YTDC1_RAT
ID YTDC1_RAT Reviewed; 738 AA.
AC Q9QY02; G3V690; O54729;
DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-FEB-2014, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=YTH domain-containing protein 1;
DE AltName: Full=RA301-binding protein;
DE AltName: Full=Splicing factor YT521 {ECO:0000303|PubMed:9473574};
GN Name=Ythdc1; Synonyms=Yt521 {ECO:0000303|PubMed:9473574};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=9473574; DOI=10.1016/s0169-328x(97)00262-3;
RA Imai Y., Matsuo N., Ogawa S., Tohyama M., Takagi T.;
RT "Cloning of a gene, YT521, for a novel RNA splicing-related protein induced
RT by hypoxia/reoxygenation.";
RL Brain Res. Mol. Brain Res. 53:33-40(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP PHOSPHORYLATION, AND INTERACTION WITH KHDRBS1; SRSF1; SRSF2 AND TRA2B.
RX PubMed=10564280; DOI=10.1091/mbc.10.11.3909;
RA Hartmann A.M., Nayler O., Schwaiger F.W., Obermeier A., Stamm S.;
RT "The interaction and colocalization of Sam68 with the splicing-associated
RT factor YT521-B in nuclear dots is regulated by the Src family kinase
RT p59fyn.";
RL Mol. Biol. Cell 10:3909-3926(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=10973987; DOI=10.1083/jcb.150.5.949;
RA Nayler O., Hartmann A.M., Stamm S.;
RT "The ER repeat protein YT521-B localizes to a novel subnuclear
RT compartment.";
RL J. Cell Biol. 150:949-962(2000).
RN [6]
RP INTERACTION WITH KHDRBS3.
RC TISSUE=Brain;
RX PubMed=11118435; DOI=10.1074/jbc.m006851200;
RA Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A.,
RA Stamm S.;
RT "The STAR/GSG family protein rSLM-2 regulates the selection of alternative
RT splice sites.";
RL J. Biol. Chem. 276:8665-8673(2001).
RN [7]
RP INTERACTION WITH RBMX.
RX PubMed=19282290; DOI=10.1074/jbc.m901026200;
RA Heinrich B., Zhang Z., Raitskin O., Hiller M., Benderska N., Hartmann A.M.,
RA Bracco L., Elliott D., Ben-Ari S., Soreq H., Sperling J., Sperling R.,
RA Stamm S.;
RT "Heterogeneous nuclear ribonucleoprotein G regulates splice site selection
RT by binding to CC(A/C)-rich regions in pre-mRNA.";
RL J. Biol. Chem. 284:14303-14315(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35 AND SER-311, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [9] {ECO:0007744|PDB:2MTV}
RP STRUCTURE BY NMR OF 347-502, FUNCTION, AND RNA-BINDING.
RX PubMed=25389274; DOI=10.1093/nar/gku1116;
RA Theler D., Dominguez C., Blatter M., Boudet J., Allain F.H.;
RT "Solution structure of the YTH domain in complex with N6-methyladenosine
RT RNA: a reader of methylated RNA.";
RL Nucleic Acids Res. 42:13911-13919(2014).
CC -!- FUNCTION: Regulator of alternative splicing that specifically
CC recognizes and binds N6-methyladenosine (m6A)-containing RNAs
CC (PubMed:25389274). M6A is a modification present at internal sites of
CC mRNAs and some non-coding RNAs and plays a role in the efficiency of
CC mRNA splicing, processing and stability (PubMed:25389274). Acts as a
CC key regulator of exon-inclusion or exon-skipping during alternative
CC splicing via interaction with mRNA splicing factors SRSF3 and SRSF10
CC (By similarity). Specifically binds m6A-containing mRNAs and promotes
CC recruitment of SRSF3 to its mRNA-binding elements adjacent to m6A
CC sites, leading to exon-inclusion during alternative splicing (By
CC similarity). In contrast, interaction with SRSF3 prevents interaction
CC with SRSF10, a splicing factor that promotes exon skipping: this
CC prevents SRSF10 from binding to its mRNA-binding sites close to m6A-
CC containing regions, leading to inhibit exon skipping during alternative
CC splicing (By similarity). May also regulate alternative splice site
CC selection (PubMed:10564280, PubMed:9473574). Also involved in nuclear
CC export of m6A-containing mRNAs via interaction with SRSF3: interaction
CC with SRSF3 facilitates m6A-containing mRNA-binding to both SRSF3 and
CC NXF1, promoting mRNA nuclear export (By similarity). Involved in S-
CC adenosyl-L-methionine homeostasis by regulating expression of MAT2A
CC transcripts, probably by binding m6A-containing MAT2A mRNAs (By
CC similarity). Also recognizes and binds m6A on other RNA molecules (By
CC similarity). Involved in random X inactivation mediated by Xist RNA:
CC recognizes and binds m6A-containing Xist and promotes transcription
CC repression activity of Xist (By similarity). Also recognizes and binds
CC m6A-containing single-stranded DNA (By similarity). Involved in
CC germline development: required for spermatogonial development in males
CC and oocyte growth and maturation in females, probably via its role in
CC alternative splicing (By similarity). {ECO:0000250|UniProtKB:E9Q5K9,
CC ECO:0000250|UniProtKB:Q96MU7, ECO:0000269|PubMed:10564280,
CC ECO:0000269|PubMed:25389274, ECO:0000269|PubMed:9473574}.
CC -!- SUBUNIT: Interacts with SRSF1 (PubMed:10564280). Interacts with SRSF2
CC (PubMed:10564280). Interacts with SRSF3 (By similarity). Interacts with
CC SRSF7 (By similarity). Interacts with SRSF10 (By similarity). Interacts
CC with CPSF6 (By similarity). Interacts with KHDRBS1/SAM68
CC (PubMed:10564280). Interacts with TRA2B (PubMed:10564280). Interacts
CC with KHDRBS3 (PubMed:11118435). Interacts with EMD (By similarity).
CC Interacts with RBMX (PubMed:19282290). Interacts with ZCCHC8 (By
CC similarity). {ECO:0000250|UniProtKB:E9Q5K9,
CC ECO:0000250|UniProtKB:Q96MU7, ECO:0000269|PubMed:10564280,
CC ECO:0000269|PubMed:11118435, ECO:0000269|PubMed:19282290}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10973987}. Nucleus
CC speckle {ECO:0000250|UniProtKB:Q96MU7}. Note=Localizes to a novel
CC subnuclear structure, the YT bodies. {ECO:0000269|PubMed:10973987}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=YT521-B {ECO:0000303|PubMed:10564280};
CC IsoId=Q9QY02-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QY02-2; Sequence=VSP_006819, VSP_006820;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10564280}.
CC -!- DOMAIN: The YTH domain mediates RNA-binding.
CC {ECO:0000250|UniProtKB:Q96MU7}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000269|PubMed:10564280}.
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DR EMBL; D78303; BAA23885.1; -; mRNA.
DR EMBL; AF144731; AAD55973.1; -; mRNA.
DR EMBL; AABR06078005; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473981; EDL89830.1; -; Genomic_DNA.
DR RefSeq; NP_596914.1; NM_133423.1.
DR RefSeq; XP_006250870.1; XM_006250808.3. [Q9QY02-2]
DR PDB; 2MTV; NMR; -; A=347-502.
DR PDBsum; 2MTV; -.
DR AlphaFoldDB; Q9QY02; -.
DR BMRB; Q9QY02; -.
DR SMR; Q9QY02; -.
DR BioGRID; 251046; 1.
DR STRING; 10116.ENSRNOP00000002736; -.
DR CarbonylDB; Q9QY02; -.
DR iPTMnet; Q9QY02; -.
DR PhosphoSitePlus; Q9QY02; -.
DR PaxDb; Q9QY02; -.
DR Ensembl; ENSRNOT00000110796; ENSRNOP00000080807; ENSRNOG00000001996. [Q9QY02-2]
DR Ensembl; ENSRNOT00000119155; ENSRNOP00000095873; ENSRNOG00000001996. [Q9QY02-1]
DR GeneID; 170956; -.
DR KEGG; rno:170956; -.
DR UCSC; RGD:621706; rat. [Q9QY02-1]
DR CTD; 91746; -.
DR RGD; 621706; Ythdc1.
DR eggNOG; KOG1902; Eukaryota.
DR GeneTree; ENSGT00940000155803; -.
DR HOGENOM; CLU_029591_0_0_1; -.
DR InParanoid; Q9QY02; -.
DR OMA; CHTSTVY; -.
DR OrthoDB; 1523119at2759; -.
DR TreeFam; TF325590; -.
DR PRO; PR:Q9QY02; -.
DR Proteomes; UP000002494; Chromosome 14.
DR Proteomes; UP000234681; Chromosome 14.
DR Bgee; ENSRNOG00000001996; Expressed in thymus and 20 other tissues.
DR Genevisible; Q9QY02; RN.
DR GO; GO:0016604; C:nuclear body; IDA:RGD.
DR GO; GO:0016607; C:nuclear speck; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:1990247; F:N6-methyladenosine-containing RNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; ISS:UniProtKB.
DR GO; GO:0009048; P:dosage compensation by inactivation of X chromosome; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; ISO:RGD.
DR GO; GO:0110104; P:mRNA alternative polyadenylation; ISO:RGD.
DR GO; GO:0006406; P:mRNA export from nucleus; ISS:UniProtKB.
DR GO; GO:0006376; P:mRNA splice site selection; ISS:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IDA:RGD.
DR GO; GO:0010608; P:post-transcriptional regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0048160; P:primary follicle stage; ISO:RGD.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; ISO:RGD.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISO:RGD.
DR InterPro; IPR007275; YTH_domain.
DR InterPro; IPR045168; YTH_prot.
DR PANTHER; PTHR12357; PTHR12357; 1.
DR Pfam; PF04146; YTH; 2.
DR PROSITE; PS50882; YTH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Isopeptide bond; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; RNA-binding;
KW Ubl conjugation.
FT CHAIN 1..738
FT /note="YTH domain-containing protein 1"
FT /id="PRO_0000223077"
FT DOMAIN 358..495
FT /note="YTH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00225"
FT REGION 1..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 512..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 680..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..63
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..91
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..197
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..259
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..648
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 364..366
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q9Y5A9"
FT BINDING 380
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT BINDING 431
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT BINDING 479
FT /ligand="RNA"
FT /ligand_id="ChEBI:CHEBI:33697"
FT /ligand_part="N(6)-methyladenosine 5'-phosphate residue"
FT /ligand_part_id="ChEBI:CHEBI:74449"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 148
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 323
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT MOD_RES 548
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT CROSSLNK 96
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96MU7"
FT VAR_SEQ 328..345
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9473574"
FT /id="VSP_006819"
FT VAR_SEQ 577..584
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9473574"
FT /id="VSP_006820"
FT CONFLICT 353
FT /note="Y -> S (in Ref. 1; BAA23885 and 2; AAD55973)"
FT /evidence="ECO:0000305"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:2MTV"
FT STRAND 359..363
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:2MTV"
FT STRAND 400..405
FT /evidence="ECO:0007829|PDB:2MTV"
FT TURN 407..409
FT /evidence="ECO:0007829|PDB:2MTV"
FT STRAND 411..418
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:2MTV"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:2MTV"
FT TURN 467..470
FT /evidence="ECO:0007829|PDB:2MTV"
FT STRAND 481..483
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 485..494
FT /evidence="ECO:0007829|PDB:2MTV"
FT HELIX 499..501
FT /evidence="ECO:0007829|PDB:2MTV"
SQ SEQUENCE 738 AA; 85902 MW; 9FC68314E029FA98 CRC64;
MAADSREEKD GELNVLDDIL TEVPEQDDEL YNPESEQDKN EKKGSKRKSE RMESIDTKRQ
KPSIHSRQLI SKPLSSSVSN NKRIVSTKGK SVTEYKNEEY QRSERNKRLD ADRKIRLSSS
SSREPYKSQP EKPCLRKRDS ERRAKSPTPD GSERIGLEVD RRASRSSQSS KEEGNSEEYG
SDHETGSSAS SEQGNNTENE EEGGEEDVEE DEEVDEDGDD DEEVDEDAEE EEDEEEDEEE
EDEEEEEEEE EEYEQDERDQ KEEGNDYDTR SEASDSGSES VSFTDGSVRS GSGTDGSDEK
KKERKRARGI SPIVFDRSGS SASESYAGSE KKHEKLSSSV RAVRKDQTSK LKYVLQDARF
FLIKSNNHEN VSLAKAKGVW STLPVNEKKL NLAFRSARSV ILIFSVRESG KFQGFARLSS
ESHHGGSPIH WVLPAGMSAK MLGGVFKIDW ICRRELPFTK SAHLTNPWNE HKPVKIGRDG
QEIELECGTQ LCLLFPPDES IDLYQLIHKM RHKRRMHSQP RSRGRPSRRE PVRDVGRRRP
EDYDIHNSRK KPRIDYPPEF HQRPGYLKDP RYQEVDSFTN LIPNRRFSGV RRDVFLNGSY
NDYVREFHNM GPPPPWQGMP PYPGIEQPPH HPYYQHHAPP PQAHPPYSGH HPVPHEARYR
DKRVHDYDMR VDDFLRRTQA VVSGRRSRPR ERDRERERDR PRDNRRDRER DRGRDRERER
ERICDRDRDR GERGRYRR
