MSI4_ARATH
ID MSI4_ARATH Reviewed; 507 AA.
AC O22607; Q42322; Q42323; Q58T21; Q93VF7; Q9SLD1;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 3.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=WD-40 repeat-containing protein MSI4 {ECO:0000305};
DE AltName: Full=Altered cold-responsive gene 1 protein {ECO:0000303|PubMed:14745450};
DE AltName: Full=Nucleosome remodeling factor complex component 4;
DE AltName: Full=Protein MULTICOPY SUPPRESSOR OF IRA1 4 {ECO:0000303|PubMed:9872415};
DE Short=AtMSI4 {ECO:0000303|PubMed:9872415};
GN Name=MSI4 {ECO:0000303|PubMed:9872415};
GN Synonyms=ACG1 {ECO:0000303|PubMed:14745450},
GN FVE {ECO:0000303|PubMed:14745447, ECO:0000303|PubMed:15911588};
GN OrderedLocusNames=At2g19520 {ECO:0000312|Araport:AT2G19520};
GN ORFNames=F3P11.12 {ECO:0000312|EMBL:AAD10151.2};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND MUTAGENESIS OF ALA-222 AND ASP-241.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14745447; DOI=10.1038/ng1295;
RA Ausin I., Alonso-Blanco C., Jarillo J.A., Ruiz-Garcia L.,
RA Martinez-Zapater J.M.;
RT "Regulation of flowering time by FVE, a retinoblastoma-associated
RT protein.";
RL Nat. Genet. 36:162-166(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15911588; DOI=10.1534/genetics.104.036533;
RA Werner J.D., Borevitz J.O., Uhlenhaut N.H., Ecker J.R., Chory J.,
RA Weigel D.;
RT "FRIGIDA-independent variation in flowering time of natural Arabidopsis
RT thaliana accessions.";
RL Genetics 170:1197-1207(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-507, AND ZINC-BINDING.
RC STRAIN=cv. Columbia;
RX PubMed=9872415; DOI=10.1016/s0014-5793(98)01500-2;
RA Kenzior A.L., Folk W.R.;
RT "AtMSI4 and RbAp48 WD-40 repeat proteins bind metal ions.";
RL FEBS Lett. 440:425-429(1998).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-142 AND 452-507.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [8]
RP FUNCTION.
RX PubMed=12548286; DOI=10.1038/ng1085;
RA Blazquez M.A., Ahn J.H., Weigel D.;
RT "A thermosensory pathway controlling flowering time in Arabidopsis
RT thaliana.";
RL Nat. Genet. 33:168-171(2003).
RN [9]
RP FUNCTION.
RX PubMed=14593187; DOI=10.1126/science.1091109;
RA He Y., Michaels S.D., Amasino R.M.;
RT "Regulation of flowering time by histone acetylation in Arabidopsis.";
RL Science 302:1751-1754(2003).
RN [10]
RP FUNCTION.
RX PubMed=14745450; DOI=10.1038/ng1298;
RA Kim H.-J., Hyun Y., Park J.-Y., Park M.-J., Park M.-K., Kim M.D.,
RA Kim H.-J., Lee M.H., Moon J., Lee I., Kim J.;
RT "A genetic link between cold responses and flowering time through FVE in
RT Arabidopsis thaliana.";
RL Nat. Genet. 36:167-171(2004).
RN [11]
RP DWD MOTIF.
RX PubMed=18223036; DOI=10.1105/tpc.107.055418;
RA Lee J.H., Terzaghi W., Gusmaroli G., Charron J.B., Yoon H.J., Chen H.,
RA He Y.J., Xiong Y., Deng X.W.;
RT "Characterization of Arabidopsis and rice DWD proteins and their roles as
RT substrate receptors for CUL4-RING E3 ubiquitin ligases.";
RL Plant Cell 20:152-167(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [13]
RP INTERACTION WITH HOS1, AND SUBCELLULAR LOCATION.
RX PubMed=22960247; DOI=10.1093/pcp/pcs123;
RA Lee J.H., Kim J.J., Kim S.H., Cho H.J., Kim J., Ahn J.H.;
RT "The E3 ubiquitin ligase HOS1 regulates low ambient temperature-responsive
RT flowering in Arabidopsis thaliana.";
RL Plant Cell Physiol. 53:1802-1814(2012).
RN [14]
RP INTERACTION WITH AHL16.
RX PubMed=23394836; DOI=10.1016/j.cub.2013.01.030;
RA Xu Y., Wang Y., Stroud H., Gu X., Sun B., Gan E.S., Ng K.H., Jacobsen S.E.,
RA He Y., Ito T.;
RT "A matrix protein silences transposons and repeats through interaction with
RT retinoblastoma-associated proteins.";
RL Curr. Biol. 23:345-350(2013).
RN [15]
RP FUNCTION.
RX PubMed=25922987; DOI=10.1111/tpj.12868;
RA Luo M., Tai R., Yu C.W., Yang S., Chen C.Y., Lin W.D., Schmidt W., Wu K.;
RT "Regulation of flowering time by the histone deacetylase HDA5 in
RT Arabidopsis.";
RL Plant J. 82:925-936(2015).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH LHP1; PDP1; PDP2 AND PDP3,
RP AND SUBUNIT.
RX PubMed=29314758; DOI=10.1111/jipb.12630;
RA Zhou J.X., Liu Z.W., Li Y.Q., Li L., Wang B., Chen S., He X.J.;
RT "Arabidopsis PWWP domain proteins mediate H3K27 trimethylation on FLC and
RT regulate flowering time.";
RL J. Integr. Plant Biol. 60:362-368(2018).
RN [17]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY DEHYDROABIETINAL.
RC STRAIN=cv. Columbia, cv. Landsberg erecta, cv. No-0, and cv. Wassilewskija;
RX PubMed=32392578; DOI=10.1093/jxb/eraa232;
RA Chowdhury Z., Mohanty D., Giri M.K., Venables B.J., Chaturvedi R., Chao A.,
RA Petros R.A., Shah J.;
RT "Dehydroabietinal promotes flowering time and plant defense in Arabidopsis
RT via the autonomous pathway genes FLOWERING LOCUS D, FVE, and RELATIVE OF
RT EARLY FLOWERING 6.";
RL J. Exp. Bot. 71:4903-4913(2020).
CC -!- FUNCTION: Core histone-binding subunit that may target chromatin
CC assembly factors, chromatin remodeling factors and histone deacetylases
CC to their histone substrates in a manner that is regulated by
CC nucleosomal DNA. Component of the flowering autonomous pathway which
CC positively regulates flowering by promoting transcriptional repression
CC of the flowering repressor FLC. May promote histone deacetylation at
CC the FLC locus leading to the formation of repressive chromatin
CC structures. Forms a histone deacetylase complex with HDA5, HDA6 and FLD
CC that represses FLC gene expression to control flowering time
CC (PubMed:25922987). Also negatively regulates cold-responsive genes.
CC Acts together with PDP1 and MSI5 to regulate the function of the PRC2
CC complex on FLC (PubMed:29314758). Required for systemic acquired
CC resistance (SAR) toward pathogenic bacteria (e.g. Pseudomonas syringae
CC pv tomato DC3000 (avrPto)) (PubMed:32392578). Together with FLD and
CC MSI4/FVE, contributes to dehydroabietinal-dependent (DA, a diterpenoid
CC tricyclic diterpene) activation of flowering ans SAR (PubMed:32392578).
CC {ECO:0000269|PubMed:12548286, ECO:0000269|PubMed:14593187,
CC ECO:0000269|PubMed:14745447, ECO:0000269|PubMed:14745450,
CC ECO:0000269|PubMed:25922987, ECO:0000269|PubMed:29314758,
CC ECO:0000269|PubMed:32392578}.
CC -!- SUBUNIT: Interacts with AHL16 and HOS1 (PubMed:22960247,
CC PubMed:23394836). Interacts with LHP1, PDP1, PDP2 and PDP3
CC (PubMed:29314758). Component of the PRC2 (polycomb repressive complex
CC 2) complex which regulates histone methylation on histone H3K27
CC (PubMed:29314758). {ECO:0000269|PubMed:22960247,
CC ECO:0000269|PubMed:23394836, ECO:0000269|PubMed:29314758}.
CC -!- INTERACTION:
CC O22607; P93831: CLF; NbExp=3; IntAct=EBI-9661079, EBI-307155;
CC O22607; Q9M0V3: DDB1A; NbExp=2; IntAct=EBI-9661079, EBI-1632780;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14745447,
CC ECO:0000269|PubMed:22960247}.
CC -!- TISSUE SPECIFICITY: Expressed in rosette leaves, cauline leaves, main
CC stems and developing fruits. Expressed at higher levels in roots and
CC flowers. {ECO:0000269|PubMed:14745447}.
CC -!- INDUCTION: Induced by dehydroabietinal-dependent (DA), a diterpenoid
CC tricyclic diterpene that promotes flowering and systemic acquired
CC resistance (SAR). {ECO:0000269|PubMed:32392578}.
CC -!- DOMAIN: The DWD box is required for interaction with DDB1A.
CC {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Reduced H3K27me3 level but increased levels of
CC histone H3 acetylation and H3K4me3 on FLC in the fve msi5 double mutant
CC (PubMed:29314758). Delayed flowering (PubMed:32392578). Impaired
CC systemic acquired resistance (SAR) toward pathogenic bacteria (e.g.
CC Pseudomonas syringae pv tomato DC3000 (avrPto)) (PubMed:32392578). Lost
CC ability of dehydroabietinal-dependent (DA, a diterpenoid tricyclic
CC diterpene) to trigger flowering and systemic acquired resistance (SAR)
CC (PubMed:32392578). {ECO:0000269|PubMed:29314758,
CC ECO:0000269|PubMed:32392578}.
CC -!- MISCELLANEOUS: Binds zinc.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10151.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA85542.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF498101; AAP29474.1; -; Genomic_DNA.
DR EMBL; AF498102; AAP29475.1; -; mRNA.
DR EMBL; AY849994; AAX51264.1; -; Genomic_DNA.
DR EMBL; AC005917; AAD10151.2; ALT_INIT; Genomic_DNA.
DR EMBL; CP002685; AEC06891.1; -; Genomic_DNA.
DR EMBL; AY059799; AAL24281.1; -; mRNA.
DR EMBL; AY057655; AAL15286.1; -; mRNA.
DR EMBL; AY081447; AAM10009.1; -; mRNA.
DR EMBL; AF028711; AAD03340.1; -; mRNA.
DR EMBL; Z37286; CAA85542.1; ALT_FRAME; mRNA.
DR EMBL; Z37287; CAA85543.1; -; mRNA.
DR PIR; G84577; G84577.
DR RefSeq; NP_565456.2; NM_127510.5.
DR AlphaFoldDB; O22607; -.
DR SMR; O22607; -.
DR BioGRID; 1826; 34.
DR DIP; DIP-59614N; -.
DR IntAct; O22607; 8.
DR STRING; 3702.AT2G19520.1; -.
DR iPTMnet; O22607; -.
DR PaxDb; O22607; -.
DR PRIDE; O22607; -.
DR ProteomicsDB; 250785; -.
DR EnsemblPlants; AT2G19520.1; AT2G19520.1; AT2G19520.
DR GeneID; 816471; -.
DR Gramene; AT2G19520.1; AT2G19520.1; AT2G19520.
DR KEGG; ath:AT2G19520; -.
DR Araport; AT2G19520; -.
DR TAIR; locus:2050372; AT2G19520.
DR eggNOG; KOG0264; Eukaryota.
DR HOGENOM; CLU_020445_2_0_1; -.
DR InParanoid; O22607; -.
DR OMA; GHKAAWS; -.
DR OrthoDB; 831322at2759; -.
DR PhylomeDB; O22607; -.
DR PRO; PR:O22607; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O22607; baseline and differential.
DR Genevisible; O22607; AT.
DR GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:TAIR.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0035098; C:ESC/E(Z) complex; IDA:UniProtKB.
DR GO; GO:0000118; C:histone deacetylase complex; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005730; C:nucleolus; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IDA:TAIR.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:TAIR.
DR GO; GO:0009908; P:flower development; IEA:UniProtKB-KW.
DR GO; GO:0080188; P:gene silencing by RNA-directed DNA methylation; IDA:TAIR.
DR GO; GO:0043966; P:histone H3 acetylation; IMP:UniProtKB.
DR GO; GO:0098532; P:histone H3-K27 trimethylation; IMP:UniProtKB.
DR GO; GO:0080182; P:histone H3-K4 trimethylation; IMP:UniProtKB.
DR GO; GO:2000028; P:regulation of photoperiodism, flowering; IMP:UniProtKB.
DR GO; GO:0048510; P:regulation of timing of transition from vegetative to reproductive phase; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1904629; P:response to diterpene; IMP:UniProtKB.
DR GO; GO:0010224; P:response to UV-B; IEP:TAIR.
DR GO; GO:0009627; P:systemic acquired resistance; IMP:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 4.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromatin regulator; Developmental protein; Differentiation;
KW Flowering; Nucleus; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; WD repeat.
FT CHAIN 1..507
FT /note="WD-40 repeat-containing protein MSI4"
FT /id="PRO_0000051083"
FT REPEAT 95..137
FT /note="WD 1"
FT /evidence="ECO:0000255"
FT REPEAT 162..202
FT /note="WD 2"
FT /evidence="ECO:0000255"
FT REPEAT 217..257
FT /note="WD 3"
FT /evidence="ECO:0000255"
FT REPEAT 290..330
FT /note="WD 4"
FT /evidence="ECO:0000255"
FT REPEAT 335..375
FT /note="WD 5"
FT /evidence="ECO:0000255"
FT REPEAT 384..424
FT /note="WD 6"
FT /evidence="ECO:0000255"
FT REPEAT 439..486
FT /note="WD 7"
FT /evidence="ECO:0000255"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 308..323
FT /note="DWD box"
FT /evidence="ECO:0000255"
FT COMPBIAS 258..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT MUTAGEN 222
FT /note="A->V: In allele fve-1; loss of function allele that
FT causes increased levels of FLC and late flowering."
FT /evidence="ECO:0007744|PubMed:22223895"
FT MUTAGEN 241
FT /note="D->N: In allele fve-2; loss of function allele that
FT causes increased levels of FLC and late flowering."
FT /evidence="ECO:0000269|PubMed:14745447"
FT CONFLICT 89
FT /note="W -> L (in Ref. 7; CAA85542)"
FT /evidence="ECO:0000269|PubMed:14745447"
FT CONFLICT 126
FT /note="V -> F (in Ref. 7; CAA85542)"
FT /evidence="ECO:0000305"
FT CONFLICT 202
FT /note="A -> P (in Ref. 6; AAD03340)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="T -> P (in Ref. 6; AAD03340)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> A (in Ref. 7; CAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 489
FT /note="V -> F (in Ref. 7; CAA85543)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="E -> A (in Ref. 6; AAD03340)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 507 AA; 55759 MW; C37F8000F8B33397 CRC64;
MESDEAAAVS PQATTPSGGT GASGPKKRGR KPKTKEDSQT PSSQQQSDVK MKESGKKTQQ
SPSVDEKYSQ WKGLVPILYD WLANHNLVWP SLSCRWGPQL EQATYKNRQR LYLSEQTDGS
VPNTLVIANC EVVKPRVAAA EHISQFNEEA RSPFVKKYKT IIHPGEVNRI RELPQNSKIV
ATHTDSPDVL IWDVETQPNR HAVLGAANSR PDLILTGHQD NAEFALAMCP TEPFVLSGGK
DKSVVLWSIQ DHITTIGTDS KSSGSIIKQT GEGTDKNESP TVGPRGVYHG HEDTVEDVAF
SPTSAQEFCS VGDDSCLILW DARTGTNPVT KVEKAHDADL HCVDWNPHDD NLILTGSADN
TVRLFDRRKL TANGVGSPIY KFEGHKAAVL CVQWSPDKSS VFGSSAEDGL LNIWDYDRVS
KKSDRAAKSP AGLFFQHAGH RDKVVDFHWN ASDPWTIVSV SDDCETTGGG GTLQIWRMSD
LIYRPEEEVV AELEKFKSHV MTCASKP
