HIR1_YEAST
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 03-AUG-2022, entry version 202.
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=6; IntAct=EBI-8316, EBI-3003;
CC P32479; P32479: HIR1; NbExp=4; IntAct=EBI-8316, EBI-8316;
CC P32479; P32480: HIR2; NbExp=8; IntAct=EBI-8316, EBI-8323;
CC P32479; Q01448: HPC2; NbExp=6; 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};
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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 AlphaFoldDB; P32479; -.
DR SMR; P32479; -.
DR BioGRID; 32691; 500.
DR ComplexPortal; CPX-124; HIR complex.
DR DIP; DIP-2365N; -.
DR IntAct; P32479; 34.
DR MINT; P32479; -.
DR STRING; 4932.YBL008W; -.
DR iPTMnet; P32479; -.
DR MaxQB; P32479; -.
DR PaxDb; P32479; -.
DR PRIDE; P32479; -.
DR EnsemblFungi; YBL008W_mRNA; YBL008W; YBL008W.
DR GeneID; 852275; -.
DR KEGG; sce:YBL008W; -.
DR SGD; S000000104; HIR1.
DR VEuPathDB; FungiDB:YBL008W; -.
DR eggNOG; KOG0973; Eukaryota.
DR GeneTree; ENSGT00550000074919; -.
DR HOGENOM; CLU_004372_3_0_1; -.
DR InParanoid; P32479; -.
DR OMA; KRFDVHQ; -.
DR BioCyc; YEAST:G3O-28914-MON; -.
DR Reactome; R-SCE-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR PRO; PR:P32479; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32479; protein.
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; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:SGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; IDA:SGD.
DR GO; GO:1905268; P:negative regulation of chromatin organization; IDA:ComplexPortal.
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:0006368; P:transcription elongation from RNA polymerase II promoter; IGI:SGD.
DR Gene3D; 2.130.10.10; -; 2.
DR InterPro; IPR031120; HIR1.
DR InterPro; IPR011494; Hira.
DR InterPro; IPR019015; HIRA_B_motif.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR PANTHER; PTHR13831; PTHR13831; 1.
DR Pfam; PF07569; Hira; 1.
DR Pfam; PF09453; HIRA_B; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 2.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 4.
DR PROSITE; PS50294; WD_REPEATS_REGION; 2.
PE 1: Evidence at protein level;
KW Centromere; Chromatin regulator; Chromosome; Nucleus; Phosphoprotein;
KW 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 440..466
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"
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
