EPAS1_MOUSE
ID EPAS1_MOUSE Reviewed; 874 AA.
AC P97481; O08787; O55046;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Endothelial PAS domain-containing protein 1;
DE Short=EPAS-1;
DE AltName: Full=HIF-1-alpha-like factor;
DE Short=HLF;
DE Short=mHLF;
DE AltName: Full=HIF-related factor;
DE Short=HRF;
DE AltName: Full=Hypoxia-inducible factor 2-alpha;
DE Short=HIF-2-alpha;
DE Short=HIF2-alpha;
GN Name=Epas1; Synonyms=Hif2a;
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].
RC TISSUE=Brain;
RX PubMed=9000051; DOI=10.1101/gad.11.1.72;
RA Tian H., McKnight S.L., Russell D.W.;
RT "Endothelial PAS domain protein 1 (EPAS1), a transcription factor
RT selectively expressed in endothelial cells.";
RL Genes Dev. 11:72-82(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Hypothalamus, and Skeletal muscle;
RX PubMed=9113979; DOI=10.1073/pnas.94.9.4273;
RA Ema M., Taya S., Yokotani N., Sogawa K., Matsuda Y., Fujii-Kuriyama Y.;
RT "A novel bHLH-PAS factor with close sequence similarity to hypoxia-
RT inducible factor 1alpha regulates the VEGF expression and is potentially
RT involved in lung and vascular development.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:4273-4278(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain capillary;
RX PubMed=9178256; DOI=10.1016/s0925-4773(97)00674-6;
RA Flamme I., Froehlich T., von Reutern M., Kappel A., Damert A., Risau W.;
RT "HRF, a putative basic helix-loop-helix-PAS-domain transcription factor is
RT closely related to hypoxia-inducible factor-1 alpha and developmentally
RT expressed in blood vessels.";
RL Mech. Dev. 63:51-60(1997).
RN [4]
RP PROTEIN SEQUENCE OF 846-864, AND MUTAGENESIS OF PRO-530 AND ASN-851.
RX PubMed=12080085; DOI=10.1101/gad.991402;
RA Lando D., Peet D.J., Gorman J.J., Whelan D.A., Whitelaw M.L., Bruick R.K.;
RT "FIH-1 is an asparaginyl hydroxylase enzyme that regulates the
RT transcriptional activity of hypoxia-inducible factor.";
RL Genes Dev. 16:1466-1471(2002).
RN [5]
RP INTERACTION WITH CREBBP, PHOSPHORYLATION AT THR-844, AND MUTAGENESIS OF
RP THR-844.
RX PubMed=11983697; DOI=10.1074/jbc.m201307200;
RA Gradin K., Takasaki C., Fujii-Kuriyama Y., Sogawa K.;
RT "The transcriptional activation function of the HIF-like factor requires
RT phosphorylation at a conserved threonine.";
RL J. Biol. Chem. 277:23508-23514(2002).
RN [6]
RP HYDROXYLATION AT ASN-851.
RX PubMed=11823643; DOI=10.1126/science.1068592;
RA Lando D., Peet D.J., Whelan D.A., Gorman J.J., Whitelaw M.L.;
RT "Asparagine hydroxylation of the HIF transactivation domain a hypoxic
RT switch.";
RL Science 295:858-861(2002).
RN [7]
RP INTERACTION WITH HIF3A, AND SUBCELLULAR LOCATION.
RX PubMed=21546903; DOI=10.1038/cdd.2011.47;
RA Torii S., Goto Y., Ishizawa T., Hoshi H., Goryo K., Yasumoto K.,
RA Fukumura H., Sogawa K.;
RT "Pro-apoptotic activity of inhibitory PAS domain protein (IPAS), a negative
RT regulator of HIF-1, through binding to pro-survival Bcl-2 family
RT proteins.";
RL Cell Death Differ. 18:1711-1725(2011).
RN [8] {ECO:0007744|PDB:4ZP4, ECO:0007744|PDB:4ZPH, ECO:0007744|PDB:4ZPK, ECO:0007744|PDB:4ZQD}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 3-361 IN COMPLEXES WITH ARNT;
RP INHIBITOR AND DNA, MUTAGENESIS OF ALA-23; ARG-27; PHE-169; ARG-171;
RP ASN-184; LYS-186; VAL-192 AND HIS-194, REGION, FUNCTION, AND INTERACTION
RP WITH ARNT.
RX PubMed=26245371; DOI=10.1038/nature14883;
RA Wu D., Potluri N., Lu J., Kim Y., Rastinejad F.;
RT "Structural integration in hypoxia-inducible factors.";
RL Nature 524:303-308(2015).
CC -!- FUNCTION: Transcription factor involved in the induction of oxygen
CC regulated genes. Heterodimerizes with ARNT; heterodimer binds to core
CC DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of
CC target gene promoters (PubMed:26245371). Regulates the vascular
CC endothelial growth factor (VEGF) expression and seems to be implicated
CC in the development of blood vessels and the tubular system of lung. May
CC also play a role in the formation of the endothelium that gives rise to
CC the blood brain barrier. Potent activator of the Tie-2 tyrosine kinase
CC expression. Activation requires recruitment of transcriptional
CC coactivators such as CREBBP and probably EP300. Interaction with redox
CC regulatory protein APEX seems to activate CTAD (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:26245371}.
CC -!- SUBUNIT: Interacts with HIF3A isoform 2 (PubMed:21546903). Efficient
CC DNA binding requires dimerization with another bHLH protein.
CC Heterodimerizes with ARNT; heterodimer binds to core DNA sequence 5'-
CC TACGTG-3' within the hypoxia response element (HRE) of target gene
CC promoters (PubMed:26245371). Interacts with CREBBP (PubMed:11983697).
CC Interacts with EGLN1. Interacts with VHL (By similarity).
CC {ECO:0000250|UniProtKB:Q99814, ECO:0000269|PubMed:11983697,
CC ECO:0000269|PubMed:21546903, ECO:0000269|PubMed:26245371}.
CC -!- INTERACTION:
CC P97481; P53762: Arnt; NbExp=5; IntAct=EBI-15704570, EBI-78852;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:21546903}. Nucleus speckle
CC {ECO:0000269|PubMed:21546903}. Note=Colocalizes with HIF3A isoform 2 in
CC the nucleus and speckles. {ECO:0000269|PubMed:21546903}.
CC -!- TISSUE SPECIFICITY: Expressed in most tissues, with highest levels in
CC lung, followed by heart, kidney, brain and liver. Predominantly
CC expressed in endothelial cells. Also found in smooth muscle cells of
CC the uterus, neurons, and brown adipose tissue. High expression in
CC embryonic choroid plexus and kidney glomeruli.
CC -!- DEVELOPMENTAL STAGE: In day 11 embryo, expression is almost exclusively
CC seen in endothelial cells of the intersegmental blood vessels
CC separating the somites, the atrial and ventricular chambers of the
CC heart, and the dorsal aorta. High expression also occurs in
CC extraembryonic membranes. In the developing brain of day 13 embryo,
CC endothelial cells of the highly vascularized choroid plexus contain
CC high levels of EPAS1.
CC -!- PTM: In normoxia, is probably hydroxylated on Pro-405 and Pro-530 by
CC EGLN1/PHD1, EGLN2/PHD2 and/or EGLN3/PHD3. The hydroxylated prolines
CC promote interaction with VHL, initiating rapid ubiquitination and
CC subsequent proteasomal degradation. Under hypoxia, proline
CC hydroxylation is impaired and ubiquitination is attenuated, resulting
CC in stabilization (By similarity). {ECO:0000250}.
CC -!- PTM: In normoxia, is hydroxylated on Asn-851 by HIF1AN thus probably
CC abrogating interaction with CREBBP and EP300 and preventing
CC transcriptional activation. {ECO:0000269|PubMed:11823643}.
CC -!- PTM: Phosphorylated on multiple sites in the CTAD.
CC {ECO:0000269|PubMed:11983697}.
CC -!- PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of
CC asparagine is (S) stereospecific within HIF CTAD domains.
CC {ECO:0000269|PubMed:11823643}.
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DR EMBL; U81983; AAB41496.1; -; mRNA.
DR EMBL; D89787; BAA20130.1; -; mRNA.
DR EMBL; AF045160; AAC12871.1; -; mRNA.
DR CCDS; CCDS37713.1; -.
DR RefSeq; NP_034267.3; NM_010137.3.
DR PDB; 4ZP4; X-ray; 2.35 A; B/D=3-361.
DR PDB; 4ZPH; X-ray; 2.80 A; B/D=3-361.
DR PDB; 4ZPK; X-ray; 3.60 A; B=3-361.
DR PDB; 4ZQD; X-ray; 2.87 A; B/D=3-361.
DR PDB; 6E3S; X-ray; 3.00 A; B=3-362.
DR PDB; 6E3T; X-ray; 3.00 A; B=3-362.
DR PDB; 6E3U; X-ray; 2.85 A; B=3-362.
DR PDBsum; 4ZP4; -.
DR PDBsum; 4ZPH; -.
DR PDBsum; 4ZPK; -.
DR PDBsum; 4ZQD; -.
DR PDBsum; 6E3S; -.
DR PDBsum; 6E3T; -.
DR PDBsum; 6E3U; -.
DR AlphaFoldDB; P97481; -.
DR SMR; P97481; -.
DR BioGRID; 199458; 23.
DR DIP; DIP-46109N; -.
DR IntAct; P97481; 4.
DR STRING; 10090.ENSMUSP00000024954; -.
DR iPTMnet; P97481; -.
DR PhosphoSitePlus; P97481; -.
DR MaxQB; P97481; -.
DR PaxDb; P97481; -.
DR PRIDE; P97481; -.
DR ProteomicsDB; 277882; -.
DR Antibodypedia; 29965; 744 antibodies from 39 providers.
DR DNASU; 13819; -.
DR Ensembl; ENSMUST00000024954; ENSMUSP00000024954; ENSMUSG00000024140.
DR GeneID; 13819; -.
DR KEGG; mmu:13819; -.
DR UCSC; uc008duj.2; mouse.
DR CTD; 2034; -.
DR MGI; MGI:109169; Epas1.
DR VEuPathDB; HostDB:ENSMUSG00000024140; -.
DR eggNOG; KOG3558; Eukaryota.
DR GeneTree; ENSGT00940000155930; -.
DR HOGENOM; CLU_010044_3_1_1; -.
DR InParanoid; P97481; -.
DR OMA; QPTPQHC; -.
DR OrthoDB; 547545at2759; -.
DR PhylomeDB; P97481; -.
DR TreeFam; TF317772; -.
DR Reactome; R-MMU-1234158; Regulation of gene expression by Hypoxia-inducible Factor.
DR Reactome; R-MMU-1234174; Cellular response to hypoxia.
DR Reactome; R-MMU-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 13819; 2 hits in 75 CRISPR screens.
DR ChiTaRS; Epas1; mouse.
DR PRO; PR:P97481; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; P97481; protein.
DR Bgee; ENSMUSG00000024140; Expressed in right lung lobe and 265 other tissues.
DR Genevisible; P97481; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0050897; F:cobalt ion binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IGI:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001223; F:transcription coactivator binding; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IMP:MGI.
DR GO; GO:0001974; P:blood vessel remodeling; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IGI:MGI.
DR GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
DR GO; GO:0001892; P:embryonic placenta development; IGI:MGI.
DR GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0010467; P:gene expression; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0055072; P:iron ion homeostasis; IGI:MGI.
DR GO; GO:0030324; P:lung development; IMP:MGI.
DR GO; GO:0007005; P:mitochondrion organization; IMP:MGI.
DR GO; GO:0042789; P:mRNA transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0048625; P:myoblast fate commitment; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0042421; P:norepinephrine biosynthetic process; ISO:MGI.
DR GO; GO:0042415; P:norepinephrine metabolic process; IMP:MGI.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:1903181; P:positive regulation of dopamine biosynthetic process; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0002027; P:regulation of heart rate; IMP:MGI.
DR GO; GO:2000434; P:regulation of protein neddylation; ISS:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0043619; P:regulation of transcription from RNA polymerase II promoter in response to oxidative stress; IDA:MGI.
DR GO; GO:0001666; P:response to hypoxia; IMP:MGI.
DR GO; GO:0006979; P:response to oxidative stress; IMP:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; IMP:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:MGI.
DR GO; GO:0007601; P:visual perception; IMP:MGI.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 4.10.280.10; -; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR014887; HIF-1_TAD_C.
DR InterPro; IPR021537; HIF_alpha_subunit.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR InterPro; IPR001067; Nuc_translocat.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR Pfam; PF11413; HIF-1; 1.
DR Pfam; PF08778; HIF-1a_CTAD; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 1.
DR PRINTS; PR00785; NCTRNSLOCATR.
DR SMART; SM00353; HLH; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 2.
DR SUPFAM; SSF47459; SSF47459; 1.
DR SUPFAM; SSF55785; SSF55785; 2.
DR TIGRFAMs; TIGR00229; sensory_box; 2.
DR PROSITE; PS50888; BHLH; 1.
DR PROSITE; PS50112; PAS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Angiogenesis; Developmental protein;
KW Differentiation; Direct protein sequencing; DNA-binding; Hydroxylation;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..874
FT /note="Endothelial PAS domain-containing protein 1"
FT /id="PRO_0000127420"
FT DOMAIN 14..67
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT DOMAIN 84..154
FT /note="PAS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 230..300
FT /note="PAS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 304..347
FT /note="PAC"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 26..53
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:26245371"
FT REGION 171..192
FT /note="Required for heterodimer formation with ARNT"
FT /evidence="ECO:0000269|PubMed:26245371"
FT REGION 438..489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..541
FT /note="NTAD"
FT REGION 777..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 834..874
FT /note="CTAD"
FT COMPBIAS 441..489
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 405
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 530
FT /note="4-hydroxyproline"
FT /evidence="ECO:0000250"
FT MOD_RES 844
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:11983697"
FT MOD_RES 851
FT /note="(3S)-3-hydroxyasparagine"
FT /evidence="ECO:0000269|PubMed:11823643"
FT MUTAGEN 23
FT /note="A->D: Decreases HRE DNA binding."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 27
FT /note="R->A: Decreases HRE DNA binding."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 169
FT /note="F->D: Decreases heterodimer formation with ARNT."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 171
FT /note="R->A: Markedly decreases heterodimer formation with
FT ARNT. Impairs heterodimer formation with ARNT; when
FT associated with D-192."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 184
FT /note="N->D: Decreases HRE DNA binding; when associated
FT with D-186."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 186
FT /note="K->D: Decreases HRE DNA binding; when associated
FT with D-184."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 192
FT /note="V->D: Markedly decreases heterodimer formation with
FT ARNT. Impairs heterodimer formation with ARNT; when
FT associated with A-171."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 194
FT /note="H->A: Decreases heterodimer formation with ARNT."
FT /evidence="ECO:0000269|PubMed:26245371"
FT MUTAGEN 530
FT /note="P->A: Confers transcriptional activity at normoxia;
FT when associated with A-851."
FT /evidence="ECO:0000269|PubMed:12080085"
FT MUTAGEN 844
FT /note="T->A: Decreases interaction with CREBBP."
FT /evidence="ECO:0000269|PubMed:11983697"
FT MUTAGEN 851
FT /note="N->A: Confers transcriptional activity at normoxia;
FT when associated with A-530."
FT /evidence="ECO:0000269|PubMed:12080085"
FT CONFLICT 25
FT /note="C -> S (in Ref. 2; BAA20130)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> KS (in Ref. 1; AAB41496)"
FT /evidence="ECO:0000305"
FT CONFLICT 439..440
FT /note="VS -> AA (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="D -> G (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="G -> V (in Ref. 2; BAA20130)"
FT /evidence="ECO:0000305"
FT CONFLICT 663
FT /note="A -> P (in Ref. 2; BAA20130)"
FT /evidence="ECO:0000305"
FT CONFLICT 669
FT /note="S -> W (in Ref. 1; AAB41496)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="P -> L (in Ref. 1; AAB41496)"
FT /evidence="ECO:0000305"
FT CONFLICT 678
FT /note="P -> L (in Ref. 1; AAB41496)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="D -> E (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 731
FT /note="P -> L (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 762
FT /note="A -> G (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 786
FT /note="P -> L (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 791
FT /note="S -> F (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="S -> N (in Ref. 3; AAC12871)"
FT /evidence="ECO:0000305"
FT HELIX 27..39
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 53..74
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 96..103
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 115..119
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 131..134
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 137..147
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 165..174
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:6E3S"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 189..200
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 221..228
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 277..280
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 283..299
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 300..303
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 307..310
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 314..327
FT /evidence="ECO:0007829|PDB:4ZP4"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:4ZP4"
FT STRAND 334..343
FT /evidence="ECO:0007829|PDB:4ZP4"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4ZP4"
SQ SEQUENCE 874 AA; 96712 MW; A6FFA490AE43640C CRC64;
MTADKEKKRS SSELRKEKSR DAARCRRSKE TEVFYELAHE LPLPHSVSSH LDKASIMRLA
ISFLRTHKLL SSVCSENESE AEADQQMDNL YLKALEGFIA VVTQDGDMIF LSENISKFMG
LTQVELTGHS IFDFTHPCDH EEIRENLTLK NGSGFGKKSK DVSTERDFFM RMKCTVTNRG
RTVNLKSATW KVLHCTGQVR VYNNCPPHSS LCGSKEPLLS CLIIMCEPIQ HPSHMDIPLD
SKTFLSRHSM DMKFTYCDDR ILELIGYHPE ELLGRSAYEF YHALDSENMT KSHQNLCTKG
QVVSGQYRML AKHGGYVWLE TQGTVIYNPR NLQPQCIMCV NYVLSEIEKN DVVFSMDQTE
SLFKPHLMAM NSIFDSSDDV AVTEKSNYLF TKLKEEPEEL AQLAPTPGDA IISLDFGSQN
FDEPSAYGKA ILPPGQPWVS GLRSHSAQSE SGSLPAFTVP QADTPGNTTP SASSSSSCST
PSSPEDYYSS LENPLKIEVI EKLFAMDTEP RDPGSTQTDF SELDLETLAP YIPMDGEDFQ
LSPICPEEPL MPESPQPTPQ HCFSTMTSIF QPLTPGATHG PFFLDKYPQQ LESRKTESEH
WPMSSIFFDA GSKGSLSPCC GQASTPLSSM GGRSNTQWPP DPPLHFGPTK WPVGDQSAES
LGALPVGSSQ LEPPSAPPHV SMFKMRSAKD FGARGPYMMS PAMIALSNKL KLKRQLEYEE
QAFQDTSGGD PPGTSSSHLM WKRMKSLMGG TCPLMPDKTI SANMAPDEFT QKSMRGLGQP
LRHLPPPQPP STRSSGENAK TGFPPQCYAS QFQDYGPPGA QKVSGVASRL LGPSFEPYLL
PELTRYDCEV NVPVPGSSTL LQGRDLLRAL DQAT
