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 29-MAY-2024, entry version 208. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 20. DR IntAct; Q9NZL3; 14. 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; 9606-ENSP00000337368; -. DR PeptideAtlas; Q9NZL3; -. DR ProteomicsDB; 83427; -. DR Pumba; Q9NZL3; -. DR Antibodypedia; 65029; 146 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 AGR; HGNC:13017; -. 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; 5252669at2759; -. 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 1177 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 179 other cell types or tissues. DR ExpressionAtlas; Q9NZL3; baseline and differential. 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:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR CDD; cd07765; KRAB_A-box; 1. DR Gene3D; 6.10.140.140; -; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 18. DR InterPro; IPR001909; KRAB. DR InterPro; IPR036051; KRAB_dom_sf. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR24377; IP01015P-RELATED; 1. DR PANTHER; PTHR24377:SF1012; ZINC FINGER PROTEIN 45; 1. DR Pfam; PF01352; KRAB; 1. DR Pfam; PF00096; zf-C2H2; 16. DR SMART; SM00349; KRAB; 1. DR SMART; SM00355; ZnF_C2H2; 18. DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 10. DR SUPFAM; SSF109640; KRAB domain (Kruppel-associated box); 1. 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 //