ZMY11_MOUSE
ID ZMY11_MOUSE Reviewed; 602 AA.
AC Q8R5C8; G5E8Q2; Q8C155;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2012, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Zinc finger MYND domain-containing protein 11;
GN Name=Zmynd11;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 101-602.
RC STRAIN=C57BL/6J; TISSUE=Skin;
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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 154-371 IN COMPLEXES WITH HISTONE
RP 3.3 TAIL AND ZINC, FUNCTION, AND MUTAGENESIS OF ARG-168; 234-ASP--GLU-236;
RP GLU-251; ASN-266; PHE-291; TRP-294; ASP-307 AND PHE-310.
RX PubMed=24590075; DOI=10.1038/nature13045;
RA Wen H., Li Y., Xi Y., Jiang S., Stratton S., Peng D., Tanaka K., Ren Y.,
RA Xia Z., Wu J., Li B., Barton M.C., Li W., Li H., Shi X.;
RT "ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour
RT suppression.";
RL Nature 508:263-268(2014).
CC -!- FUNCTION: Chromatin reader that specifically recognizes and binds
CC histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3) and regulates RNA
CC polymerase II elongation. Does not bind other histone H3 subtypes (H3.1
CC or H3.2). Colocalizes with highly expressed genes and functions as a
CC transcription corepressor by modulating RNA polymerase II at the
CC elongation stage (PubMed:24590075). Binds non-specifically to dsDNA (By
CC similarity). Acts as a tumor-suppressor by repressing a transcriptional
CC program essential for tumor cell growth (PubMed:24590075).
CC {ECO:0000250|UniProtKB:Q15326, ECO:0000269|PubMed:24590075}.
CC -!- SUBUNIT: Homooligomer; forms homooligomers via its C-terminus.
CC Interacts with histone H3.3 trimethylated at 'Lys-36' (H3.3K36me3).
CC Interacts (via MYND-type zinc finger) with NCOR1. Interacts (via MYND-
CC type zinc finger) with MGA protein (via PXLXP motif). Interacts (via
CC MYND-type zinc finger) with EZH2. Interacts with EMSY and E2F6.
CC Interacts with PIAS1 and UBE2I (By similarity).
CC {ECO:0000250|UniProtKB:Q15326}.
CC -!- INTERACTION:
CC Q8R5C8; P84243: H3-3B; Xeno; NbExp=6; IntAct=EBI-647813, EBI-120658;
CC Q8R5C8; P68431: H3C12; Xeno; NbExp=4; IntAct=EBI-647813, EBI-79722;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q15326}.
CC Chromosome {ECO:0000250|UniProtKB:Q15326}. Note=Associates with
CC chromatin and mitotic chromosomes. {ECO:0000250|UniProtKB:Q15326}.
CC -!- DOMAIN: The PWWP domain specifically recognizes and binds histone H3.3
CC trimethylated at 'Lys-36' (H3.3K36me3) and adopts a five-bladed beta-
CC barrel fold with an extended C-terminal alpha-helix, with a conserved
CC H3.3K36me3-binding aromatic cage formed by Phe-291 and Trp-294 of the
CC beta1-beta2 loop and Phe-310 of the beta3-beta4 loop. Specific
CC recognition of H3.3 histone is mediated by the encapsulation of the
CC H3.3-specific 'Ser 31' residue in a composite pocket formed by the
CC tandem bromo-PWWP domains (PubMed:24590075).
CC {ECO:0000269|PubMed:24590075}.
CC -!- PTM: Ubiquitinated, leading to proteasomal degradation.
CC {ECO:0000250|UniProtKB:Q15326}.
CC -!- PTM: Sumoylated following its interaction with PIAS1 and UBE2I.
CC {ECO:0000250|UniProtKB:Q15326}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH22945.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC146596; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC153144; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466588; EDL32291.1; -; Genomic_DNA.
DR EMBL; CH466588; EDL32294.1; -; Genomic_DNA.
DR EMBL; BC022945; AAH22945.1; ALT_INIT; mRNA.
DR EMBL; AK028931; BAC26199.1; -; mRNA.
DR CCDS; CCDS56870.1; -.
DR RefSeq; NP_001186070.1; NM_001199141.2.
DR RefSeq; NP_001334403.1; NM_001347474.1.
DR RefSeq; NP_001334405.1; NM_001347476.1.
DR RefSeq; XP_006516569.1; XM_006516506.3.
DR PDB; 4N4G; X-ray; 1.95 A; A=154-371.
DR PDB; 4N4H; X-ray; 2.30 A; A=154-371.
DR PDB; 4N4I; X-ray; 2.00 A; A=154-371.
DR PDBsum; 4N4G; -.
DR PDBsum; 4N4H; -.
DR PDBsum; 4N4I; -.
DR AlphaFoldDB; Q8R5C8; -.
DR SMR; Q8R5C8; -.
DR BioGRID; 211523; 1.
DR DIP; DIP-49596N; -.
DR IntAct; Q8R5C8; 4.
DR STRING; 10090.ENSMUSP00000059767; -.
DR iPTMnet; Q8R5C8; -.
DR PhosphoSitePlus; Q8R5C8; -.
DR EPD; Q8R5C8; -.
DR MaxQB; Q8R5C8; -.
DR PaxDb; Q8R5C8; -.
DR PeptideAtlas; Q8R5C8; -.
DR PRIDE; Q8R5C8; -.
DR ProteomicsDB; 274998; -.
DR Antibodypedia; 9245; 259 antibodies from 30 providers.
DR DNASU; 66505; -.
DR Ensembl; ENSMUST00000110634; ENSMUSP00000106264; ENSMUSG00000021156.
DR Ensembl; ENSMUST00000110636; ENSMUSP00000106266; ENSMUSG00000021156.
DR GeneID; 66505; -.
DR KEGG; mmu:66505; -.
DR UCSC; uc007pkx.1; mouse.
DR CTD; 10771; -.
DR MGI; MGI:1913755; Zmynd11.
DR VEuPathDB; HostDB:ENSMUSG00000021156; -.
DR eggNOG; KOG3612; Eukaryota.
DR GeneTree; ENSGT00940000156942; -.
DR InParanoid; Q8R5C8; -.
DR OMA; MTRVHGM; -.
DR OrthoDB; 369818at2759; -.
DR BioGRID-ORCS; 66505; 4 hits in 75 CRISPR screens.
DR ChiTaRS; Zmynd11; mouse.
DR PRO; PR:Q8R5C8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8R5C8; protein.
DR Bgee; ENSMUSG00000021156; Expressed in ciliary body and 262 other tissues.
DR ExpressionAtlas; Q8R5C8; baseline and differential.
DR Genevisible; Q8R5C8; MM.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:UniProtKB.
DR GO; GO:0042393; F:histone binding; IPI:UniProtKB.
DR GO; GO:0035064; F:methylated histone binding; IDA:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IMP:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISO:MGI.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
DR GO; GO:0046329; P:negative regulation of JNK cascade; ISO:MGI.
DR GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:UniProtKB.
DR CDD; cd05841; BS69_related; 1.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR001487; Bromodomain.
DR InterPro; IPR036427; Bromodomain-like_sf.
DR InterPro; IPR000313; PWWP_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR035505; ZMYND8/11_PWWP.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR002893; Znf_MYND.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00439; Bromodomain; 1.
DR Pfam; PF00855; PWWP; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00293; PWWP; 1.
DR SUPFAM; SSF47370; SSF47370; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS50014; BROMODOMAIN_2; 1.
DR PROSITE; PS50812; PWWP; 1.
DR PROSITE; PS01360; ZF_MYND_1; 1.
DR PROSITE; PS50865; ZF_MYND_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bromodomain; Chromatin regulator; Chromosome; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation;
KW Tumor suppressor; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..602
FT /note="Zinc finger MYND domain-containing protein 11"
FT /id="PRO_0000211219"
FT DOMAIN 168..238
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT DOMAIN 280..331
FT /note="PWWP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00162"
FT ZN_FING 100..148
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT ZN_FING 563..598
FT /note="MYND-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT REGION 291..310
FT /note="Aromatic cage required for H3.3K36me3-specific
FT binding"
FT REGION 366..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 394..400
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 390..415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 258
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24590075,
FT ECO:0007744|PDB:4N4G, ECO:0007744|PDB:4N4I"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24590075,
FT ECO:0007744|PDB:4N4G, ECO:0007744|PDB:4N4I"
FT BINDING 277
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24590075,
FT ECO:0007744|PDB:4N4G, ECO:0007744|PDB:4N4I"
FT BINDING 281
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|PubMed:24590075,
FT ECO:0007744|PDB:4N4G, ECO:0007744|PDB:4N4I"
FT BINDING 563
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 566
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 574
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 575
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 581
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 585
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 594
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT BINDING 598
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00134"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15326"
FT CROSSLNK 366
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15326"
FT CROSSLNK 407
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15326"
FT CROSSLNK 408
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q15326"
FT MUTAGEN 168
FT /note="R->A: Impaired H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 234..236
FT /note="DSE->ASA: No effect on protein folding and histone
FT binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 251
FT /note="E->A: Impaired H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 266
FT /note="N->A: Impaired H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 291
FT /note="F->A: Abolished H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 294
FT /note="W->A: Abolished H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 307
FT /note="D->A: Impaired H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT MUTAGEN 310
FT /note="F->A: Abolished H3.3K36me3 binding."
FT /evidence="ECO:0000269|PubMed:24590075"
FT CONFLICT 371
FT /note="G -> S (in Ref. 4; BAC26199)"
FT /evidence="ECO:0000305"
FT CONFLICT 519
FT /note="S -> N (in Ref. 3; AAH22945)"
FT /evidence="ECO:0000305"
FT CONFLICT 523
FT /note="D -> E (in Ref. 3; AAH22945)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="G -> C (in Ref. 3; AAH22945)"
FT /evidence="ECO:0000305"
FT CONFLICT 531
FT /note="L -> V (in Ref. 3; AAH22945)"
FT /evidence="ECO:0000305"
FT HELIX 155..171
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:4N4I"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 198..206
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 213..231
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 236..257
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 259..267
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:4N4G"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:4N4G"
FT TURN 289..291
FT /evidence="ECO:0007829|PDB:4N4I"
FT STRAND 293..302
FT /evidence="ECO:0007829|PDB:4N4G"
FT STRAND 305..312
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 313..315
FT /evidence="ECO:0007829|PDB:4N4G"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4N4G"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4N4G"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:4N4G"
FT HELIX 341..359
FT /evidence="ECO:0007829|PDB:4N4G"
SQ SEQUENCE 602 AA; 70838 MW; 963A9EF2ABBCD3C2 CRC64;
MARLTKRRQA DTKAIQHLWA AIEIIRNQKQ IANIDRITKY MSRVHGMHPK ETTRQLSLAV
KDGLIVETLT VGCKGSKAGI EQEGYWLPGD EIDWETETHD WYCFECHLPG EVLICDLCFR
VYHSKCLSDE FRLRDSSSHW QCPVCRSIKK KHSNKQEMGT YLRFIVSRMK ERAIDLNKKG
KDSKHPMYRR LVHSAVDVPT IQEKVNEGKY RSYEEFKADA QLLLHNTVIF YGADSEQADI
ARMLYKDTCH ELDELQLCKN CFYLSNARPD NWFCYPCIPN HELVWAKMKG FGFWPAKVMQ
KEDNQVDVRF FGHHHQRAWI PSENIQDITV NVHRLHVKRS MGWKKACDEL ELHQRFLREG
RFWKSKNEDR GEEEAESSIS STSNEQLKVT QEPRAKKGRR NQSVEPKKEE PEPETEAVSS
SQEIPTMPQP IERVSVSTQT KKLSASSPRM LHRSTQTTSD GVCQSMCHDK YTKIFNDFKD
RMKSDHKRET ERVVREALEK LRSEMEEEKR QAVNKAVASL QGDMDRKGKQ LKEKCKEEFV
EEIKKLAAQH KQLISQTKKK QWCYNCEEEA MYHCCWNTSY CSIKCQQEHW HAEHKRTCRR
KR
