inhibits the binding of transcription factors and CC interferes with the activity of remodeling SWI/SNF complexes. CC Inhibits histone acetylation by EP300 and recruits class I HDACs, CC which induces an hypoacetylated state of chromatin. In addition, CC isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP- CC ribose, and may be involved in ADP-ribose-mediated chromatin CC modulation. CC -!- SUBUNIT: The nucleosome is a histone octamer containing two CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 CC heterotetramer and two H2A-H2B heterodimers. Interacts with SPOP. CC Part of a complex consisting of H2AFY, CUL3 and SPOP. Interacts CC with HDAC1 and HDAC2 (By similarity). CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Enriched in CC inactive X chromosome chromatin and in senescence-associated CC heterochromatin. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=2; CC IsoId=O75367-1; Sequence=Displayed; CC Name=1; CC IsoId=O75367-2; Sequence=VSP_002056; CC Note=Specifically binds ADP-ribose and O-acetyl-ADP-ribose. CC Important residues for binding are Asp-203, Gly-224, Gly-314 and CC Phe-348; CC Name=3; CC IsoId=O75367-3; Sequence=VSP_038379; CC -!- TISSUE SPECIFICITY: Ubiquitous. CC -!- PTM: Monoubiquitinated at either Lys-116 or Lys-117. May also be CC polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 CC complex and does not promote proteasomal degradation. Instead, it CC is required for enrichment in inactive X chromosome chromatin. CC -!- MISCELLANEOUS: The number of individuals with antibodies against CC this antigen is 2-fold higher in pediatric patients with cancer CC compared to healthy controls. CC -!- SIMILARITY: Contains 1 histone H2A domain. CC -!- SIMILARITY: Contains 1 Macro domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF041483; AAC33433.1; -; mRNA. DR EMBL; AF044286; AAC33434.1; -; mRNA. DR EMBL; AF054174; AAC39908.1; -; mRNA. DR EMBL; AK023409; BAB14565.1; -; mRNA. DR EMBL; AC026691; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC013331; AAH13331.1; -; mRNA. DR EMBL; BC095406; AAH95406.1; -; mRNA. DR EMBL; AY134746; AAN08620.1; -; mRNA. DR IPI; IPI00059366; -. DR IPI; IPI00304171; -. DR IPI; IPI00744148; -. DR RefSeq; NP_001035248.1; -. DR RefSeq; NP_004884.1; -. DR RefSeq; NP_613075.1; -. DR RefSeq; NP_613258.2; -. DR UniGene; Hs.420272; -. DR UniGene; Hs.599225; -. DR PDB; 1U35; X-ray; 3.00 A; C/G=1-120. DR PDB; 1ZR3; X-ray; 1.66 A; A/B/C/D=162-372. DR PDB; 1ZR5; X-ray; 2.92 A; A/B=161-372. DR PDB; 2F8N; X-ray; 2.90 A; G=1-119. DR PDB; 2FXK; X-ray; 2.54 A; A/B=162-372. DR PDB; 3HSV; X-ray; 1.43 A; M=172-186. DR PDB; 3IID; X-ray; 1.90 A; A=162-372. DR PDB; 3IIF; X-ray; 2.10 A; A/B/C=162-372. DR PDB; 3IVB; X-ray; 1.75 A; M=167-181. DR PDBsum; 1U35; -. DR PDBsum; 1ZR3; -. DR PDBsum; 1ZR5; -. DR PDBsum; 2F8N; -. DR PDBsum; 2FXK; -. DR PDBsum; 3HSV; -. DR PDBsum; 3IID; -. DR PDBsum; 3IIF; -. DR PDBsum; 3IVB; -. DR ProteinModelPortal; O75367; -. DR DIP; DIP-44283N; -. DR IntAct; O75367; 2. DR MINT; MINT-2866965; -. DR STRING; O75367; -. DR PhosphoSite; O75367; -. DR SWISS-2DPAGE; O75367; -. DR PRIDE; O75367; -. DR Ensembl; ENST00000510038; ENSP00000424971; ENSG00000113648. DR Ensembl; ENST00000511689; ENSP00000423563; ENSG00000113648. DR GeneID; 9555; -. DR KEGG; hsa:9555; -. DR UCSC; uc003lam.1; human. DR UCSC; uc003lan.1; human. DR CTD; 9555; -. DR GeneCards; GC05M134697; -. DR HGNC; HGNC:4740; H2AFY. DR MIM; 610054; gene. DR PharmGKB; PA29117; -. DR eggNOG; prNOG11347; -. DR HOVERGEN; HBG009342; -. DR InParanoid; O75367; -. DR OMA; ANDEELH; -. DR OrthoDB; EOG9QRKQ7; -. DR PhylomeDB; O75367; -. DR NextBio; 35835; -. DR PMAP-CutDB; O75367; -. DR ArrayExpress; O75367; -. DR Bgee; O75367; -. DR CleanEx; HS_H2AFY; -. DR Genevestigator; O75367; -. DR GermOnline; ENSG00000113648; Homo sapiens. DR GO; GO:0001740; C:Barr body; IDA:MGI. DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB. DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB. DR GO; GO:0016568; P:chromatin modification; IEA:UniProtKB-KW. DR GO; GO:0007549; P:dosage compensation; IDA:MGI. DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB. DR InterPro; IPR002589; A1pp. DR InterPro; IPR021171; Core_histone_macro-H2A. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR007125; Histone_core_D. DR InterPro; IPR002119; Histone_H2A. DR Gene3D; G3DSA:1.10.20.10; Histone-fold; 1. DR PANTHER; PTHR23430; Histone_H2A; 1. DR Pfam; PF00125; Histone; 1. DR Pfam; PF01661; Macro; 1. DR PIRSF; PIRSF037942; Core_histone_macro-H2A; 1. DR PRINTS; PR00620; HISTONEH2A. DR SMART; SM00506; A1pp; 1. DR SMART; SM00414; H2A; 1. DR SUPFAM; SSF47113; Histone-fold; 1. DR PROSITE; PS51154; MACRO; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome; KW Complete proteome; DNA-binding; Isopeptide bond; Methylation; KW Nucleosome core; Nucleus; Phosphoprotein; Ubl conjugation. FT INIT_MET 1 1 Removed (By similarity). FT CHAIN 2 372 Core histone macro-H2A.1. FT /FTId=PRO_0000055318. FT DOMAIN 2 117 Histone H2A. FT DOMAIN 184 370 Macro. FT COMPBIAS 118 162 Lys-rich. FT MOD_RES 18 18 N6-methyllysine. FT MOD_RES 123 123 N6,N6-dimethyllysine (Probable). FT MOD_RES 129 129 Phosphothreonine. FT MOD_RES 170 170 Phosphoserine. FT MOD_RES 173 173 Phosphoserine. FT MOD_RES 174 174 Phosphothreonine. FT MOD_RES 178 178 Phosphothreonine. FT CROSSLNK 116 116 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. FT CROSSLNK 117 117 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin); FT alternate. FT VAR_SEQ 159 159 Missing (in isoform 3). FT /FTId=VSP_038379. FT VAR_SEQ 198 229 NLIHSEISNLAGFEVEAIINPTNADIDLKDDL -> QVVQA FT DIASIDSDAVVHPTNTDFYIGGEV (in isoform 1). FT /FTId=VSP_002056. FT CONFLICT 186 186 L -> F (in Ref. 3; BAB14565). FT CONFLICT 210 210 F -> S (in Ref. 3; BAB14565). FT CONFLICT 225 225 L -> P (in Ref. 1; AAC33433). FT CONFLICT 291 291 E -> G (in Ref. 5; AAH95406). FT HELIX 15 19 FT HELIX 25 35 FT STRAND 39 41 FT HELIX 45 70 FT STRAND 74 76 FT HELIX 78 87 FT HELIX 89 94 FT TURN 95 97 FT STRAND 98 100 FT HELIX 111 113 FT STRAND 185 190 FT STRAND 196 202 FT HELIX 204 209 FT STRAND 213 219 FT HELIX 227 252 FT STRAND 260 264 FT STRAND 268 277 FT HELIX 286 303 FT STRAND 307 311 FT HELIX 323 340 FT STRAND 348 355 FT HELIX 356 367 SQ SEQUENCE 372 AA; 39617 MW; 37DED989EF7E69DC CRC64; MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA AVLEYLTAEI LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI ASGGVLPNIH PELLAKKRGS KGKLEAIITP PPAKKAKSPS QKKPVSKKAG GKKGARKSKK KQGEVSKAAS ADSTTEGTPA DGFTVLSTKS LFLGQKLNLI HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE FVEAVLELRK KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY FVLFDSESIG IYVQEMAKLD AN //