ZN224_HUMAN
ID ZN224_HUMAN Reviewed; 707 AA.
AC Q9NZL3; A6NFW9; P17033; Q86V10; Q8IZC8; Q9UID9; Q9Y2P6;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Zinc finger protein 224;
DE AltName: Full=Bone marrow zinc finger 2;
DE Short=BMZF-2;
DE AltName: Full=Zinc finger protein 233;
DE AltName: Full=Zinc finger protein 255;
DE AltName: Full=Zinc finger protein 27;
DE AltName: Full=Zinc finger protein KOX22;
GN Name=ZNF224; Synonyms=BMZF2, KOX22, ZNF233, ZNF255, ZNF27;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-118.
RX PubMed=12743021; DOI=10.1101/gr.963903;
RA Shannon M., Hamilton A.T., Gordon L., Branscomb E., Stubbs L.;
RT "Differential expansion of zinc-finger transcription factor loci in
RT homologous human and mouse gene clusters.";
RL Genome Res. 13:1097-1110(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS VAL-118 AND LEU-162.
RC TISSUE=Uterus;
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 [MRNA] OF 86-707, AND VARIANTS VAL-118; LEU-162 AND
RP GLU-640.
RC TISSUE=Bone marrow;
RX PubMed=10585455; DOI=10.1074/jbc.274.50.35741;
RA Han Z.-G., Zhang Q.-H., Ye M., Kan L.-X., Gu B.-W., He K.-L., Shi S.-L.,
RA Zhou J., Fu G., Mao M., Chen S.-J., Yu L., Chen Z.;
RT "Molecular cloning of six novel Kruppel-like zinc finger genes from
RT hematopoietic cells and identification of a novel transregulatory domain
RT KRNB.";
RL J. Biol. Chem. 274:35741-35748(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 86-707, VARIANTS VAL-118; LEU-162 AND
RP GLU-640, INTERACTION WITH WT1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12239212; DOI=10.1074/jbc.m205667200;
RA Lee T.H., Lwu S., Kim J., Pelletier J.;
RT "Inhibition of Wilms tumor 1 transactivation by bone marrow zinc finger 2,
RT a novel transcriptional repressor.";
RL J. Biol. Chem. 277:44826-44837(2002).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 232-287.
RC TISSUE=Lymphoid tissue;
RX PubMed=2288909;
RA Thiesen H.-J.;
RT "Multiple genes encoding zinc finger domains are expressed in human T
RT cells.";
RL New Biol. 2:363-374(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 442-707.
RA Kodoyianni V., Ge Y., Berggren W.T., Severin J., Krummel G.K., Gordon L.,
RA Shannon M., Olsen A.S., Smith L.M.;
RT "Sequence analysis of a 1Mb region in 19q13.2 containing a zinc finger gene
RT cluster.";
RL Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DEPDC1A.
RX PubMed=20587513; DOI=10.1158/0008-5472.can-10-0255;
RA Harada Y., Kanehira M., Fujisawa Y., Takata R., Shuin T., Miki T.,
RA Fujioka T., Nakamura Y., Katagiri T.;
RT "Cell-permeable peptide DEPDC1-ZNF224 interferes with transcriptional
RT repression and oncogenicity in bladder cancer cells.";
RL Cancer Res. 70:5829-5839(2010).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=23665872; DOI=10.1007/s00018-013-1359-4;
RA Wang W., Cai J., Wu Y., Hu L., Chen Z., Hu J., Chen Z., Li W., Guo M.,
RA Huang Z.;
RT "Novel activity of KRAB domain that functions to reinforce nuclear
RT localization of KRAB-containing zinc finger proteins by interacting with
RT KAP1.";
RL Cell. Mol. Life Sci. 70:3947-3958(2013).
RN [10]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-473 AND LYS-625, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [11]
RP STRUCTURE BY NMR OF 227-707.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the ZF-C2H2 domain from human zinc finger protein
RT 224.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation as a
CC transcriptional repressor. The DEPDC1A-ZNF224 complex may play a
CC critical role in bladder carcinogenesis by repressing the transcription
CC of the A20 gene, leading to transport of NF-KB protein into the
CC nucleus, resulting in suppression of apoptosis of bladder cancer cells.
CC {ECO:0000269|PubMed:20587513}.
CC -!- SUBUNIT: Interacts with WT1. Interacts with DEPDC1A.
CC {ECO:0000269|PubMed:12239212, ECO:0000269|PubMed:20587513}.
CC -!- INTERACTION:
CC Q9NZL3; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-12357267, EBI-11530605;
CC Q9NZL3; Q9NW38: FANCL; NbExp=3; IntAct=EBI-12357267, EBI-2339898;
CC Q9NZL3; P43361: MAGEA8; NbExp=3; IntAct=EBI-12357267, EBI-10182930;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12239212,
CC ECO:0000269|PubMed:20587513, ECO:0000269|PubMed:23665872}.
CC Note=Colocalizes with DEPDC1A at the nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. Mainly expressed in fetal tissues.
CC {ECO:0000269|PubMed:12239212}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AF187990; AAF04106.2; -; mRNA.
DR EMBL; AC084219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC114266; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC051902; AAH51902.1; -; mRNA.
DR EMBL; AF067164; AAD32448.1; -; mRNA.
DR EMBL; AY148489; AAN61121.1; -; mRNA.
DR EMBL; X52353; CAA36579.1; -; mRNA.
DR EMBL; AC021092; AAF24968.1; -; Genomic_DNA.
DR CCDS; CCDS33046.1; -.
DR PIR; I37962; I37962.
DR RefSeq; NP_001308574.1; NM_001321645.1.
DR RefSeq; NP_037530.2; NM_013398.3.
DR RefSeq; XP_016882750.1; XM_017027261.1.
DR PDB; 2ELY; NMR; -; A=227-259.
DR PDB; 2ELZ; NMR; -; A=647-679.
DR PDB; 2EM0; NMR; -; A=675-707.
DR PDB; 2EM6; NMR; -; A=199-231.
DR PDB; 2EM7; NMR; -; A=339-371.
DR PDB; 2EM8; NMR; -; A=423-455.
DR PDB; 2EM9; NMR; -; A=367-399.
DR PDB; 2EN1; NMR; -; A=563-595.
DR PDB; 2EN8; NMR; -; A=171-203.
DR PDB; 2ENA; NMR; -; A=311-343.
DR PDB; 2ENC; NMR; -; A=395-427.
DR PDB; 2EOQ; NMR; -; A=283-315.
DR PDB; 2EOR; NMR; -; A=255-287.
DR PDB; 2EQ4; NMR; -; A=451-483.
DR PDB; 2YSP; NMR; -; A=507-539.
DR PDB; 2YTH; NMR; -; A=479-511.
DR PDBsum; 2ELY; -.
DR PDBsum; 2ELZ; -.
DR PDBsum; 2EM0; -.
DR PDBsum; 2EM6; -.
DR PDBsum; 2EM7; -.
DR PDBsum; 2EM8; -.
DR PDBsum; 2EM9; -.
DR PDBsum; 2EN1; -.
DR PDBsum; 2EN8; -.
DR PDBsum; 2ENA; -.
DR PDBsum; 2ENC; -.
DR PDBsum; 2EOQ; -.
DR PDBsum; 2EOR; -.
DR PDBsum; 2EQ4; -.
DR PDBsum; 2YSP; -.
DR PDBsum; 2YTH; -.
DR AlphaFoldDB; Q9NZL3; -.
DR SMR; Q9NZL3; -.
DR BioGRID; 113550; 17.
DR IntAct; Q9NZL3; 12.
DR STRING; 9606.ENSP00000337368; -.
DR iPTMnet; Q9NZL3; -.
DR PhosphoSitePlus; Q9NZL3; -.
DR BioMuta; ZNF224; -.
DR DMDM; 313104253; -.
DR jPOST; Q9NZL3; -.
DR MassIVE; Q9NZL3; -.
DR MaxQB; Q9NZL3; -.
DR PaxDb; Q9NZL3; -.
DR PeptideAtlas; Q9NZL3; -.
DR PRIDE; Q9NZL3; -.
DR ProteomicsDB; 83427; -.
DR Antibodypedia; 65029; 129 antibodies from 19 providers.
DR DNASU; 7767; -.
DR Ensembl; ENST00000336976.10; ENSP00000337368.5; ENSG00000267680.6.
DR Ensembl; ENST00000684943.1; ENSP00000509045.1; ENSG00000267680.6.
DR Ensembl; ENST00000693561.1; ENSP00000508532.1; ENSG00000267680.6.
DR GeneID; 7767; -.
DR KEGG; hsa:7767; -.
DR MANE-Select; ENST00000693561.1; ENSP00000508532.1; NM_001321645.3; NP_001308574.1.
DR UCSC; uc002oyh.3; human.
DR CTD; 7767; -.
DR DisGeNET; 7767; -.
DR GeneCards; ZNF224; -.
DR HGNC; HGNC:13017; ZNF224.
DR HPA; ENSG00000267680; Low tissue specificity.
DR MIM; 194555; gene.
DR neXtProt; NX_Q9NZL3; -.
DR OpenTargets; ENSG00000267680; -.
DR PharmGKB; PA37596; -.
DR VEuPathDB; HostDB:ENSG00000267680; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160225; -.
DR HOGENOM; CLU_002678_17_1_1; -.
DR InParanoid; Q9NZL3; -.
DR OMA; VQHEMET; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9NZL3; -.
DR TreeFam; TF341885; -.
DR PathwayCommons; Q9NZL3; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9NZL3; -.
DR SIGNOR; Q9NZL3; -.
DR BioGRID-ORCS; 7767; 11 hits in 1101 CRISPR screens.
DR EvolutionaryTrace; Q9NZL3; -.
DR GeneWiki; ZNF224; -.
DR GenomeRNAi; 7767; -.
DR Pharos; Q9NZL3; Tbio.
DR PRO; PR:Q9NZL3; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9NZL3; protein.
DR Bgee; ENSG00000267680; Expressed in cerebellar hemisphere and 177 other tissues.
DR ExpressionAtlas; Q9NZL3; baseline and differential.
DR Genevisible; Q9NZL3; HS.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0017053; C:transcription repressor complex; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 14.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 18.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Isopeptide bond; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..707
FT /note="Zinc finger protein 224"
FT /id="PRO_0000047465"
FT DOMAIN 8..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 176..198
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 204..226
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 232..254
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 260..282
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 288..310
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 316..338
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 344..366
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 372..394
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 400..422
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 428..450
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 456..478
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 484..506
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 512..534
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 540..562
FT /note="C2H2-type 14; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 568..590
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 596..618
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 652..674
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 680..702
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 473
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 625
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 118
FT /note="M -> V (in dbSNP:rs2068061)"
FT /evidence="ECO:0000269|PubMed:10585455,
FT ECO:0000269|PubMed:12239212, ECO:0000269|PubMed:12743021,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_047061"
FT VARIANT 162
FT /note="H -> L (in dbSNP:rs4239529)"
FT /evidence="ECO:0000269|PubMed:10585455,
FT ECO:0000269|PubMed:12239212, ECO:0000269|PubMed:15489334"
FT /id="VAR_024204"
FT VARIANT 438
FT /note="K -> N (in dbSNP:rs3208201)"
FT /id="VAR_047062"
FT VARIANT 447
FT /note="Q -> H (in dbSNP:rs58935748)"
FT /id="VAR_061941"
FT VARIANT 506
FT /note="H -> D (in dbSNP:rs3746323)"
FT /id="VAR_047063"
FT VARIANT 640
FT /note="K -> E (in dbSNP:rs3746319)"
FT /evidence="ECO:0000269|PubMed:10585455,
FT ECO:0000269|PubMed:12239212"
FT /id="VAR_021891"
FT CONFLICT 137..151
FT /note="GLSVIHTRQKSSQGN -> RTICNSHKTEIFPRAI (in Ref. 3;
FT AAD32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 286
FT /note="K -> T (in Ref. 5; CAA36579)"
FT /evidence="ECO:0000305"
FT CONFLICT 400..401
FT /note="FK -> IQ (in Ref. 3; AAD32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="N -> I (in Ref. 3; AAD32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="Y -> H (in Ref. 3; AAD32448)"
FT /evidence="ECO:0000305"
FT CONFLICT 562
FT /note="H -> R (in Ref. 1; AAF04106)"
FT /evidence="ECO:0000305"
FT STRAND 174..177
FT /evidence="ECO:0007829|PDB:2EN8"
FT TURN 179..181
FT /evidence="ECO:0007829|PDB:2EN8"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:2EN8"
FT HELIX 188..195
FT /evidence="ECO:0007829|PDB:2EN8"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:2EN8"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2EM6"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:2EM6"
FT TURN 224..226
FT /evidence="ECO:0007829|PDB:2EM6"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:2EM6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2ELY"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:2ELY"
FT HELIX 246..254
FT /evidence="ECO:0007829|PDB:2ELY"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:2EOR"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:2EOR"
FT STRAND 268..271
FT /evidence="ECO:0007829|PDB:2EOR"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:2EOQ"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2EOQ"
FT HELIX 300..309
FT /evidence="ECO:0007829|PDB:2EOQ"
FT STRAND 313..317
FT /evidence="ECO:0007829|PDB:2ENA"
FT TURN 319..321
FT /evidence="ECO:0007829|PDB:2ENA"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:2ENA"
FT HELIX 328..338
FT /evidence="ECO:0007829|PDB:2ENA"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:2EM7"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:2EM7"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:2EM7"
FT HELIX 356..362
FT /evidence="ECO:0007829|PDB:2EM7"
FT HELIX 363..366
FT /evidence="ECO:0007829|PDB:2EM7"
FT STRAND 371..373
FT /evidence="ECO:0007829|PDB:2EM9"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:2EM9"
FT STRAND 380..383
FT /evidence="ECO:0007829|PDB:2EM9"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:2EM9"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:2EM9"
FT STRAND 399..401
FT /evidence="ECO:0007829|PDB:2ENC"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:2ENC"
FT STRAND 408..411
FT /evidence="ECO:0007829|PDB:2ENC"
FT HELIX 412..421
FT /evidence="ECO:0007829|PDB:2ENC"
FT STRAND 427..429
FT /evidence="ECO:0007829|PDB:2EM8"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:2EM8"
FT STRAND 436..439
FT /evidence="ECO:0007829|PDB:2EM8"
FT HELIX 440..451
FT /evidence="ECO:0007829|PDB:2EM8"
FT TURN 459..462
FT /evidence="ECO:0007829|PDB:2EQ4"
FT HELIX 468..477
FT /evidence="ECO:0007829|PDB:2EQ4"
FT STRAND 480..482
FT /evidence="ECO:0007829|PDB:2EQ4"
FT STRAND 487..489
FT /evidence="ECO:0007829|PDB:2YTH"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2YTH"
FT HELIX 496..502
FT /evidence="ECO:0007829|PDB:2YTH"
FT HELIX 503..506
FT /evidence="ECO:0007829|PDB:2YTH"
FT STRAND 511..513
FT /evidence="ECO:0007829|PDB:2YSP"
FT TURN 515..517
FT /evidence="ECO:0007829|PDB:2YSP"
FT STRAND 520..522
FT /evidence="ECO:0007829|PDB:2YSP"
FT HELIX 524..531
FT /evidence="ECO:0007829|PDB:2YSP"
FT STRAND 567..569
FT /evidence="ECO:0007829|PDB:2EN1"
FT TURN 571..573
FT /evidence="ECO:0007829|PDB:2EN1"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:2EN1"
FT HELIX 580..586
FT /evidence="ECO:0007829|PDB:2EN1"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:2EN1"
FT STRAND 655..657
FT /evidence="ECO:0007829|PDB:2ELZ"
FT HELIX 664..670
FT /evidence="ECO:0007829|PDB:2ELZ"
FT HELIX 671..675
FT /evidence="ECO:0007829|PDB:2ELZ"
FT STRAND 683..685
FT /evidence="ECO:0007829|PDB:2EM0"
FT HELIX 692..698
FT /evidence="ECO:0007829|PDB:2EM0"
FT HELIX 699..702
FT /evidence="ECO:0007829|PDB:2EM0"
FT STRAND 703..706
FT /evidence="ECO:0007829|PDB:2EM0"
SQ SEQUENCE 707 AA; 82280 MW; E9C1346D52BBF38F CRC64;
MTTFKEAMTF KDVAVVFTEE ELGLLDLAQR KLYRDVMLEN FRNLLSVGHQ AFHRDTFHFL
REEKIWMMKT AIQREGNSGD KIQTEMETVS EAGTHQEWSF QQIWEKIASD LTRSQDLMIN
SSQFSKEGDF PCQTEAGLSV IHTRQKSSQG NGYKPSFSDV SHFDFHQQLH SGEKSHTCDE
CGKNFCYISA LRIHQRVHMG EKCYKCDVCG KEFSQSSHLQ THQRVHTGEK PFKCVECGKG
FSRRSALNVH HKLHTGEKPY NCEECGKAFI HDSQLQEHQR IHTGEKPFKC DICGKSFCGR
SRLNRHSMVH TAEKPFRCDT CDKSFRQRSA LNSHRMIHTG EKPYKCEECG KGFICRRDLY
THHMVHTGEK PYNCKECGKS FRWASCLLKH QRVHSGEKPF KCEECGKGFY TNSQCYSHQR
SHSGEKPYKC VECGKGYKRR LDLDFHQRVH TGEKLYNCKE CGKSFSRAPC LLKHERLHSG
EKPFQCEECG KRFTQNSHLH SHQRVHTGEK PYKCEKCGKG YNSKFNLDMH QKVHTGERPY
NCKECGKSFG WASCLLKHQR LHSGEKPFKC EECGKRFTQN SQLHSHQRVH TGEKPYKCDE
CGKGFSWSST RLTHQRRHSR ETPLKCEQHG KNIVQNSFSK VQEKVHSVEK PYKCEDCGKG
YNRRLNLDMH QRVHMGEKTW KCRECDMCFS QASSLRLHQN VHVGEKP
