IFI4_MOUSE
ID IFI4_MOUSE Reviewed; 619 AA.
AC P0DOV2; B7ZNS3; P15092; Q08619; Q3TM07; Q3U776; Q3U7F4; Q3U7K5; Q3UCH9;
AC Q8C4X3; Q921V9;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Interferon-activable protein 204;
DE Short=Ifi-204;
DE AltName: Full=Interferon-inducible protein p204;
GN Name=Ifi204;
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 [MRNA].
RX PubMed=2477366; DOI=10.1016/s0021-9258(18)71476-2;
RA Choubey D., Snoddy J., Chaturvedi V., Toniato E., Opdenakker G., Thakur A.,
RA Samanta H., Engel D.A., Lengyel P.;
RT "Interferons as gene activators. Indications for repeated gene duplication
RT during the evolution of a cluster of interferon-activatable genes on murine
RT chromosome 1.";
RL J. Biol. Chem. 264:17182-17189(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 1-208.
RC STRAIN=C57BL/6J; TISSUE=Bone marrow macrophage;
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 FUNCTION.
RX PubMed=10329630; DOI=10.1093/emboj/18.10.2845;
RA Liu C.J., Wang H., Lengyel P.;
RT "The interferon-inducible nucleolar p204 protein binds the ribosomal RNA-
RT specific UBF1 transcription factor and inhibits ribosomal RNA
RT transcription.";
RL EMBO J. 18:2845-2854(1999).
RN [6]
RP FUNCTION, AND INTERACTION WITH ID1; ID2 AND ID3.
RX PubMed=11940648; DOI=10.1128/mcb.22.9.2893-2905.2002;
RA Liu C.-J., Ding B., Wang H., Lengyel P.;
RT "The MyoD-inducible p204 protein overcomes the inhibition of myoblast
RT differentiation by Id proteins.";
RL Mol. Cell. Biol. 22:2893-2905(2002).
RN [7]
RP FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP RUNX2.
RX PubMed=15557274; DOI=10.1074/jbc.m412604200;
RA Liu C.-J., Chang E., Yu J., Carlson C.S., Prazak L., Yu X.-P., Ding B.,
RA Lengyel P., Di Cesare P.E.;
RT "The interferon-inducible p204 protein acts as a transcriptional
RT coactivator of Cbfa1 and enhances osteoblast differentiation.";
RL J. Biol. Chem. 280:2788-2796(2005).
RN [8]
RP FUNCTION.
RX PubMed=16458891; DOI=10.1016/j.febslet.2006.01.032;
RA Asefa B., Dermott J.M., Kaldis P., Stefanisko K., Garfinkel D.J.,
RA Keller J.R.;
RT "p205, a potential tumor suppressor, inhibits cell proliferation via
RT multiple pathways of cell cycle regulation.";
RL FEBS Lett. 580:1205-1214(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16556595; DOI=10.1074/jbc.m511747200;
RA Ding B., Liu C.-J., Huang Y., Hickey R.P., Yu J., Kong W., Lengyel P.;
RT "p204 is required for the differentiation of P19 murine embryonal carcinoma
RT cells to beating cardiac myocytes: its expression is activated by the
RT cardiac Gata4, Nkx2.5, and Tbx5 proteins.";
RL J. Biol. Chem. 281:14882-14892(2006).
RN [10]
RP FUNCTION.
RX PubMed=16556596; DOI=10.1074/jbc.m511748200;
RA Ding B., Liu C.-J., Huang Y., Yu J., Kong W., Lengyel P.;
RT "p204 protein overcomes the inhibition of the differentiation of P19 murine
RT embryonal carcinoma cells to beating cardiac myocytes by Id proteins.";
RL J. Biol. Chem. 281:14893-14906(2006).
RN [11]
RP INDUCTION, AND FUNCTION.
RX PubMed=16244109; DOI=10.1189/jlb.0205083;
RA Dauffy J., Mouchiroud G., Bourette R.P.;
RT "The interferon-inducible gene, Ifi204, is transcriptionally activated in
RT response to M-CSF, and its expression favors macrophage differentiation in
RT myeloid progenitor cells.";
RL J. Leukoc. Biol. 79:173-183(2006).
RN [12]
RP FUNCTION.
RX PubMed=25710914; DOI=10.4049/jimmunol.1402764;
RA Storek K.M., Gertsvolf N.A., Ohlson M.B., Monack D.M.;
RT "cGAS and Ifi204 cooperate to produce type I IFNs in response to
RT Francisella infection.";
RL J. Immunol. 194:3236-3245(2015).
RN [13]
RP FUNCTION, ACETYLATION, SUBCELLULAR LOCATION, INTERACTION WITH STING, AND
RP INDUCTION BY MYCOBACTERIUM BOVIS.
RX PubMed=28529930; DOI=10.3389/fcimb.2017.00169;
RA Chunfa L., Xin S., Qiang L., Sreevatsan S., Yang L., Zhao D., Zhou X.;
RT "The Central Role of IFI204 in IFN-beta Release and Autophagy Activation
RT during Mycobacterium bovis Infection.";
RL Front. Cell. Infect. Microbiol. 7:169-169(2017).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY STAPHYLOCOCCUS AUREUS.
RX PubMed=30936875; DOI=10.3389/fimmu.2019.00474;
RA Chen W., Yu S.X., Zhou F.H., Zhang X.J., Gao W.Y., Li K.Y., Liu Z.Z.,
RA Han W.Y., Yang Y.J.;
RT "DNA Sensor IFI204 Contributes to Host Defense Against Staphylococcus
RT aureus Infection in Mice.";
RL Front. Immunol. 10:474-474(2019).
RN [15] {ECO:0007744|PDB:5YZP, ECO:0007744|PDB:5YZW, ECO:0007744|PDB:5Z7D}
RP X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 216-417, DNA-BINDING, AND
RP FUNCTION.
RX PubMed=33619523; DOI=10.1093/nar/gkab076;
RA Fan X., Jiang J., Zhao D., Chen F., Ma H., Smith P., Unterholzner L.,
RA Xiao T.S., Jin T.;
RT "Structural mechanism of DNA recognition by the p204 HIN domain.";
RL Nucleic Acids Res. 49:2959-2972(2021).
CC -!- FUNCTION: Interferon-stimulated protein that plays a role in several
CC biological processes including cell differentiation, autophagy and
CC innate immunity (PubMed:16244109, PubMed:25710914, PubMed:30936875).
CC Cooperates with CGAS to sense dsDNA and activates the STING-dependent
CC type I IFN pathway (PubMed:25710914, PubMed:33619523). Mechanistically,
CC gets acteylated upon bacterial infection and then translocates from
CC nucleus into cytoplasm to recruit STING for activation of TBK1-
CC dependent IRF3 nuclear translocation and IFN-beta release
CC (PubMed:28529930). Inhibits the transcription of ribosomal RNA. May
CC inhibit DNA binding by UBTF. Inhibits cell growth via p53/TP53 and RB1-
CC dependent and independent pathways. Acts as a coactivator of RUNX2
CC during osteogenesis. May be involved in macrophage differentiation.
CC Enables skeletal muscle and cardiac myocyte differentiation by
CC sequestring Id proteins in the cytosol and promoting their
CC ubiquitination and subsequent degradation.
CC {ECO:0000269|PubMed:10329630, ECO:0000269|PubMed:11940648,
CC ECO:0000269|PubMed:15557274, ECO:0000269|PubMed:16244109,
CC ECO:0000269|PubMed:16458891, ECO:0000269|PubMed:16556595,
CC ECO:0000269|PubMed:16556596, ECO:0000269|PubMed:25710914,
CC ECO:0000269|PubMed:28529930, ECO:0000269|PubMed:30936875,
CC ECO:0000269|PubMed:33619523}.
CC -!- SUBUNIT: Interacts with UBTF. Interacts with RUNX2. Interacts with ID1,
CC ID2 and ID3. Interacts with STING (PubMed:28529930).
CC {ECO:0000269|PubMed:11940648, ECO:0000269|PubMed:15557274,
CC ECO:0000269|PubMed:28529930}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28529930}. Nucleus,
CC nucleolus. Cytoplasm {ECO:0000269|PubMed:28529930}. Note=Nuclear in
CC proliferating cells, translocates to cytosol during cell
CC differentiation or bacterial infection. {ECO:0000269|PubMed:28529930}.
CC -!- TISSUE SPECIFICITY: Present in osteoblasts (at protein level).
CC {ECO:0000269|PubMed:15557274}.
CC -!- INDUCTION: By beta interferon. By macrophage differentiation factors.
CC During myocyte differentiation. By different bacterial infections such
CC as Staphylococcus aureus or Mycobacterium bovis.
CC {ECO:0000269|PubMed:16244109, ECO:0000269|PubMed:28529930,
CC ECO:0000269|PubMed:30936875}.
CC -!- DOMAIN: The 2 HIN-200 domains are able to interact with RUNX2.
CC -!- PTM: Acetylated upon bacterial infection, leading to translocation from
CC nucleus to cytoplasm and subsequent recruitment of STING to activate
CC IFN-beta production. {ECO:0000269|PubMed:28529930}.
CC -!- DISRUPTION PHENOTYPE: Deletion mutant mice display increased
CC susceptibility to Staphylococcus aureus pulmonary infection.
CC {ECO:0000269|PubMed:30936875}.
CC -!- SIMILARITY: Belongs to the HIN-200 family. {ECO:0000305}.
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DR EMBL; M31419; AAA39313.1; -; mRNA.
DR EMBL; AK150522; BAE29634.1; -; mRNA.
DR EMBL; CT010351; CAJ18559.1; -; mRNA.
DR EMBL; BC010546; AAH10546.1; -; mRNA.
DR CCDS; CCDS35792.1; -.
DR PIR; B34457; B34457.
DR RefSeq; NP_032355.2; NM_008329.2.
DR PDB; 5YZP; X-ray; 1.58 A; A=216-417.
DR PDB; 5YZW; X-ray; 2.00 A; A/B=427-619.
DR PDB; 5Z7D; X-ray; 4.50 A; A/B/C=216-619.
DR PDB; 6OE9; X-ray; 1.94 A; A=211-415.
DR PDBsum; 5YZP; -.
DR PDBsum; 5YZW; -.
DR PDBsum; 5Z7D; -.
DR PDBsum; 6OE9; -.
DR AlphaFoldDB; P0DOV2; -.
DR SASBDB; P0DOV2; -.
DR SMR; P0DOV2; -.
DR STRING; 10090.ENSMUSP00000106845; -.
DR iPTMnet; P0DOV2; -.
DR PhosphoSitePlus; P0DOV2; -.
DR SwissPalm; P0DOV2; -.
DR EPD; P0DOV2; -.
DR jPOST; P0DOV2; -.
DR MaxQB; P0DOV2; -.
DR PRIDE; P0DOV2; -.
DR ProteomicsDB; 267106; -.
DR DNASU; 15951; -.
DR Ensembl; ENSMUST00000111214; ENSMUSP00000106845; ENSMUSG00000073489.
DR GeneID; 15951; -.
DR KEGG; mmu:15951; -.
DR CTD; 15951; -.
DR MGI; MGI:96429; Ifi204.
DR VEuPathDB; HostDB:ENSMUSG00000073489; -.
DR eggNOG; ENOG502QTQS; Eukaryota.
DR GeneTree; ENSGT00390000013296; -.
DR OMA; YNINCKE; -.
DR OrthoDB; 1304994at2759; -.
DR PhylomeDB; P0DOV2; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 15951; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Ifi204; mouse.
DR PRO; PR:P0DOV2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; P0DOV2; protein.
DR Bgee; ENSMUSG00000073489; Expressed in granulocyte and 114 other tissues.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0042405; C:nuclear inclusion body; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IGI:MGI.
DR GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0002218; P:activation of innate immune response; ISO:MGI.
DR GO; GO:0042149; P:cellular response to glucose starvation; ISO:MGI.
DR GO; GO:0035457; P:cellular response to interferon-alpha; IDA:UniProtKB.
DR GO; GO:0035458; P:cellular response to interferon-beta; IDA:MGI.
DR GO; GO:0071479; P:cellular response to ionizing radiation; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0048839; P:inner ear development; IDA:MGI.
DR GO; GO:0072332; P:intrinsic apoptotic signaling pathway by p53 class mediator; ISO:MGI.
DR GO; GO:0042771; P:intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; ISO:MGI.
DR GO; GO:0030224; P:monocyte differentiation; ISO:MGI.
DR GO; GO:2000117; P:negative regulation of cysteine-type endopeptidase activity; ISO:MGI.
DR GO; GO:0043392; P:negative regulation of DNA binding; ISO:MGI.
DR GO; GO:0045824; P:negative regulation of innate immune response; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0045071; P:negative regulation of viral genome replication; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0040029; P:regulation of gene expression, epigenetic; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0009617; P:response to bacterium; IEP:MGI.
DR Gene3D; 1.10.533.10; -; 1.
DR Gene3D; 2.40.50.140; -; 4.
DR InterPro; IPR004020; DAPIN.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR040205; HIN-200.
DR InterPro; IPR004021; HIN200/IF120x.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR PANTHER; PTHR12200; PTHR12200; 2.
DR Pfam; PF02760; HIN; 2.
DR Pfam; PF02758; PYRIN; 1.
DR SMART; SM01289; PYRIN; 1.
DR PROSITE; PS50824; DAPIN; 1.
DR PROSITE; PS50834; HIN_200; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Cytoplasm; Developmental protein;
KW DNA-binding; Immunity; Innate immunity; Nucleus; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..619
FT /note="Interferon-activable protein 204"
FT /id="PRO_0000153721"
FT DOMAIN 1..88
FT /note="Pyrin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00061"
FT REPEAT 134..140
FT /note="1"
FT REPEAT 141..147
FT /note="2"
FT REPEAT 148..154
FT /note="3"
FT DOMAIN 213..413
FT /note="HIN-200 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT DOMAIN 417..615
FT /note="HIN-200 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00106"
FT REGION 86..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..154
FT /note="3 X 7 AA tandem repeats of A-[GR]-T-S-T-A-Q"
FT REGION 550..614
FT /note="Interaction with ID2"
FT /evidence="ECO:0000269|PubMed:11940648"
FT MOTIF 24..35
FT /note="Nuclear export signal"
FT MOTIF 150..157
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 93..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 155..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..221
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 67
FT /note="A -> E (in Ref. 1; AAA39313, 2; CAJ18559 and 3;
FT AAH10546)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> ARTSTAQARTSTAQARTSTAQA (in Ref. 1; AAA39313)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="A -> ARTSTAQE (in Ref. 2; CAJ18559 and 3; AAH10546)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="I -> S (in Ref. 1; AAA39313, 2; CAJ18559 and 3;
FT AAH10546)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="R -> M (in Ref. 1; AAA39313, 2; CAJ18559 and 3;
FT AAH10546)"
FT /evidence="ECO:0000305"
FT CONFLICT 513
FT /note="T -> R (in Ref. 1; AAA39313)"
FT /evidence="ECO:0000305"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6OE9"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 229..236
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:5YZP"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:5YZP"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 282..291
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:5YZP"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:5YZP"
FT HELIX 316..323
FT /evidence="ECO:0007829|PDB:5YZP"
FT HELIX 328..331
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 339..351
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 356..362
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 365..371
FT /evidence="ECO:0007829|PDB:5YZP"
FT HELIX 373..375
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 385..395
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 397..403
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:5YZP"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:5YZW"
FT TURN 448..451
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 452..460
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 465..471
FT /evidence="ECO:0007829|PDB:5YZW"
FT HELIX 473..477
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 489..493
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:5YZW"
FT HELIX 502..504
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:5YZW"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:5YZW"
FT HELIX 530..534
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 541..554
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 557..564
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 567..573
FT /evidence="ECO:0007829|PDB:5YZW"
FT HELIX 575..579
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 587..597
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 602..605
FT /evidence="ECO:0007829|PDB:5YZW"
FT STRAND 611..614
FT /evidence="ECO:0007829|PDB:5YZW"
SQ SEQUENCE 619 AA; 69438 MW; 877717943E654308 CRC64;
MVNEYKRIVL LRGLECINKH YFSLFKSLLA RDLNLERDNQ EQYTTIQIAN MMEEKFPADS
GLGKLIAFCE EVPALRKRAE ILKKERSEVT GETSLEKNGQ EAGPATPTST TSHMLASERG
ETSATQEETS TAQAGTSTAQ ARTSTAQAGT STAQKRKIMR EEETGVKKSK AAKEPDQPPC
CEEPTARCQS PILHSSSSAS SNIPSAKNQK SQPQNQNIPR GAVLHSEPLT VMVLTATDPF
EYESPEHEVK NMLHATVATV SQYFHVKVFN INLKEKFTKK NFIIISNYFE SKGILEINET
SSVLEAAPDQ MIEVPNSIIR NANASPKICD IQKGTSGAVF YGVFTLHKKT VNRKNTIYEI
KDGSGSIEVV GSGKWHNINC KEGDKLHLFC FHLKTIDRQP KLVCGEHSFI KISKRGNVPK
EPAKEEDHHH GPKQVMVLKV TEPFTYDLKE DKRMFHATVA TETEFFRVKV FDTALKSKFI
PRNIIAISDY FGCNGFLEIY RASCVSDVNV NPTMVISNTL RQRANATPKI SYLFSQARGT
FVSGEYLVNK KTERNKFIYY GIGDDTGKME VVVYGRLTNV RCEPGSKLRL VCFELTSTED
GWQLRSVRHS YMQVINARK
