ZN484_HUMAN
ID ZN484_HUMAN Reviewed; 852 AA.
AC Q5JVG2; B1AL89; B4DRI2;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Zinc finger protein 484;
GN Name=ZNF484;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-156 AND LYS-816, 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 [6]
RP STRUCTURE BY NMR OF 379-803.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the C2H2 type zinc finger region of human zinc
RT finger protein 484.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q5JVG2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5JVG2-2; Sequence=VSP_043079;
CC Name=3;
CC IsoId=Q5JVG2-3; Sequence=VSP_044922;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AK091203; BAG52305.1; -; mRNA.
DR EMBL; AK299274; BAG61294.1; -; mRNA.
DR EMBL; AL136981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62837.1; -; Genomic_DNA.
DR EMBL; BC112394; AAI12395.1; -; mRNA.
DR EMBL; BC112396; AAI12397.1; -; mRNA.
DR CCDS; CCDS35066.1; -. [Q5JVG2-1]
DR CCDS; CCDS35067.1; -. [Q5JVG2-2]
DR CCDS; CCDS59136.1; -. [Q5JVG2-3]
DR RefSeq; NP_001007102.1; NM_001007101.2. [Q5JVG2-2]
DR RefSeq; NP_001248387.1; NM_001261458.1. [Q5JVG2-3]
DR RefSeq; NP_001248388.1; NM_001261459.1. [Q5JVG2-2]
DR RefSeq; NP_001248389.1; NM_001261460.1. [Q5JVG2-2]
DR RefSeq; NP_113674.1; NM_031486.2. [Q5JVG2-1]
DR RefSeq; XP_016870670.1; XM_017015181.1. [Q5JVG2-2]
DR PDB; 2EMF; NMR; -; A=379-411.
DR PDB; 2EMG; NMR; -; A=463-495.
DR PDB; 2EMH; NMR; -; A=491-523.
DR PDB; 2EMI; NMR; -; A=547-579.
DR PDB; 2EOV; NMR; -; A=519-551.
DR PDB; 2EP1; NMR; -; A=435-467.
DR PDB; 2EP2; NMR; -; A=603-635.
DR PDB; 2EP3; NMR; -; A=631-663.
DR PDB; 2EQW; NMR; -; A=409-437.
DR PDB; 2YTJ; NMR; -; A=771-803.
DR PDB; 2YTO; NMR; -; A=659-691.
DR PDB; 2YTP; NMR; -; A=687-719.
DR PDB; 2YTS; NMR; -; A=715-747.
DR PDBsum; 2EMF; -.
DR PDBsum; 2EMG; -.
DR PDBsum; 2EMH; -.
DR PDBsum; 2EMI; -.
DR PDBsum; 2EOV; -.
DR PDBsum; 2EP1; -.
DR PDBsum; 2EP2; -.
DR PDBsum; 2EP3; -.
DR PDBsum; 2EQW; -.
DR PDBsum; 2YTJ; -.
DR PDBsum; 2YTO; -.
DR PDBsum; 2YTP; -.
DR PDBsum; 2YTS; -.
DR AlphaFoldDB; Q5JVG2; -.
DR SMR; Q5JVG2; -.
DR BioGRID; 123752; 13.
DR IntAct; Q5JVG2; 5.
DR iPTMnet; Q5JVG2; -.
DR PhosphoSitePlus; Q5JVG2; -.
DR BioMuta; ZNF484; -.
DR DMDM; 74762200; -.
DR jPOST; Q5JVG2; -.
DR MassIVE; Q5JVG2; -.
DR MaxQB; Q5JVG2; -.
DR PaxDb; Q5JVG2; -.
DR PeptideAtlas; Q5JVG2; -.
DR PRIDE; Q5JVG2; -.
DR ProteomicsDB; 4953; -.
DR ProteomicsDB; 63331; -. [Q5JVG2-1]
DR ProteomicsDB; 63332; -. [Q5JVG2-2]
DR Antibodypedia; 28320; 100 antibodies from 16 providers.
DR DNASU; 83744; -.
DR Ensembl; ENST00000332591.6; ENSP00000364646.3; ENSG00000127081.14. [Q5JVG2-2]
DR Ensembl; ENST00000375495.8; ENSP00000364645.3; ENSG00000127081.14. [Q5JVG2-1]
DR Ensembl; ENST00000395505.6; ENSP00000378881.3; ENSG00000127081.14. [Q5JVG2-3]
DR Ensembl; ENST00000395506.7; ENSP00000378882.4; ENSG00000127081.14. [Q5JVG2-2]
DR GeneID; 83744; -.
DR KEGG; hsa:83744; -.
DR MANE-Select; ENST00000375495.8; ENSP00000364645.3; NM_031486.4; NP_113674.1.
DR UCSC; uc004asu.3; human. [Q5JVG2-1]
DR CTD; 83744; -.
DR DisGeNET; 83744; -.
DR GeneCards; ZNF484; -.
DR HGNC; HGNC:23385; ZNF484.
DR HPA; ENSG00000127081; Low tissue specificity.
DR neXtProt; NX_Q5JVG2; -.
DR OpenTargets; ENSG00000127081; -.
DR PharmGKB; PA134992184; -.
DR VEuPathDB; HostDB:ENSG00000127081; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000163284; -.
DR HOGENOM; CLU_002678_35_1_1; -.
DR InParanoid; Q5JVG2; -.
DR OMA; CEYNQCK; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q5JVG2; -.
DR TreeFam; TF350810; -.
DR PathwayCommons; Q5JVG2; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q5JVG2; -.
DR BioGRID-ORCS; 83744; 21 hits in 1088 CRISPR screens.
DR ChiTaRS; ZNF484; human.
DR EvolutionaryTrace; Q5JVG2; -.
DR GenomeRNAi; 83744; -.
DR Pharos; Q5JVG2; Tbio.
DR PRO; PR:Q5JVG2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5JVG2; protein.
DR Bgee; ENSG00000127081; Expressed in corpus callosum and 106 other tissues.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IBA:GO_Central.
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: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; 17.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 11.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 15.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 18.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..852
FT /note="Zinc finger protein 484"
FT /id="PRO_0000233986"
FT DOMAIN 8..78
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 223..245
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 279..301
FT /note="C2H2-type 2; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 328..350
FT /note="C2H2-type 3; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 356..378
FT /note="C2H2-type 4; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 384..406
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 412..434
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 440..462
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 468..490
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 524..546
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 552..574
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 580..602
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 608..630
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..658
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 692..714
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 720..742
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 748..770
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 776..798
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT CROSSLNK 156
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 816
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043079"
FT VAR_SEQ 1..5
FT /note="MTKSL -> MSVLSLP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044922"
FT VARIANT 502
FT /note="G -> D (in dbSNP:rs3739602)"
FT /id="VAR_033570"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:2EMF"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:2EMF"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:2EMF"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:2EMF"
FT HELIX 403..405
FT /evidence="ECO:0007829|PDB:2EMF"
FT STRAND 411..413
FT /evidence="ECO:0007829|PDB:2EQW"
FT STRAND 415..417
FT /evidence="ECO:0007829|PDB:2EQW"
FT STRAND 420..425
FT /evidence="ECO:0007829|PDB:2EQW"
FT HELIX 426..434
FT /evidence="ECO:0007829|PDB:2EQW"
FT STRAND 443..445
FT /evidence="ECO:0007829|PDB:2EP1"
FT HELIX 452..459
FT /evidence="ECO:0007829|PDB:2EP1"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:2EP1"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:2EP1"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:2EMG"
FT HELIX 480..487
FT /evidence="ECO:0007829|PDB:2EMG"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:2EMG"
FT STRAND 495..497
FT /evidence="ECO:0007829|PDB:2EMH"
FT TURN 499..501
FT /evidence="ECO:0007829|PDB:2EMH"
FT STRAND 504..507
FT /evidence="ECO:0007829|PDB:2EMH"
FT HELIX 508..519
FT /evidence="ECO:0007829|PDB:2EMH"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:2EOV"
FT HELIX 536..545
FT /evidence="ECO:0007829|PDB:2EOV"
FT STRAND 555..557
FT /evidence="ECO:0007829|PDB:2EMI"
FT STRAND 560..563
FT /evidence="ECO:0007829|PDB:2EMI"
FT HELIX 564..571
FT /evidence="ECO:0007829|PDB:2EMI"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:2EMI"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:2EP2"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:2EP2"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:2EP2"
FT HELIX 620..628
FT /evidence="ECO:0007829|PDB:2EP2"
FT STRAND 635..637
FT /evidence="ECO:0007829|PDB:2EP3"
FT STRAND 639..641
FT /evidence="ECO:0007829|PDB:2EP3"
FT STRAND 644..647
FT /evidence="ECO:0007829|PDB:2EP3"
FT HELIX 648..655
FT /evidence="ECO:0007829|PDB:2EP3"
FT TURN 656..660
FT /evidence="ECO:0007829|PDB:2EP3"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:2YTO"
FT STRAND 672..675
FT /evidence="ECO:0007829|PDB:2YTO"
FT HELIX 676..686
FT /evidence="ECO:0007829|PDB:2YTO"
FT STRAND 695..697
FT /evidence="ECO:0007829|PDB:2YTP"
FT STRAND 700..703
FT /evidence="ECO:0007829|PDB:2YTP"
FT HELIX 704..711
FT /evidence="ECO:0007829|PDB:2YTP"
FT TURN 712..714
FT /evidence="ECO:0007829|PDB:2YTP"
FT STRAND 719..721
FT /evidence="ECO:0007829|PDB:2YTS"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:2YTS"
FT STRAND 728..731
FT /evidence="ECO:0007829|PDB:2YTS"
FT HELIX 732..738
FT /evidence="ECO:0007829|PDB:2YTS"
FT HELIX 739..741
FT /evidence="ECO:0007829|PDB:2YTS"
FT STRAND 775..777
FT /evidence="ECO:0007829|PDB:2YTJ"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:2YTJ"
FT STRAND 784..787
FT /evidence="ECO:0007829|PDB:2YTJ"
FT HELIX 788..797
FT /evidence="ECO:0007829|PDB:2YTJ"
SQ SEQUENCE 852 AA; 98221 MW; 98A75F9C12877908 CRC64;
MTKSLESVSF KDVTVDFSRD EWQQLDLAQK SLYREVMLEN YFNLISVGCQ VPKPEVIFSL
EQEEPCMLDG EIPSQSRPDG DIGFGPLQQR MSEEVSFQSE ININLFTRDD PYSILEELWK
DDEHTRKCGE NQNKPLSRVV FINKKTLAND SIFEYKDIGE IVHVNTHLVS SRKRPHNCNS
CGKNLEPIIT LYNRNNATEN SDKTIGDGDI FTHLNSHTEV TACECNQCGK PLHHKQALIQ
QQKIHTRESL YLFSDYVNVF SPKSHAFAHE SICAEEKQHE CHECEAVFTQ KSQLDGSQRV
YAGICTEYEK DFSLKSNRQK TPYEGNYYKC SDYGRAFIQK SDLFRCQRIH SGEKPYEYSE
CEKNLPQNSN LNIHKKIHTG GKHFECTECG KAFTRKSTLS MHQKIHTGEK PYVCTECGKA
FIRKSHFITH ERIHTGEKPY ECSDCGKSFI KKSQLHVHQR IHTGENPFIC SECGKVFTHK
TNLIIHQKIH TGERPYICTV CGKAFTDRSN LIKHQKIHTG EKPYKCSDCG KSFTWKSRLR
IHQKCHTGER HYECSECGKA FIQKSTLSMH QRIHRGEKPY VCTECGKAFF HKSHFITHER
IHTGEKPYEC SICGKSFTKK SQLHVHQQIH TGEKPYRCAE CGKAFTDRSN LFTHQKIHTG
EKPYKCSDCG KAFTRKSGLH IHQQSHTGER HYECSECGKA FARKSTLIMH QRIHTGEKPY
ICNECGKSFI QKSHLNRHRR IHTGEKPYEC SDCGKSFIKK SQLHEHHRIH TGEKPYICAE
CGKAFTIRSN LIKHQKIHTK QKPYKCSDLG KALNWKPQLS MPQKSDNGEV ECSMPQLWCG
DSEGDQGQLS SI
