ID HIR1_YEAST Reviewed; 840 AA. AC P32479; D6VPZ2; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 3. DT 02-SEP-2026, entry version 220. DE RecName: Full=Protein HIR1; DE AltName: Full=Histone transcription regulator 1; GN Name=HIR1; OrderedLocusNames=YBL008W; ORFNames=YBL0318; OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=559292; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION. RX PubMed=8417331; DOI=10.1128/mcb.13.1.28-38.1993; RA Sherwood P.W., Tsang S.V., Osley M.A.; RT "Characterization of HIR1 and HIR2, two genes required for regulation of RT histone gene transcription in Saccharomyces cerevisiae."; RL Mol. Cell. Biol. 13:28-38(1993). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=1441753; DOI=10.1002/yea.320080909; RA Delaveau T., Jacq C., Perea J.; RT "Sequence of a 12.7 kb segment of yeast chromosome II identifies a PDR-like RT gene and several new open reading frames."; RL Yeast 8:761-768(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 204508 / S288c; RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x; RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H., RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., RA Mewes H.-W., Kleine K.; RT "Complete DNA sequence of yeast chromosome II."; RL EMBO J. 13:5795-5809(1994). RN [4] RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 260. RC STRAIN=ATCC 204508 / S288c; RX PubMed=24374639; DOI=10.1534/g3.113.008995; RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.; RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now."; RL G3 (Bethesda) 4:389-398(2014). RN [5] RP FUNCTION, AND INTERACTION WITH HIR2. RX PubMed=9001207; DOI=10.1128/mcb.17.2.545; RA Spector M.S., Raff A., DeSilva H., Lee K., Osley M.A.; RT "Hir1p and Hir2p function as transcriptional corepressors to regulate RT histone gene transcription in the Saccharomyces cerevisiae cell cycle."; RL Mol. Cell. Biol. 17:545-552(1997). RN [6] RP FUNCTION, SELF-ASSOCIATION, AND INTERACTION WITH HIR2 AND SPT4. RX PubMed=9504914; DOI=10.1093/genetics/148.2.657; RA DeSilva H., Lee K., Osley M.A.; RT "Functional dissection of yeast Hir1p, a WD repeat-containing RT transcriptional corepressor."; RL Genetics 148:657-667(1998). RN [7] RP FUNCTION. RX PubMed=9671488; DOI=10.1128/mcb.18.8.4783; RA Qian Z., Huang H., Hong J.Y., Burck C.L., Johnston S.D., Berman J., RA Carol A., Liebman S.W.; RT "Yeast Ty1 retrotransposition is stimulated by a synergistic interaction RT between mutations in chromatin assembly factor I and histone regulatory RT proteins."; RL Mol. Cell. Biol. 18:4783-4792(1998). RN [8] RP FUNCTION. RX PubMed=9671489; DOI=10.1128/mcb.18.8.4793; RA Kaufman P.D., Cohen J.L., Osley M.A.; RT "Hir proteins are required for position-dependent gene silencing in RT Saccharomyces cerevisiae in the absence of chromatin assembly factor I."; RL Mol. Cell. Biol. 18:4793-4806(1998). RN [9] RP FUNCTION, AND INTERACTION WITH SNF2; SNF5 AND SWI3. RX PubMed=10445029; DOI=10.1016/s1097-2765(00)80189-6; RA Dimova D., Nackerdien Z., Furgeson S., Eguchi S., Osley M.A.; RT "A role for transcriptional repressors in targeting the yeast Swi/Snf RT complex."; RL Mol. Cell 4:75-83(1999). RN [10] RP FUNCTION, AND INTERACTION WITH ASF1. RX PubMed=11412995; DOI=10.1016/s0960-9822(01)00140-3; RA Sharp J.A., Fouts E.T., Krawitz D.C., Kaufman P.D.; RT "Yeast histone deposition protein Asf1p requires Hir proteins and PCNA for RT heterochromatic silencing."; RL Curr. Biol. 11:463-473(2001). RN [11] RP FUNCTION, AND INTERACTION WITH ASF1. RX PubMed=11404324; DOI=10.1093/genetics/158.2.587; RA Sutton A., Bucaria J., Osley M.A., Sternglanz R.; RT "Yeast ASF1 protein is required for cell cycle regulation of histone gene RT transcription."; RL Genetics 158:587-596(2001). RN [12] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=11782447; DOI=10.1101/gad.925302; RA Sharp J.A., Franco A.A., Osley M.A., Kaufman P.D.; RT "Chromatin assembly factor I and Hir proteins contribute to building RT functional kinetochores in S. cerevisiae."; RL Genes Dev. 16:85-100(2002). RN [13] RP FUNCTION. RX PubMed=11937489; DOI=10.1101/gad.978902; RA Ng H.H., Robert F., Young R.A., Struhl K.; RT "Genome-wide location and regulated recruitment of the RSC nucleosome- RT remodeling complex."; RL Genes Dev. 16:806-819(2002). RN [14] RP FUNCTION. RX PubMed=12524332; DOI=10.1093/genetics/162.4.1557; RA Formosa T., Ruone S., Adams M.D., Olsen A.E., Eriksson P., Yu Y., RA Rhoades A.R., Kaufman P.D., Stillman D.J.; RT "Defects in SPT16 or POB3 (yFACT) in Saccharomyces cerevisiae cause RT dependence on the Hir/Hpc pathway: polymerase passage may degrade chromatin RT structure."; RL Genetics 162:1557-1571(2002). RN [15] RP FUNCTION. RX PubMed=11756556; DOI=10.1128/mcb.22.2.614-625.2002; RA Krawitz D.C., Kama T., Kaufman P.D.; RT "Chromatin assembly factor I mutants defective for PCNA binding require RT Asf1/Hir proteins for silencing."; RL Mol. Cell. Biol. 22:614-625(2002). RN [16] RP FUNCTION. RX PubMed=12975325; DOI=10.1101/gad.1131103; RA Sharp J.A., Krawitz D.C., Gardner K.A., Fox C.A., Kaufman P.D.; RT "The budding yeast silencing protein Sir1 is a functional component of RT centromeric chromatin."; RL Genes Dev. 17:2356-2361(2003). RN [17] RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]. RX PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., RA O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [18] RP FUNCTION. RX PubMed=15057281; DOI=10.1038/sj.emboj.7600161; RA Crotti L.B., Basrai M.A.; RT "Functional roles for evolutionarily conserved Spt4p at centromeres and RT heterochromatin in Saccharomyces cerevisiae."; RL EMBO J. 23:1804-1814(2004). RN [19] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX RP WITH HIR2; HIR3 AND HPC2, AND INTERACTION WITH ASF1. RX PubMed=16303565; DOI=10.1016/j.cub.2005.10.053; RA Green E.M., Antczak A.J., Bailey A.O., Franco A.A., Wu K.J., RA Yates J.R. III, Kaufman P.D.; RT "Replication-independent histone deposition by the HIR complex and Asf1."; RL Curr. Biol. 15:2044-2049(2005). RN [20] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A RP COMPLEX WITH HIR2; HIR3 AND HPC2. RX PubMed=16264190; DOI=10.1101/gad.1341105; RA Prochasson P., Florens L., Swanson S.K., Washburn M.P., Workman J.L.; RT "The HIR corepressor complex binds to nucleosomes generating a distinct RT protein/DNA complex resistant to remodeling by SWI/SNF."; RL Genes Dev. 19:2534-2539(2005). RN [21] RP FUNCTION. RX PubMed=16020781; DOI=10.1534/genetics.105.044719; RA Sharp J.A., Rizki G., Kaufman P.D.; RT "Regulation of histone deposition proteins Asf1/Hir1 by multiple DNA damage RT checkpoint kinases in Saccharomyces cerevisiae."; RL Genetics 171:885-899(2005). RN [22] RP FUNCTION. RX PubMed=16039596; DOI=10.1016/j.molcel.2005.05.028; RA Schermer U.J., Korber P., Hoerz W.; RT "Histones are incorporated in trans during reassembly of the yeast PHO5 RT promoter."; RL Mol. Cell 19:279-285(2005). RN [23] RP FUNCTION. RX PubMed=16449659; DOI=10.1128/mcb.26.4.1496-1509.2006; RA Nourani A., Robert F., Winston F.; RT "Evidence that Spt2/Sin1, an HMG-like factor, plays roles in transcription RT elongation, chromatin structure, and genome stability in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 26:1496-1509(2006). RN [24] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ADR376; RX PubMed=17330950; DOI=10.1021/pr060559j; RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., RA Elias J.E., Gygi S.P.; RT "Large-scale phosphorylation analysis of alpha-factor-arrested RT Saccharomyces cerevisiae."; RL J. Proteome Res. 6:1190-1197(2007). RN [25] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200; RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; RT "A multidimensional chromatography technology for in-depth phosphoproteome RT analysis."; RL Mol. Cell. Proteomics 7:1389-1396(2008). RN [26] RP INTERACTION WITH RTT106, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE. RX PubMed=19683497; DOI=10.1016/j.molcel.2009.06.023; RA Fillingham J., Kainth P., Lambert J.P., van Bakel H., Tsui K., RA Pena-Castillo L., Nislow C., Figeys D., Hughes T.R., Greenblatt J., RA Andrews B.J.; RT "Two-color cell array screen reveals interdependent roles for histone RT chaperones and a chromatin boundary regulator in histone gene repression."; RL Mol. Cell 35:340-351(2009). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19779198; DOI=10.1126/science.1172867; RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.; RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights RT into evolution."; RL Science 325:1682-1686(2009). CC -!- FUNCTION: Component of the HIR complex, which cooperates with ASF1 to CC promote replication-independent chromatin assembly. The HIR complex is CC also required for the periodic repression of three of the four histone CC gene loci during cell cycle as well as for autogenous regulation of the CC HTA1-HTB1 locus by H2A and H2B. DNA-binding by the HIR complex may CC repress transcription by inhibiting nucleosome remodeling by the CC SWI/SNF complex. The HIR complex may also be required for CC transcriptional silencing of centromeric, telomeric and mating-type CC loci in the absence of CAF-1. {ECO:0000269|PubMed:10445029, CC ECO:0000269|PubMed:11404324, ECO:0000269|PubMed:11412995, CC ECO:0000269|PubMed:11756556, ECO:0000269|PubMed:11782447, CC ECO:0000269|PubMed:11937489, ECO:0000269|PubMed:12524332, CC ECO:0000269|PubMed:12975325, ECO:0000269|PubMed:15057281, CC ECO:0000269|PubMed:16020781, ECO:0000269|PubMed:16039596, CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565, CC ECO:0000269|PubMed:16449659, ECO:0000269|PubMed:8417331, CC ECO:0000269|PubMed:9001207, ECO:0000269|PubMed:9504914, CC ECO:0000269|PubMed:9671488, ECO:0000269|PubMed:9671489}. CC -!- SUBUNIT: Component of the HIR complex, composed of HIR1, HIR2, HIR3 and CC HPC2 (PubMed:16264190, PubMed:16303565, PubMed:9001207, CC PubMed:9504914). This complex may consist of one copy of HIR1 and HIR3 CC and two copies of HIR2 and HPC2 (PubMed:16264190). The HIR complex CC interacts with ASF1 (PubMed:11404324, PubMed:11412995). Interacts with CC SNF2 (PubMed:10445029). Interacts with SNF5 (PubMed:10445029). CC Interacts with SWI3 (PubMed:10445029). Interacts with RTT106 CC (PubMed:19683497). May interact with SPT4 (PubMed:9504914). May self- CC associate (PubMed:9504914). {ECO:0000269|PubMed:10445029, CC ECO:0000269|PubMed:11404324, ECO:0000269|PubMed:11412995, CC ECO:0000269|PubMed:16264190, ECO:0000269|PubMed:16303565, CC ECO:0000269|PubMed:19683497, ECO:0000269|PubMed:9001207, CC ECO:0000269|PubMed:9504914}. CC -!- INTERACTION: CC P32479; P32447: ASF1; NbExp=7; IntAct=EBI-8316, EBI-3003; CC P32479; P32479: HIR1; NbExp=4; IntAct=EBI-8316, EBI-8316; CC P32479; P32480: HIR2; NbExp=9; IntAct=EBI-8316, EBI-8323; CC P32479; Q01448: HPC2; NbExp=7; IntAct=EBI-8316, EBI-8520; CC P32479; P32914: SPT4; NbExp=2; IntAct=EBI-8316, EBI-17928; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11782447}. CC Chromosome, centromere {ECO:0000269|PubMed:11782447}. Chromosome CC {ECO:0000269|PubMed:19683497}. Note=Enriched at centromeres CC (PubMed:11782447). Localizes to the promoter region of histones HTA1- CC HTB1, HHT1-HHF1, and HHT2-HHF2, (PubMed:19683497). CC {ECO:0000269|PubMed:11782447, ECO:0000269|PubMed:19683497}. CC -!- DISRUPTION PHENOTYPE: Decreases nucleosomal density (PubMed:19683497). CC Increases HTA1 RNA level; simultaneous disruption RTT109 alleviates the CC effect (PubMed:19683497). Abolishes localization of RTT106 to the HTA1- CC HTB1 promoter (PubMed:19683497). {ECO:0000269|PubMed:19683497}. CC -!- MISCELLANEOUS: Present with 846 molecules/cell in log phase SD medium. CC {ECO:0000269|PubMed:14562106}. CC -!- SIMILARITY: Belongs to the WD repeat HIR1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=L03838; Type=Frameshift; Evidence={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; L03838; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; S47695; AAB23989.1; -; Genomic_DNA. DR EMBL; Z35769; CAA84827.1; -; Genomic_DNA. DR EMBL; BK006936; DAA07112.2; -; Genomic_DNA. DR PIR; S41218; S41218. DR RefSeq; NP_009545.2; NM_001178248.2. DR PDB; 8GHL; EM; 2.96 A; A/G=1-840. DR PDB; 8GHM; EM; 12.00 A; A/G=1-840. DR PDB; 8GHN; EM; 2.96 A; A/G=1-840. DR AlphaFoldDB; P32479; -. DR SMR; P32479; -. DR BioGRID; 32691; 514. DR ComplexPortal; CPX-124; HIR histone chaperone complex. DR DIP; DIP-2365N; -. DR FunCoup; P32479; 247. DR IntAct; P32479; 38. DR MINT; P32479; -. DR STRING; 4932.YBL008W; -. DR iPTMnet; P32479; -. DR PaxDb; 4932-YBL008W; -. DR PeptideAtlas; P32479; -. DR EnsemblFungi; YBL008W_mRNA; YBL008W; YBL008W. DR GeneID; 852275; -. DR KEGG; sce:YBL008W; -. DR AGR; SGD:S000000104; -. DR SGD; S000000104; HIR1. DR VEuPathDB; FungiDB:YBL008W; -. DR eggNOG; KOG0973; Eukaryota. DR HOGENOM; CLU_004372_3_0_1; -. DR InParanoid; P32479; -. DR OMA; KRFDVHQ; -. DR OrthoDB; 1741719at2759; -. DR BioCyc; YEAST:G3O-28914-MONOMER; -. DR Reactome; R-SCE-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF). DR BioGRID-ORCS; 852275; 7 hits in 10 CRISPR screens. DR PRO; PR:P32479; -. DR Proteomes; UP000002311; Chromosome II. DR RNAct; P32479; protein. DR GO; GO:0005694; C:chromosome; EXP:UniProtKB. DR GO; GO:0000775; C:chromosome, centromeric region; IDA:SGD. DR GO; GO:0000417; C:HIR complex; IDA:SGD. DR GO; GO:0005634; C:nucleus; EXP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD. DR GO; GO:0006325; P:chromatin organization; IDA:SGD. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:SGD. DR GO; GO:0016480; P:negative regulation of transcription by RNA polymerase III; IMP:SGD. DR GO; GO:0006334; P:nucleosome assembly; IDA:ComplexPortal. DR GO; GO:1902275; P:regulation of chromatin organization; IDA:ComplexPortal. DR GO; GO:0006368; P:transcription elongation by RNA polymerase II; IGI:SGD. DR FunFam; 2.130.10.10:FF:000290; Protein HIR; 1. DR FunFam; 2.130.10.10:FF:001073; Protein HIR; 1. DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2. DR InterPro; IPR055410; Beta-prop_CAF1B_HIR1. DR InterPro; IPR031120; HIR1-like. DR InterPro; IPR011494; HIRA-like_C. DR InterPro; IPR019015; HIRA_B_motif. DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf. DR InterPro; IPR036322; WD40_repeat_dom_sf. DR InterPro; IPR001680; WD40_rpt. DR PANTHER; PTHR13831; MEMBER OF THE HIR1 FAMILY OF WD-REPEAT PROTEINS; 1. DR PANTHER; PTHR13831:SF0; PROTEIN HIRA; 1. DR Pfam; PF24105; Beta-prop_CAF1B_HIR1; 1. DR Pfam; PF07569; Hira; 1. DR Pfam; PF09453; HIRA_B; 1. DR SMART; SM00320; WD40; 6. DR SUPFAM; SSF50978; WD40 repeat-like; 2. DR PROSITE; PS00678; WD_REPEATS_1; 1. DR PROSITE; PS50082; WD_REPEATS_2; 4. DR PROSITE; PS50294; WD_REPEATS_REGION; 2. DR PDBsum; 8GHL; -. DR PDBsum; 8GHM; -. DR PDBsum; 8GHN; -. PE 1: Evidence at protein level; KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; WD repeat. FT CHAIN 1..840 FT /note="Protein HIR1" FT /id="PRO_0000051016" FT REPEAT 15..54 FT /note="WD 1" FT REPEAT 77..116 FT /note="WD 2" FT REPEAT 135..174 FT /note="WD 3" FT REPEAT 177..216 FT /note="WD 4" FT REPEAT 230..273 FT /note="WD 5" FT REPEAT 312..350 FT /note="WD 6" FT REPEAT 354..393 FT /note="WD 7" FT REGION 1..389 FT /note="Mediates transcriptional repression" FT REGION 304..840 FT /note="Interaction with ASF1" FT REGION 392..840 FT /note="Mediates transcriptional repression, self- FT association and interaction with HIR2" FT REGION 436..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 582..602 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..465 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 610 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17330950, FT ECO:0007744|PubMed:18407956" FT CONFLICT 32 FT /note="L -> F (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 260 FT /note="V -> M (in Ref. 2; AAB23989 and 3; CAA84827)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="W -> M (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 2..4 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 20..25 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 29..36 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 41..45 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 46..58 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 63..65 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 66..68 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 72..75 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 82..87 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 103..111 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 115..117 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 124..133 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 140..145 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 149..156 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 161..165 FT /evidence="ECO:0007829|PDB:8GHN" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 171..175 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 182..187 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 191..198 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 203..209 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 215..222 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 224..226 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 244..253 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 255..264 FT /evidence="ECO:0007829|PDB:8GHN" FT TURN 265..267 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 281..291 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 325..332 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 337..341 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 348..357 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 368..375 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 378..384 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 396..401 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 404..406 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 413..416 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 419..435 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 488..490 FT /evidence="ECO:0007829|PDB:8GHN" FT STRAND 493..496 FT /evidence="ECO:0007829|PDB:8GHN" FT HELIX 545..550 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 557..559 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 565..567 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 621..623 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 627..631 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 639..642 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 648..650 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 652..657 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 659..668 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 673..675 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 679..684 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 687..705 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 707..712 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 714..716 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 718..735 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 737..740 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 748..754 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 757..762 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 765..771 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 772..775 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 776..784 FT /evidence="ECO:0007829|PDB:8GHL" FT HELIX 785..788 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 793..796 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 803..810 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 811..814 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 815..821 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 822..824 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 825..829 FT /evidence="ECO:0007829|PDB:8GHL" FT TURN 831..833 FT /evidence="ECO:0007829|PDB:8GHL" FT STRAND 835..838 FT /evidence="ECO:0007829|PDB:8GHL" SQ SEQUENCE 840 AA; 93858 MW; 40A2932F3306358A CRC64; MKVVKFPWLA HREESRKYEI YTVDVSHDGK RLATGGLDGK IRIWSIDSIL RCMELESLTP EIPLPQDLQM PLCSMSRHTG SITCVKFSPD GKYLASGSDD RILLIWALDE EQSSQPAFGS EHEREHWTVR KRLVAHDNDI QDICWAPDSS ILVTVGLDRS VIVWNGSTFE KLKRFDVHQS LVKGVVFDPA NKYFATTSDD RTMKIFRYHK TGDISFTIEH IITEPFKESP LTTYFRRPSW SPDGQHIAVP NATNGPVSSV AIVNRGTWDT NVSLIGHDAP TEVARFNPRL FERNAGVKQK KDDDPENALV GQNDDKVHHF DKNIDSVVAT AGQDKSLAVW STSRPRPILV AFDIANKSIT DMSWNPDGSL LFVASLDSSI TLFKFENNEL GKPIPLEKNM EQLYRYGVDK DSLDFPESIN QLLLEDQTKS FKHTKISTSK LGENHPTLAT NSASNQKDNN DASVSRSEHI NILIPKRKKD AILNKAVTLK SGKKRVAPTL ISTSSSSPFS NGIKKPTLDS KRIENNVKSS TKTINSKNTL LNVPEGVEKK ISISSFPLPR LGIHSLIMGT KERSAWKISN SELENDDADN AGGKGSDGTS NSIDDIAVLS EEENDFHRMT LNAKLTQEKI WSEEPTTRCL LQSDVIPDTD VVVLEGGSLD DIAVLEIRNG VERSIQFDSE ALLDNPTRIL GYQGGKRTIE TFIPEVIICA IGSKDCKCWC LASANGSIYI LSYNGQQRIP KICLGHKVIK MVTSSKYLLV LTERGLFFAW DLLDLKLVLR NVPILPILNG QPIHGNKVRI NKVIKCFRLD GSSCDLLLEV GDPKNVYKWT KDLGCWSLYK //