MTF2_MOUSE
ID MTF2_MOUSE Reviewed; 593 AA.
AC Q02395; Q05C61; Q569Z8; Q6PG89; Q8BGP9; Q8BSJ7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Metal-response element-binding transcription factor 2;
DE AltName: Full=Metal regulatory transcription factor 2;
DE AltName: Full=Metal-response element DNA-binding protein M96;
DE AltName: Full=Polycomb-like protein 2;
DE Short=mPCl2;
DE AltName: Full=Zinc-regulated factor 1;
DE Short=ZiRF1;
GN Name=Mtf2; Synonyms=Pcl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Egg, Testis, and Wolffian duct;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and NMRI; TISSUE=Head, Mammary tumor, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-476 (ISOFORM 2), AND FUNCTION.
RC TISSUE=Lymphoma;
RX PubMed=7772254; DOI=10.1089/dna.1994.13.731;
RA Inouye C., Remondelli P., Karin M., Elledge S.;
RT "Isolation of a cDNA encoding a metal response element binding protein
RT using a novel expression cloning procedure: the one hybrid system.";
RL DNA Cell Biol. 13:731-742(1994).
RN [4]
RP FUNCTION.
RX PubMed=9173905; DOI=10.1042/bj3230079;
RA Remondelli P., Leone A.;
RT "Interactions of the zinc-regulated factor (ZiRF1) with the mouse
RT metallothionein Ia promoter.";
RL Biochem. J. 323:79-85(1997).
RN [5]
RP FUNCTION, AND ASSOCIATION WITH THE PRC2 COMPLEX.
RX PubMed=20144788; DOI=10.1016/j.stem.2009.12.014;
RA Walker E., Chang W.Y., Hunkapiller J., Cagney G., Garcha K., Torchia J.,
RA Krogan N.J., Reiter J.F., Stanford W.L.;
RT "Polycomb-like 2 associates with PRC2 and regulates transcriptional
RT networks during mouse embryonic stem cell self-renewal and
RT differentiation.";
RL Cell Stem Cell 6:153-166(2010).
RN [6]
RP FUNCTION, ASSOCIATION WITH THE PRC2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21367819; DOI=10.1242/dev.053652;
RA Casanova M., Preissner T., Cerase A., Poot R., Yamada D., Li X.,
RA Appanah R., Bezstarosti K., Demmers J., Koseki H., Brockdorff N.;
RT "Polycomblike 2 facilitates the recruitment of PRC2 Polycomb group
RT complexes to the inactive X chromosome and to target loci in embryonic stem
RT cells.";
RL Development 138:1471-1482(2011).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21059868; DOI=10.1128/mcb.00259-10;
RA Li X., Isono K., Yamada D., Endo T.A., Endoh M., Shinga J.,
RA Mizutani-Koseki Y., Otte A.P., Casanova M., Kitamura H., Kamijo T.,
RA Sharif J., Ohara O., Toyada T., Bernstein B.E., Brockdorff N., Koseki H.;
RT "Mammalian polycomb-like Pcl2/Mtf2 is a novel regulatory component of PRC2
RT that can differentially modulate polycomb activity both at the Hox gene
RT cluster and at Cdkn2a genes.";
RL Mol. Cell. Biol. 31:351-364(2011).
RN [8]
RP FUNCTION, AND H3K36ME3-BINDING.
RX PubMed=23104054; DOI=10.1038/nsmb.2434;
RA Ballare C., Lange M., Lapinaite A., Martin G.M., Morey L., Pascual G.,
RA Liefke R., Simon B., Shi Y., Gozani O., Carlomagno T., Benitah S.A.,
RA Di Croce L.;
RT "Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb
RT activity.";
RL Nat. Struct. Mol. Biol. 19:1257-1265(2012).
RN [9]
RP ASSOCIATION WITH THE PRC2 COMPLEX.
RX PubMed=22438827; DOI=10.1371/journal.pgen.1002576;
RA Hunkapiller J., Shen Y., Diaz A., Cagney G., McCleary D.,
RA Ramalho-Santos M., Krogan N., Ren B., Song J.S., Reiter J.F.;
RT "Polycomb-like 3 promotes polycomb repressive complex 2 binding to CpG
RT islands and embryonic stem cell self-renewal.";
RL PLoS Genet. 8:E1002576-E1002576(2012).
RN [10]
RP STRUCTURE BY NMR OF 40-98 AND 104-162.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the tudor domain of metal-response element-binding
RT transcription factor 2.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Polycomb group (PcG) protein that specifically binds histone
CC H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex,
CC thus enhancing PRC2 H3K27me3 methylation activity (PubMed:20144788,
CC PubMed:21367819, PubMed:21059868, PubMed:23104054, PubMed:22438827).
CC Regulates the transcriptional networks during embryonic stem cell self-
CC renewal and differentiation (PubMed:20144788). Promotes recruitment of
CC the PRC2 complex to the inactive X chromosome in differentiating XX ES
CC cells and PRC2 recruitment to target genes in undifferentiated ES cells
CC (PubMed:21367819). Required to repress Hox genes by enhancing H3K27me3
CC methylation of the PRC2 complex (PubMed:21059868). In some conditions
CC may act as an inhibitor of PRC2 activity: able to activate the CDKN2A
CC gene and promote cellular senescence by suppressing the catalytic
CC activity of the PRC2 complex locally (PubMed:21059868). Binds to the
CC metal-regulating-element (MRE) of MT1A gene promoter (PubMed:7772254).
CC {ECO:0000269|PubMed:20144788, ECO:0000269|PubMed:21059868,
CC ECO:0000269|PubMed:21367819, ECO:0000269|PubMed:22438827,
CC ECO:0000269|PubMed:23104054, ECO:0000269|PubMed:7772254}.
CC -!- SUBUNIT: Associates with the PRC2 complex, which consists of the core
CC components EED, EZH1 or EZH2, SUZ12, and RBBP4, and various
CC combinations of accessory subunits including AEBP2, JARID2, PHF19, MTF2
CC and EPOP (PubMed:21367819, PubMed:22438827). Forms a dimeric PRC2.1
CC (class 1, PRC-PCL) complex consisting of at least SUZ12, RBBP4, and
CC PHF19 or MTF2; PHF19 and MTF2 stabilize the dimeric structure which
CC enhances PRC2 interaction with chromatin (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y483, ECO:0000269|PubMed:21367819,
CC ECO:0000269|PubMed:22438827}.
CC -!- INTERACTION:
CC Q02395; Q921E6: Eed; NbExp=3; IntAct=EBI-2531578, EBI-904301;
CC Q02395; P70351: Ezh1; NbExp=3; IntAct=EBI-2531578, EBI-2531737;
CC Q02395; Q61188: Ezh2; NbExp=4; IntAct=EBI-2531578, EBI-904311;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21367819}.
CC Note=Localizes to chromatin as part of the PRC2 complex.
CC {ECO:0000269|PubMed:21367819}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q02395-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q02395-2; Sequence=VSP_016240;
CC -!- DOMAIN: The Tudor domain recognizes and binds H3K36me3.
CC {ECO:0000269|PubMed:23104054}.
CC -!- DISRUPTION PHENOTYPE: Mice survive to birth; however, most of them die
CC before weaning. Axial skeletal alterations that are characteristic of
CC posterior transformations are observed: ectopic ribs that associate
CC with the seventh cervical vertebra (C7) are frequently observed.
CC Consistent with this malformation, sternums are shifted anteriorly. The
CC odontoid process, which is normally a characteristic of the second
CC cervical vertebra (C2), is frequently associated with the first
CC cervical vertebra (C1). {ECO:0000269|PubMed:21059868}.
CC -!- SIMILARITY: Belongs to the Polycomblike family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH24889.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH29076.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AK032798; BAC28027.1; -; mRNA.
DR EMBL; AK032819; BAC28039.1; -; mRNA.
DR EMBL; AK031409; BAC27390.1; -; mRNA.
DR EMBL; AK139685; BAE24103.1; -; mRNA.
DR EMBL; BC057163; AAH57163.1; -; mRNA.
DR EMBL; BC092237; AAH92237.1; -; mRNA.
DR EMBL; BC100340; AAI00341.1; -; mRNA.
DR EMBL; BC024889; AAH24889.1; ALT_SEQ; mRNA.
DR EMBL; BC029076; AAH29076.1; ALT_SEQ; mRNA.
DR EMBL; S78454; AAC34714.1; -; mRNA.
DR CCDS; CCDS39201.1; -. [Q02395-1]
DR RefSeq; NP_001240806.1; NM_001253877.1. [Q02395-2]
DR RefSeq; NP_001240807.1; NM_001253878.1. [Q02395-2]
DR RefSeq; NP_001240808.1; NM_001253879.1. [Q02395-2]
DR RefSeq; NP_001240809.1; NM_001253880.1. [Q02395-2]
DR RefSeq; NP_038855.2; NM_013827.3. [Q02395-1]
DR RefSeq; XP_011247718.1; XM_011249416.2. [Q02395-2]
DR RefSeq; XP_017176193.1; XM_017320704.1.
DR RefSeq; XP_017176194.1; XM_017320705.1.
DR PDB; 2EQJ; NMR; -; A=40-98.
DR PDB; 2YT5; NMR; -; A=104-162.
DR PDBsum; 2EQJ; -.
DR PDBsum; 2YT5; -.
DR AlphaFoldDB; Q02395; -.
DR SMR; Q02395; -.
DR BioGRID; 201592; 15.
DR DIP; DIP-56991N; -.
DR IntAct; Q02395; 11.
DR STRING; 10090.ENSMUSP00000080278; -.
DR iPTMnet; Q02395; -.
DR PhosphoSitePlus; Q02395; -.
DR EPD; Q02395; -.
DR jPOST; Q02395; -.
DR MaxQB; Q02395; -.
DR PaxDb; Q02395; -.
DR PeptideAtlas; Q02395; -.
DR PRIDE; Q02395; -.
DR ProteomicsDB; 291431; -. [Q02395-1]
DR ProteomicsDB; 291432; -. [Q02395-2]
DR Antibodypedia; 19938; 186 antibodies from 29 providers.
DR DNASU; 17765; -.
DR Ensembl; ENSMUST00000081567; ENSMUSP00000080278; ENSMUSG00000029267. [Q02395-1]
DR GeneID; 17765; -.
DR KEGG; mmu:17765; -.
DR UCSC; uc008ynj.2; mouse. [Q02395-1]
DR CTD; 22823; -.
DR MGI; MGI:105050; Mtf2.
DR VEuPathDB; HostDB:ENSMUSG00000029267; -.
DR eggNOG; KOG4323; Eukaryota.
DR GeneTree; ENSGT00950000183180; -.
DR InParanoid; Q02395; -.
DR OMA; IDRDKHR; -.
DR OrthoDB; 281828at2759; -.
DR PhylomeDB; Q02395; -.
DR TreeFam; TF106420; -.
DR Reactome; R-MMU-212300; PRC2 methylates histones and DNA.
DR BioGRID-ORCS; 17765; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Mtf2; mouse.
DR EvolutionaryTrace; Q02395; -.
DR PRO; PR:Q02395; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q02395; protein.
DR Bgee; ENSMUSG00000029267; Expressed in otic placode and 277 other tissues.
DR ExpressionAtlas; Q02395; baseline and differential.
DR Genevisible; Q02395; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IC:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0001222; F:transcription corepressor binding; ISO:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0006325; P:chromatin organization; IBA:GO_Central.
DR GO; GO:0061086; P:negative regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0061087; P:positive regulation of histone H3-K27 methylation; IMP:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0007379; P:segment specification; IMP:UniProtKB.
DR GO; GO:0048863; P:stem cell differentiation; IMP:UniProtKB.
DR GO; GO:0019827; P:stem cell population maintenance; IMP:UniProtKB.
DR CDD; cd15578; PHD1_MTF2; 1.
DR CDD; cd15580; PHD2_MTF2; 1.
DR CDD; cd04508; TUDOR; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR040477; KDM4_Tudor_2.
DR InterPro; IPR025894; Mtf2_C_dom.
DR InterPro; IPR042014; MTF2_PHD1.
DR InterPro; IPR042015; MTF2_PHD2.
DR InterPro; IPR002999; Tudor.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF14061; Mtf2_C; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF18104; Tudor_2; 1.
DR SMART; SM00249; PHD; 2.
DR SMART; SM00333; TUDOR; 1.
DR SUPFAM; SSF57903; SSF57903; 2.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..593
FT /note="Metal-response element-binding transcription factor
FT 2"
FT /id="PRO_0000059318"
FT DOMAIN 44..101
FT /note="Tudor"
FT ZN_FING 102..157
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 201..255
FT /note="PHD-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 444..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 444..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT MOD_RES 452
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT CROSSLNK 360
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT CROSSLNK 522
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9Y483"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:7772254"
FT /id="VSP_016240"
FT CONFLICT 200..201
FT /note="QQ -> PE (in Ref. 3; AAC34714)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="Missing (in Ref. 3; AAC34714)"
FT /evidence="ECO:0000305"
FT CONFLICT 394
FT /note="E -> K (in Ref. 2; AAH57163)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="G -> K (in Ref. 2; AAH57163)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="D -> G (in Ref. 1; BAC28027)"
FT /evidence="ECO:0000305"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:2EQJ"
FT STRAND 61..70
FT /evidence="ECO:0007829|PDB:2EQJ"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:2EQJ"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:2EQJ"
FT TURN 81..83
FT /evidence="ECO:0007829|PDB:2EQJ"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:2EQJ"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:2EQJ"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:2YT5"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:2YT5"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:2YT5"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:2YT5"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:2YT5"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2YT5"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:2YT5"
FT HELIX 152..156
FT /evidence="ECO:0007829|PDB:2YT5"
SQ SEQUENCE 593 AA; 66924 MW; C595438196DC3E0F CRC64;
MRDSTGAGNS LVHKRSPLRR NQKTSASLNK LSLQDGHKAK KPACKFEEGQ DVLARWSDGL
FYLGTIKKIN ILKQSCFIIF EDSSKSWVLW KDIQTGATGS GEMVCTICQE EYSEAPNEMV
ICDKCGQGYH QLCHTPHIDS SVIDSDEKWL CRQCVFATTT KRGGALKKGP NAKALQVMKQ
TLPYSVADLE WDAGHKTNVQ QCYCYCGGPG DWYLKMLQCC KCKQWFHEAC VQCLQKPMLF
GDRFYTFICS VCSSGPEYLK RLPLQWVDIA HLCLYNLSVI HKKKYFDSEL ELMTYINENW
DRLHPGELAD TPKSERYEHV LEALNDYKTM FMSGKEIKKK KHLFGLRIRV PPVPPNVAFK
AEKEPEGTSH EFKIKGRKAS KPTSDSREVS NGIEKKGKKK SVGRPPGPYT RKMIQKTAEL
PLDKESVSEN PTLDLPCSIG RTEGIAHSSN TSDVDLTGAS SANETTSASI SRHCGLSDSR
KRTRTGRSWP AAIPHLRRRR GRLPRRALQT QNSEVVKDDE GKEDYQFEEL NTEILNNLAD
QELQLNHLKN SITSYFGAAG RIACGEKYRV LARRVTLDGK VQYLVEWEGA TAS
