DRB1_ARATH
ID DRB1_ARATH Reviewed; 419 AA.
AC O04492; C0Z3F9;
DT 08-FEB-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=Double-stranded RNA-binding protein 1;
DE AltName: Full=Protein HYPONASTIC LEAVES 1;
DE AltName: Full=dsRNA-binding protein 1;
DE Short=AtDRB1;
GN Name=DRB1; Synonyms=HYL1; OrderedLocusNames=At1g09700; ORFNames=F21M12.9;
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 [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. No-0;
RX PubMed=11148283; DOI=10.2307/3871234;
RA Lu C., Fedoroff N.;
RT "A mutation in the Arabidopsis HYL1 gene encoding a dsRNA binding protein
RT affects responses to abscisic acid, auxin, and cytokinin.";
RL Plant Cell 12:2351-2366(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=cv. Columbia;
RX PubMed=19423640; DOI=10.1093/dnares/dsp009;
RA Iida K., Fukami-Kobayashi K., Toyoda A., Sakaki Y., Kobayashi M., Seki M.,
RA Shinozaki K.;
RT "Analysis of multiple occurrences of alternative splicing events in
RT Arabidopsis thaliana using novel sequenced full-length cDNAs.";
RL DNA Res. 16:155-164(2009).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14972688; DOI=10.1016/j.cub.2004.01.035;
RA Vazquez F., Gasciolli V., Crete P., Vaucheret H.;
RT "The nuclear dsRNA binding protein HYL1 is required for microRNA
RT accumulation and plant development, but not posttranscriptional transgene
RT silencing.";
RL Curr. Biol. 14:346-351(2004).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14722360; DOI=10.1073/pnas.0307969100;
RA Han M.H., Goud S., Song L., Fedoroff N.;
RT "The Arabidopsis double-stranded RNA-binding protein HYL1 plays a role in
RT microRNA-mediated gene regulation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:1093-1098(2004).
RN [8]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH DCL1; DRB2; DRB4 AND DRB5.
RX PubMed=15821876; DOI=10.1007/s11103-004-6853-5;
RA Hiraguri A., Itoh R., Kondo N., Nomura Y., Aizawa D., Murai Y., Koiwa H.,
RA Seki M., Shinozaki K., Fukuhara T.;
RT "Specific interactions between Dicer-like proteins and HYL1/DRB-family
RT dsRNA-binding proteins in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:173-188(2005).
RN [9]
RP FUNCTION, INTERACTION WITH SE, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=16889646; DOI=10.1111/j.1365-313x.2006.02835.x;
RA Yang L., Liu Z., Lu F., Dong A., Huang H.;
RT "SERRATE is a novel nuclear regulator in primary microRNA processing in
RT Arabidopsis.";
RL Plant J. 47:841-850(2006).
RN [10]
RP FUNCTION, AND INTERACTION WITH DCL1.
RX PubMed=16428603; DOI=10.1261/rna.2146906;
RA Kurihara Y., Takashi Y., Watanabe Y.;
RT "The interaction between DCL1 and HYL1 is important for efficient and
RT precise processing of pri-miRNA in plant microRNA biogenesis.";
RL RNA 12:206-212(2006).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN DSRNA-BINDING.
RX PubMed=17337628; DOI=10.1105/tpc.106.048637;
RA Wu F., Yu L., Cao W., Mao Y., Liu Z., He Y.;
RT "The N-terminal double-stranded RNA binding domains of Arabidopsis
RT HYPONASTIC LEAVES1 are sufficient for pre-microRNA processing.";
RL Plant Cell 19:914-925(2007).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=17442570; DOI=10.1016/j.cub.2007.04.005;
RA Fang Y., Spector D.L.;
RT "Identification of nuclear dicing bodies containing proteins for microRNA
RT biogenesis in living Arabidopsis plants.";
RL Curr. Biol. 17:818-823(2007).
RN [13]
RP FUNCTION.
RX PubMed=18632569; DOI=10.1073/pnas.0803356105;
RA Dong Z., Han M.-H., Fedoroff N.;
RT "The RNA-binding proteins HYL1 and SE promote accurate in vitro processing
RT of pri-miRNA by DCL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9970-9975(2008).
RN [14]
RP FUNCTION.
RX PubMed=19304749; DOI=10.1093/nar/gkp189;
RA Szarzynska B., Sobkowiak L., Pant B.D., Balazadeh S., Scheible W.R.,
RA Mueller-Roeber B., Jarmolowski A., Szweykowska-Kulinska Z.;
RT "Gene structures and processing of Arabidopsis thaliana HYL1-dependent pri-
RT miRNAs.";
RL Nucleic Acids Res. 37:3083-3093(2009).
RN [15]
RP FUNCTION.
RX PubMed=19861421; DOI=10.1261/rna.1646909;
RA Eamens A.L., Smith N.A., Curtin S.J., Wang M.B., Waterhouse P.M.;
RT "The Arabidopsis thaliana double-stranded RNA binding protein DRB1 directs
RT guide strand selection from microRNA duplexes.";
RL RNA 15:2219-2235(2009).
RN [16]
RP INTERACTION WITH RCF3; RS40 AND RS41, AND SUBCELLULAR LOCATION.
RX PubMed=26227967; DOI=10.1093/nar/gkv751;
RA Chen T., Cui P., Xiong L.;
RT "The RNA-binding protein HOS5 and serine/arginine-rich proteins RS40 and
RT RS41 participate in miRNA biogenesis in Arabidopsis.";
RL Nucleic Acids Res. 43:8283-8298(2015).
RN [17]
RP STRUCTURE BY NMR OF 1-170, FUNCTION, AND DOMAIN DSRNA-BINDING.
RX PubMed=20735118; DOI=10.1021/bi100672x;
RA Rasia R.M., Mateos J., Bologna N.G., Burdisso P., Imbert L., Palatnik J.F.,
RA Boisbouvier J.;
RT "Structure and RNA interactions of the plant MicroRNA processing-associated
RT protein HYL1.";
RL Biochemistry 49:8237-8239(2010).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 15-172 IN COMPLEX WITH DSRNA,
RP FUNCTION, SUBUNIT, AND DOMAIN DSRNA-BINDING.
RX PubMed=20462493; DOI=10.1016/j.str.2010.02.006;
RA Yang S.W., Chen H.Y., Yang J., Machida S., Chua N.H., Yuan Y.A.;
RT "Structure of Arabidopsis HYPONASTIC LEAVES1 and its molecular implications
RT for miRNA processing.";
RL Structure 18:594-605(2010).
CC -!- FUNCTION: Double-stranded RNA-binding protein involved in RNA-mediated
CC post-transcriptional gene silencing (PTGS). Functions in the microRNAs
CC (miRNAs) biogenesis by assisting DICER-LIKE 1 (DCL1) in the accurate
CC processing from primary miRNAs (pri-miRNAs) to miRNAs in the nucleus.
CC Forms a complex with SERRATE (SE) and DCL1 to promote accurate
CC processing of pri-miRNAs by DCL1. Binds and assist DCL1 for accurate
CC processing of precursor miRNAs (pre-miRNA). Indirectly involved in the
CC production of trans-acting small interfering RNAs (ta-siRNAs) derived
CC from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in
CC the production of their initiating miRNAs. Involved with argonaute 1
CC (AGO1) in the guide strand selection from miRNA duplexes, presumably by
CC directional loading of the miRNA duplex (guide stand and passenger
CC strand) onto the RNA-induced silencing complex (RISC) for passenger
CC strand degradation. Does not participate in sense transgene-induced
CC post-transcriptional gene silencing (S-PTGS). Involved in several plant
CC development aspects and response to hormones through its role in miRNAs
CC processing. {ECO:0000269|PubMed:11148283, ECO:0000269|PubMed:14722360,
CC ECO:0000269|PubMed:14972688, ECO:0000269|PubMed:15821876,
CC ECO:0000269|PubMed:16428603, ECO:0000269|PubMed:16889646,
CC ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:18632569,
CC ECO:0000269|PubMed:19304749, ECO:0000269|PubMed:19861421,
CC ECO:0000269|PubMed:20462493, ECO:0000269|PubMed:20735118}.
CC -!- SUBUNIT: Homodimer. Heterodimer with DRB2, DRB4 or DRB5. Interacts with
CC SE and DCL1 (PubMed:15821876, PubMed:16428603, PubMed:16889646,
CC PubMed:20462493). Interacts with RCF3, RS40 and RS41 (PubMed:26227967).
CC {ECO:0000269|PubMed:15821876, ECO:0000269|PubMed:16428603,
CC ECO:0000269|PubMed:16889646, ECO:0000269|PubMed:20462493,
CC ECO:0000269|PubMed:26227967}.
CC -!- INTERACTION:
CC O04492; Q3EBC8: At3g03300; NbExp=2; IntAct=EBI-632620, EBI-2464030;
CC O04492; Q9M2H8: At3g58380; NbExp=3; IntAct=EBI-632620, EBI-4429615;
CC O04492; A0A178UTG1: AXX17_At4g22700; NbExp=3; IntAct=EBI-632620, EBI-25521002;
CC O04492; Q9SP32: DCL1; NbExp=3; IntAct=EBI-632620, EBI-632627;
CC O04492; O04492: DRB1; NbExp=5; IntAct=EBI-632620, EBI-632620;
CC O04492; Q8GY79: DRB5; NbExp=7; IntAct=EBI-632620, EBI-632672;
CC O04492; Q9LPT6: OTU2; NbExp=3; IntAct=EBI-632620, EBI-20796120;
CC O04492; Q9LJ97: RAB28; NbExp=3; IntAct=EBI-632620, EBI-25520978;
CC O04492; Q9ZVD0: SE; NbExp=7; IntAct=EBI-632620, EBI-6553299;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14722360,
CC ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:17442570}. Nucleus
CC speckle {ECO:0000269|PubMed:26227967}. Note=Localizes to nuclear dicing
CC body (also named D body), a nuclear body distributed throughout the
CC nucleoplasm and involved in miRNA processing.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O04492-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O04492-2; Sequence=VSP_040613;
CC -!- TISSUE SPECIFICITY: Expressed in rosette and cauline leaves, stems,
CC roots, flowers and siliques. {ECO:0000269|PubMed:11148283,
CC ECO:0000269|PubMed:16889646}.
CC -!- INDUCTION: By abscisic acid (ABA). {ECO:0000269|PubMed:11148283}.
CC -!- DOMAIN: The dsRNA binding domains (dsRBDs) 1 and 2 are sufficient for
CC the function in miRNA precursors processing and mature miRNA
CC generation. {ECO:0000269|PubMed:17337628, ECO:0000269|PubMed:20462493,
CC ECO:0000269|PubMed:20735118}.
CC -!- DISRUPTION PHENOTYPE: Short plant, delayed flowering, leaf hyponasty,
CC reduced fertility, decreased rate of root growth, altered root
CC gravitropic response, decreased sensitivity to auxin and cytokinin and
CC hypersensitivity to abscisic acid (ABA). Reduction of several miRNA
CC accumulation. {ECO:0000269|PubMed:11148283,
CC ECO:0000269|PubMed:14972688, ECO:0000269|PubMed:16889646}.
CC -!- MISCELLANEOUS: Plants overexpressing HYL1 show decreased stability of
CC transcripts targeted by miRNAs.
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DR EMBL; AF276440; AAG49890.1; -; mRNA.
DR EMBL; AC000132; AAB60726.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28481.1; -; Genomic_DNA.
DR EMBL; AY054631; AAK96822.1; -; mRNA.
DR EMBL; AY081525; AAM10087.1; -; mRNA.
DR EMBL; AK319123; BAH57238.1; -; mRNA.
DR PIR; H86230; H86230.
DR RefSeq; NP_563850.1; NM_100842.4. [O04492-1]
DR PDB; 2L2M; NMR; -; A=97-170.
DR PDB; 2L2N; NMR; -; A=1-100.
DR PDB; 3ADG; X-ray; 1.70 A; A=15-84.
DR PDB; 3ADI; X-ray; 3.20 A; A/B/C=15-84.
DR PDB; 3ADJ; X-ray; 3.00 A; A=100-172.
DR PDBsum; 2L2M; -.
DR PDBsum; 2L2N; -.
DR PDBsum; 3ADG; -.
DR PDBsum; 3ADI; -.
DR PDBsum; 3ADJ; -.
DR AlphaFoldDB; O04492; -.
DR BMRB; O04492; -.
DR SMR; O04492; -.
DR BioGRID; 22739; 23.
DR DIP; DIP-33453N; -.
DR IntAct; O04492; 10.
DR STRING; 3702.AT1G09700.1; -.
DR PaxDb; O04492; -.
DR PRIDE; O04492; -.
DR ProteomicsDB; 241257; -. [O04492-1]
DR EnsemblPlants; AT1G09700.1; AT1G09700.1; AT1G09700. [O04492-1]
DR GeneID; 837498; -.
DR Gramene; AT1G09700.1; AT1G09700.1; AT1G09700. [O04492-1]
DR KEGG; ath:AT1G09700; -.
DR Araport; AT1G09700; -.
DR TAIR; locus:2024407; AT1G09700.
DR eggNOG; ENOG502QV9N; Eukaryota.
DR HOGENOM; CLU_054279_0_0_1; -.
DR InParanoid; O04492; -.
DR OrthoDB; 491376at2759; -.
DR EvolutionaryTrace; O04492; -.
DR PRO; PR:O04492; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O04492; baseline and differential.
DR Genevisible; O04492; AT.
DR GO; GO:0010445; C:nuclear dicing body; IDA:TAIR.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0003725; F:double-stranded RNA binding; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0035198; F:miRNA binding; IDA:TAIR.
DR GO; GO:0004525; F:ribonuclease III activity; IBA:GO_Central.
DR GO; GO:0010589; P:leaf proximal/distal pattern formation; IMP:TAIR.
DR GO; GO:0010305; P:leaf vascular tissue pattern formation; IMP:TAIR.
DR GO; GO:0035196; P:miRNA processing; IMP:TAIR.
DR GO; GO:0035279; P:miRNA-mediated gene silencing by mRNA destabilization; IMP:TAIR.
DR GO; GO:0031054; P:pre-miRNA processing; IMP:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IMP:TAIR.
DR GO; GO:0009733; P:response to auxin; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR GO; GO:0006396; P:RNA processing; IBA:GO_Central.
DR GO; GO:0006364; P:rRNA processing; IEA:InterPro.
DR GO; GO:0010267; P:ta-siRNA processing; IMP:TAIR.
DR CDD; cd19907; DSRM_AtDRB-like_rpt1; 1.
DR CDD; cd19908; DSRM_AtDRB-like_rpt2; 1.
DR InterPro; IPR044450; AtDRB-like_DSRM_1.
DR InterPro; IPR044451; AtDRB-like_DSRM_2.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR011907; RNase_III.
DR PANTHER; PTHR11207; PTHR11207; 1.
DR Pfam; PF00035; dsrm; 2.
DR SMART; SM00358; DSRM; 2.
DR PROSITE; PS50137; DS_RBD; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Nucleus; Reference proteome; Repeat;
KW RNA-binding; RNA-mediated gene silencing.
FT CHAIN 1..419
FT /note="Double-stranded RNA-binding protein 1"
FT /id="PRO_0000404652"
FT DOMAIN 15..84
FT /note="DRBM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT DOMAIN 101..170
FT /note="DRBM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00266"
FT REPEAT 247..274
FT /note="1"
FT REPEAT 275..302
FT /note="2"
FT REPEAT 303..330
FT /note="3"
FT REPEAT 331..358
FT /note="4"
FT REPEAT 359..386
FT /note="5"
FT REPEAT 387..414
FT /note="6"
FT REGION 247..414
FT /note="6 X 28 AA repeats of E-K-I-E-T-T-P-N-L-E-[PS]-[PS]-
FT S-C-M-[NS]-G-L-K-E-A-A-F-G-S-V-E-T"
FT MOTIF 207..222
FT /note="Bipartite nuclear localization"
FT VAR_SEQ 72..87
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:19423640"
FT /id="VSP_040613"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3ADG"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:3ADG"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2L2N"
FT STRAND 46..53
FT /evidence="ECO:0007829|PDB:3ADG"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:3ADG"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3ADG"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:3ADG"
FT HELIX 100..111
FT /evidence="ECO:0007829|PDB:3ADJ"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:3ADJ"
FT STRAND 119..126
FT /evidence="ECO:0007829|PDB:3ADJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:3ADJ"
FT STRAND 132..140
FT /evidence="ECO:0007829|PDB:3ADJ"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3ADJ"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:3ADJ"
FT HELIX 153..169
FT /evidence="ECO:0007829|PDB:3ADJ"
SQ SEQUENCE 419 AA; 45547 MW; FDBE165679537DFB CRC64;
MTSTDVSSGV SNCYVFKSRL QEYAQKYKLP TPVYEIVKEG PSHKSLFQST VILDGVRYNS
LPGFFNRKAA EQSAAEVALR ELAKSSELSQ CVSQPVHETG LCKNLLQEYA QKMNYAIPLY
QCQKVETLGR VTQFTCTVEI GGIKYTGAAT RTKKDAEISA GRTALLAIQS DTKNNLANYN
TQLTVLPCEK KTIQAAIPLK ETVKTLKARK AQFKKKAQKG KRTVAKNPED IIIPPQPTDH
CQNDQSEKIE TTPNLEPSSC MNGLKEAAFG SVETEKIETT PNLEPPSCMN GLKEAAFGSV
ETEKIETTPN LEPPSCMNGL KEAAFGSVET EKIETTPNLE PSSCMNGLKE AAFGSVETEK
IETTPNLEPP SCMNGLKEAA FGSVETEKIE TTPNLESSSC MSGLKEAAFG SVETEASHA
