ID RN213_MOUSE Reviewed; 5148 AA. AC E9Q555; F7A6H4; Q8BVK6; DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot. DT 29-SEP-2021, sequence version 3. DT 24-JAN-2024, entry version 84. DE RecName: Full=E3 ubiquitin-protein ligase RNF213; DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q63HN8}; DE EC=3.6.4.- {ECO:0000269|PubMed:32573437}; DE AltName: Full=E3 ubiquitin-lipopolysaccharide ligase RNF213 {ECO:0000305}; DE EC=2.3.2.- {ECO:0000250|UniProtKB:Q63HN8}; DE AltName: Full=Mysterin {ECO:0000303|PubMed:26126547}; DE AltName: Full=RING finger protein 213 {ECO:0000305}; GN Name=Rnf213 {ECO:0000312|MGI:MGI:1289196}; GN Synonyms=Mystr {ECO:0000303|PubMed:26126547}; 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 [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4807-5148. RC STRAIN=C57BL/6J; TISSUE=Testis; 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 [3] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Pancreas, Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=23410753; DOI=10.1016/j.bbrc.2013.02.015; RA Kobayashi H., Yamazaki S., Takashima S., Liu W., Okuda H., Yan J., RA Fujii Y., Hitomi T., Harada K.H., Habu T., Koizumi A.; RT "Ablation of Rnf213 retards progression of diabetes in the Akita mouse."; RL Biochem. Biophys. Res. Commun. 432:519-525(2013). RN [5] RP DISRUPTION PHENOTYPE. RX PubMed=24440776; DOI=10.1016/j.brainres.2014.01.011; RA Sonobe S., Fujimura M., Niizuma K., Nishijima Y., Ito A., Shimizu H., RA Kikuchi A., Arai-Ichinoi N., Kure S., Tominaga T.; RT "Temporal profile of the vascular anatomy evaluated by 9.4-T magnetic RT resonance angiography and histopathological analysis in mice lacking RT RNF213: a susceptibility gene for moyamoya disease."; RL Brain Res. 1552:64-71(2014). RN [6] RP DISRUPTION PHENOTYPE. RX PubMed=25383461; DOI=10.1097/wnr.0000000000000289; RA Sonobe S., Fujimura M., Niizuma K., Fujimura T., Furudate S., Nishijima Y., RA Kure S., Tominaga T.; RT "Increased vascular MMP-9 in mice lacking RNF213: moyamoya disease RT susceptibility gene."; RL NeuroReport 25:1442-1446(2014). RN [7] RP MUTAGENESIS OF ARG-4753. RX PubMed=26315378; DOI=10.1016/j.brainres.2015.07.039; RA Kanoke A., Fujimura M., Niizuma K., Ito A., Sakata H., Sato-Maeda M., RA Morita-Fujimura Y., Kure S., Tominaga T.; RT "Temporal profile of the vascular anatomy evaluated by 9.4-tesla magnetic RT resonance angiography and histological analysis in mice with the R4859K RT mutation of RNF213, the susceptibility gene for moyamoya disease."; RL Brain Res. 1624:497-505(2015). RN [8] RP MUTAGENESIS OF ARG-4753. RX PubMed=26126547; DOI=10.1161/jaha.115.002146; RA Kobayashi H., Matsuda Y., Hitomi T., Okuda H., Shioi H., Matsuda T., RA Imai H., Sone M., Taura D., Harada K.H., Habu T., Takagi Y., Miyamoto S., RA Koizumi A.; RT "Biochemical and functional characterization of RNF213 (Mysterin) R4810K, a RT susceptibility mutation of Moyamoya disease, in angiogenesis in vitro and RT in vivo."; RL J. Am. Heart Assoc. 4:0-0(2015). RN [9] RP DISRUPTION PHENOTYPE. RX PubMed=33420513; DOI=10.1007/s00335-020-09856-y; RA Houzelstein D., Simon-Chazottes D., Batista L., Tokuda S., Langa Vives F., RA Flamand M., Montagutelli X., Panthier J.J.; RT "The ring finger protein 213 gene (Rnf213) contributes to Rift Valley fever RT resistance in mice."; RL Mamm. Genome 32:30-37(2021). RN [10] RP FUNCTION. RX PubMed=34012115; DOI=10.1038/s41586-021-03566-4; RA Otten E.G., Werner E., Crespillo-Casado A., Boyle K.B., Dharamdasani V., RA Pathe C., Santhanam B., Randow F.; RT "Ubiquitylation of lipopolysaccharide by RNF213 during bacterial RT infection."; RL Nature 594:111-116(2021). RN [11] {ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY} RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) OF 591-5152 IN COMPLEX RP WITH ZINC AND ATP, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, INTERACTION WITH RP UBE2L3, DOMAIN, AND MUTAGENESIS OF ARG-4753. RX PubMed=32573437; DOI=10.7554/elife.56185; RA Ahel J., Lehner A., Vogel A., Schleiffer A., Meinhart A., Haselbach D., RA Clausen T.; RT "Moyamoya disease factor RNF213 is a giant E3 ligase with a dynein-like RT core and a distinct ubiquitin-transfer mechanism."; RL Elife 9:0-0(2020). CC -!- FUNCTION: Atypical E3 ubiquitin ligase that can catalyze ubiquitination CC of both proteins and lipids, and which is involved in various CC processes, such as lipid metabolism, angiogenesis and cell-autonomous CC immunity (PubMed:32573437). Acts as a key immune sensor by catalyzing CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide CC (LPS) via its RZ-type zinc-finger: restricts the proliferation of CC cytosolic bacteria, such as Salmonella, by generating the bacterial CC ubiquitin coat through the ubiquitination of LPS (PubMed:34012115). CC Also acts indirectly by mediating the recruitment of the LUBAC complex, CC which conjugates linear polyubiquitin chains (By similarity). CC Ubiquitination of LPS triggers cell-autonomous immunity, such as CC antibacterial autophagy, leading to degradation of the microbial CC invader (By similarity). Involved in lipid metabolism by regulating fat CC storage and lipid droplet formation; act by inhibiting the lipolytic CC process (By similarity). Also regulates lipotoxicity by inhibiting CC desaturation of fatty acids (By similarity). Also acts as an E3 CC ubiquitin-protein ligase via its RING-type zinc finger: mediates 'Lys- CC 63'-linked ubiquitination of target proteins (By similarity). Involved CC in the non-canonical Wnt signaling pathway in vascular development: CC acts by mediating ubiquitination and degradation of FLNA and NFATC2 CC downstream of RSPO3, leading to inhibit the non-canonical Wnt signaling CC pathway and promoting vessel regression (By similarity). Also has CC ATPase activity; ATPase activity is required for ubiquitination of LPS CC (PubMed:32573437). {ECO:0000250|UniProtKB:Q63HN8, CC ECO:0000269|PubMed:32573437, ECO:0000269|PubMed:34012115}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q63HN8}; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:32573437}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000269|PubMed:32573437}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000250|UniProtKB:Q63HN8}. CC -!- SUBUNIT: Monomer (PubMed:32573437). Interacts with UBE2L3/UBCH7; CC UBE2L3/UBCH7 is the most efficient ubiquitin-conjugating enzyme E2 for CC the ubiquitin ligase activity (PubMed:32573437). Interacts with CC UBE2N/UBC13; promoting 'Lys-63'-linked ubiquitination of target CC proteins (By similarity). {ECO:0000250|UniProtKB:Q63HN8, CC ECO:0000269|PubMed:32573437}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol CC {ECO:0000250|UniProtKB:Q63HN8}. Lipid droplet CC {ECO:0000250|UniProtKB:Q63HN8}. CC -!- DOMAIN: Composed of an N-terminal stalk, a dynein-like core comprised CC of two catalytically active and four inactive ATPase domains, and a C- CC terminal E3 module (PubMed:32573437). The ATPase regions do not CC generate movement but rather act like an intricate molecular 'switch' CC (PubMed:32573437). {ECO:0000269|PubMed:32573437}. CC -!- DOMAIN: The RING-type zinc finger domain is required for the ubiquitin- CC protein ligase activity. {ECO:0000250|UniProtKB:Q63HN8}. CC -!- DOMAIN: The RZ-type (RNF213-ZNFX1) zinc-finger is required for the CC ubiquitination of the lipid A moiety of bacterial lipopolysaccharide CC (LPS). {ECO:0000250|UniProtKB:Q63HN8}. CC -!- DISRUPTION PHENOTYPE: No visible phenotype (PubMed:23410753, CC PubMed:24440776). Males and female are fertile and produce normal-sized CC litters (PubMed:23410753, PubMed:24440776). Mice do not spontaneously CC develop Moyamoya disease, a chronic occlusive cerebrovascular disease CC (PubMed:24440776). Mice are however more susceptible to Rift Valley CC fever virus infection (PubMed:33420513). Mice show elevated expression CC of MMP9 (PubMed:25383461). {ECO:0000269|PubMed:23410753, CC ECO:0000269|PubMed:24440776, ECO:0000269|PubMed:25383461, CC ECO:0000269|PubMed:33420513}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC -!- CAUTION: The stoichiometry is unclear: was initially thought to form CC homohexamers (By similarity). However, the electron microscopy CC structure showed that it is monomeric and is composed of six ATPase CC modules within a single polypeptide chain (PubMed:32573437). CC {ECO:0000250|UniProtKB:Q63HN8, ECO:0000269|PubMed:32573437}. CC -!- SEQUENCE CAUTION: CC Sequence=BAC37048.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={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; AL645911; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AK077880; BAC37048.1; ALT_INIT; mRNA. DR PDB; 6TAX; EM; 3.20 A; A=591-5148. DR PDB; 6TAY; EM; 3.20 A; A=591-5148. DR PDB; 7OIK; EM; 3.50 A; A=1-5148. DR PDB; 7OIM; EM; 4.00 A; A=339-5148. DR PDBsum; 6TAX; -. DR PDBsum; 6TAY; -. DR PDBsum; 7OIK; -. DR PDBsum; 7OIM; -. DR EMDB; EMD-10429; -. DR EMDB; EMD-10430; -. DR EMDB; EMD-12931; -. DR EMDB; EMD-12932; -. DR SMR; E9Q555; -. DR IntAct; E9Q555; 1. DR MINT; E9Q555; -. DR STRING; 10090.ENSMUSP00000091429; -. DR GlyGen; E9Q555; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; E9Q555; -. DR PhosphoSitePlus; E9Q555; -. DR SwissPalm; E9Q555; -. DR EPD; E9Q555; -. DR jPOST; E9Q555; -. DR PaxDb; 10090-ENSMUSP00000091429; -. DR PeptideAtlas; E9Q555; -. DR ProteomicsDB; 300423; -. DR Pumba; E9Q555; -. DR Antibodypedia; 46314; 210 antibodies from 27 providers. DR AGR; MGI:1289196; -. DR MGI; MGI:1289196; Rnf213. DR VEuPathDB; HostDB:ENSMUSG00000070327; -. DR eggNOG; ENOG502QQ65; Eukaryota. DR HOGENOM; CLU_000066_0_0_1; -. DR InParanoid; E9Q555; -. DR PhylomeDB; E9Q555; -. DR TreeFam; TF329577; -. DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation. DR UniPathway; UPA00143; -. DR ChiTaRS; Rnf213; mouse. DR PRO; PR:E9Q555; -. DR Proteomes; UP000000589; Chromosome 11. DR RNAct; E9Q555; Protein. DR Bgee; ENSMUSG00000070327; Expressed in small intestine Peyer's patch and 218 other cell types or tissues. DR ExpressionAtlas; E9Q555; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISS:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; ISS:UniProtKB. DR GO; GO:0001525; P:angiogenesis; IMP:UniProtKB. DR GO; GO:0042742; P:defense response to bacterium; IMP:UniProtKB. DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW. DR GO; GO:0140042; P:lipid droplet formation; ISS:UniProtKB. DR GO; GO:0120323; P:lipid ubiquitination; IMP:UniProtKB. DR GO; GO:2000051; P:negative regulation of non-canonical Wnt signaling pathway; ISS:UniProtKB. DR GO; GO:0051865; P:protein autoubiquitination; ISS:UniProtKB. DR GO; GO:0070534; P:protein K63-linked ubiquitination; ISS:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB. DR GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB. DR GO; GO:0002040; P:sprouting angiogenesis; ISS:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. DR GO; GO:0098792; P:xenophagy; ISS:UniProtKB. DR CDD; cd16561; RING-HC_RNF213; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR031248; RNF213. DR InterPro; IPR046439; ZF_RZ_dom. DR InterPro; IPR018957; Znf_C3HC4_RING-type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR PANTHER; PTHR22605:SF16; E3 UBIQUITIN-PROTEIN LIGASE RNF213; 1. DR PANTHER; PTHR22605; UNCHARACTERIZED; 1. DR Pfam; PF00097; zf-C3HC4; 1. DR Pfam; PF20173; ZnF_RZ-type; 1. DR SMART; SM00382; AAA; 2. DR SMART; SM00184; RING; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR PROSITE; PS51981; ZF_RZ; 1. DR Genevisible; E9Q555; MM. PE 1: Evidence at protein level; KW 3D-structure; Angiogenesis; ATP-binding; Coiled coil; Cytoplasm; Hydrolase; KW Immunity; Isopeptide bond; Lipid droplet; Lipid metabolism; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transferase; Ubl conjugation; Ubl conjugation pathway; KW Zinc; Zinc-finger. FT CHAIN 1..5148 FT /note="E3 ubiquitin-protein ligase RNF213" FT /id="PRO_0000415918" FT ZN_FING 3947..3986 FT /note="RING-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 4429..4501 FT /note="RZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT REGION 38..341 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 3435..3465 FT /evidence="ECO:0000255" FT COMPBIAS 64..79 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 120..142 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 164..183 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 324..341 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 4462 FT /note="Nucleophile; for E3 ubiquitin-lipopolysaccharide FT ligase activity" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT BINDING 1957..1962 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 2060 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 2114 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAY" FT BINDING 2116 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 2177 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX" FT BINDING 2460 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAY" FT BINDING 2535 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX" FT BINDING 3947 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3950 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3962 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3964 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3967 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3970 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3982 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 3985 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000269|PubMed:32573437, FT ECO:0007744|PDB:6TAX, ECO:0007744|PDB:6TAY" FT BINDING 4451 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT BINDING 4455 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT BINDING 4471 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT BINDING 4474 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01325" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63HN8" FT MOD_RES 2234 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q63HN8" FT CROSSLNK 1128 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000250|UniProtKB:Q63HN8" FT MUTAGEN 4753 FT /note="R->K: Knockin mice grow normally and do not show any FT visible phenotype. Slightly impaired angiogenesis. Does not FT affect ATPase or E3 ubiquitin ligase activities." FT /evidence="ECO:0000269|PubMed:26126547, FT ECO:0000269|PubMed:26315378, ECO:0000269|PubMed:32573437" FT HELIX 493..512 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 518..534 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 556..575 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 593..601 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 602..604 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 609..613 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 614..617 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 618..621 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 629..635 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 636..639 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 644..655 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 656..660 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 663..666 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 668..671 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 673..675 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 683..685 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 689..693 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 700..702 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 704..706 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 712..719 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 721..725 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 729..735 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 740..742 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 743..748 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 751..756 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 760..771 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 772..774 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 781..800 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 803..810 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 811..826 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 831..833 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 836..849 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 865..888 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 893..895 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 897..900 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 904..908 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 909..917 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 924..927 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 930..938 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 943..950 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 952..955 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 963..981 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 995..1009 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1013..1015 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1022..1030 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1033..1043 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1045..1048 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1049..1051 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1054..1071 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1072..1076 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1080..1088 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1090..1101 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1114..1142 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1143..1147 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1149..1151 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1155..1158 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1167..1170 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1191..1202 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1207..1217 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1231..1233 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1234..1240 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1242..1256 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1257..1259 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1263..1269 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1271..1273 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1277..1288 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1289..1292 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1296..1298 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1299..1328 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1339..1345 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1362..1367 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1368..1370 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1375..1377 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1378..1386 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1389..1397 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1401..1403 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1404..1414 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1419..1439 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1448..1463 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1468..1476 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1479..1486 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1498..1506 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1508..1511 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1516..1518 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1522..1525 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1526..1530 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1541..1544 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1545..1556 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1564..1593 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1596..1600 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1602..1606 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1612..1616 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1620..1622 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1625..1627 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1631..1659 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1662..1665 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1668..1678 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1680..1682 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1687..1690 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1691..1695 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1700..1708 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1714..1725 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1727..1730 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1736..1749 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1751..1753 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1761..1774 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1789..1796 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1799..1801 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1803..1809 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 1810..1812 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 1821..1826 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1833..1843 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1849..1851 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1853..1857 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1859..1861 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1864..1880 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1887..1892 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1894..1896 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 1901..1904 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1906..1908 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1918..1929 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1933..1935 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1938..1941 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1942..1945 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1947..1959 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1960..1973 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1974..1977 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1982..1987 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 1989..1991 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 1994..2001 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2002..2004 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2005..2010 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2015..2020 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2028..2036 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2040..2042 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2048..2050 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2055..2062 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2081..2084 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2085..2087 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2090..2092 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2096..2100 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2117..2120 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2123..2136 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2155..2165 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2168..2170 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 2173..2192 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2195..2202 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2203..2205 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2208..2223 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2248..2250 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2251..2254 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2260..2262 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2266..2269 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2271..2273 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2276..2280 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2282..2285 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2289..2294 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2296..2298 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2301..2304 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 2309..2317 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2326..2329 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 2331..2341 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2352..2354 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2358..2373 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2377..2380 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2383..2387 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2388..2399 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2407..2411 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2418..2439 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2443..2449 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2456..2463 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2479..2485 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2493..2500 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2502..2504 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2510..2512 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2516..2521 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2522..2524 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2525..2527 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2537..2539 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2540..2542 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 2548..2550 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 2551..2563 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2565..2567 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 2572..2588 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2589..2591 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2598..2600 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2601..2614 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2618..2630 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2643..2653 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2654..2657 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2661..2668 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2669..2671 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2674..2676 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2679..2696 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2707..2721 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2726..2729 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2734..2737 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2738..2746 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2749..2751 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2753..2755 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2756..2759 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2762..2768 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2776..2790 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2797..2805 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2807..2810 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2818..2820 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2821..2824 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2830..2832 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 2836..2838 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2841..2848 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2852..2855 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2857..2862 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2868..2879 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2886..2889 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2890..2892 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2893..2906 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2908..2910 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 2914..2931 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2937..2947 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2956..2960 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 2975..2983 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 2992..2994 FT /evidence="ECO:0007829|PDB:7OIK" FT STRAND 3002..3009 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3011..3017 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3026..3028 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3038..3055 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3059..3062 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3065..3067 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3069..3071 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3072..3076 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3080..3082 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3085..3092 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3095..3100 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3107..3112 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3113..3119 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3122..3124 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3125..3127 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3130..3132 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3136..3138 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3141..3158 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3164..3166 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3173..3176 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3184..3196 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3205..3218 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3223..3228 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3229..3231 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3232..3234 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3237..3248 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3255..3262 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3263..3265 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3271..3281 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3288..3294 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3295..3299 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3304..3307 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3308..3310 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3314..3325 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3327..3344 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3349..3364 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3371..3378 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3381..3386 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3397..3400 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3408..3410 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3414..3419 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3422..3425 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3477..3489 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3495..3498 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3502..3511 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3512..3517 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3518..3538 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3539..3542 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3544..3547 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3549..3554 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3557..3563 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3566..3589 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3591..3593 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3596..3599 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3600..3602 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3605..3614 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3618..3620 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3654..3656 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3658..3675 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3678..3680 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3681..3691 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3693..3698 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3703..3721 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3725..3727 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 3728..3745 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3748..3750 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 3758..3761 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 3763..3783 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3788..3799 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3802..3805 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3808..3823 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3824..3827 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3829..3838 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3840..3846 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3849..3851 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3857..3889 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3895..3909 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 3918..3940 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3948..3950 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 3955..3959 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 3965..3967 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 3968..3975 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3976..3978 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 3983..3985 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4000..4025 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4026..4028 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4030..4032 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4036..4044 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4069..4072 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4075..4077 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 4083..4088 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4093..4095 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4097..4110 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4113..4115 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4117..4137 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4143..4155 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4161..4163 FT /evidence="ECO:0007829|PDB:6TAY" FT STRAND 4166..4168 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4172..4197 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4202..4204 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4205..4218 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4223..4235 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4238..4244 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4246..4248 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4252..4254 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4257..4261 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4272..4275 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4280..4292 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4297..4303 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4310..4330 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4331..4334 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4338..4342 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4343..4352 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4354..4356 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4359..4369 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4374..4377 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4381..4384 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 4385..4402 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4406..4408 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4409..4416 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4418..4421 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4422..4425 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 4523..4543 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4545..4551 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4560..4577 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4578..4580 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4582..4595 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4614..4632 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4636..4638 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4639..4647 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4650..4654 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4656..4659 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4660..4663 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4666..4668 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4669..4672 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4677..4680 FT /evidence="ECO:0007829|PDB:6TAY" FT TURN 4681..4684 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4692..4701 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4702..4706 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4709..4716 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4718..4721 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4722..4726 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4727..4740 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4743..4745 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4752..4756 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4762..4782 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4783..4785 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4786..4789 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4798..4801 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4807..4809 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4816..4819 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4821..4844 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4855..4857 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 4860..4862 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4868..4871 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4873..4877 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4880..4884 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4891..4894 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4896..4904 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4905..4907 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4908..4910 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4916..4918 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4931..4940 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4948..4956 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4961..4979 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 4985..4988 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 4989..4993 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 4994..4996 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5004..5010 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5015..5017 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5018..5035 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 5042..5044 FT /evidence="ECO:0007829|PDB:7OIK" FT HELIX 5046..5048 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5054..5065 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5069..5083 FT /evidence="ECO:0007829|PDB:6TAX" FT STRAND 5090..5092 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5099..5106 FT /evidence="ECO:0007829|PDB:6TAX" FT TURN 5109..5111 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 5115..5120 FT /evidence="ECO:0007829|PDB:6TAX" FT HELIX 5128..5130 FT /evidence="ECO:0007829|PDB:6TAY" FT HELIX 5132..5148 FT /evidence="ECO:0007829|PDB:6TAX" SQ SEQUENCE 5148 AA; 584258 MW; 668FFE0AB2C2F8CE CRC64; MECPQCGHVS SEKAPKFCSE CGQKLPSAAT VQGDLKNDNT LVVSSTPEGK TEQGAVLREE EVLLSSTDPG KELEKPEESD SNASWTTQMS KKEKRRRKRQ GTISSSEAPS SGLWSLDMPP SPGSHNSALP QNQAQQGGAA SQPGHPLDTE NMPMEDGFVH TEGSGSPLQG QAAERTDAQS NLAPSDLAEV KDLNTSKPSV DKGLPLDGGP ALSAFKGHPK MTDASQKAPL PESKGETSGQ EKKVPPIDAA ASPVKTAGKE TGEDVRKPKP SPVSPVASKH GDQEAELKGK LATPVRKSNE GGNTQPEDQR KPGEGRNFAA AVKTQQAAAP QQAAAPEPTS AFNPRDTVTV YFHAIVSRHF GFNPEEHKVY VRGGEGLGQK GWTDACEMYC TQDLHDLGSL VEGKMDIPRQ SLDKPIPYKY VIHRGGSSKD TVEYEFIYEQ AQKKGEHVNR CLRVVSTSLG NGDWHQYDDI ICMRSTGFFQ QAKNRILDST RKELLKGKKQ AAVVMLDRIF SVLQPWSDIN LQSFMTQFLQ FYSVVREPMI HDGRARKWTS LQYEEKEVWT NLWEHVKKQM APFLEGKSGE SLPADCPVRS KLTLGLSILF MVEAAEFTVP KKDLDSLCYL LIPSAGSPEA LHSDLSPVLR IRQRWRIYLT NLCLRCIDER CDRWLGILPL LHTCMQKSPP KKNSKSQPED TWAGLEGISF SEFRDKAPTR SQPLQFMQSK MALLRVDEYL FRSWLSVVPL ESLSSYLENS IDYLSDVPVR VLDCLQGISY RLPGLRKISN QNMKKDVENV FKMLMHLVDI YQHRIFGENL LQIYLTECLT LHETVCNITA NHQFFEIPAL SAELICKLLE LSPPGHTDEG LPEKSYEDLV TSTLQEALAT TRNWLRSLFK SRMLSISSAY VRLTYSEEMA VWRRLVEIGF PEKHGWKGSL LGDMEGRLKQ EPPRLQISFF CSSQCRDGGL HDSVSRSFEK CVIEAVSSAC QSQTSVLEGL SCQDLQKFGT LLSAVITKSW PVHNGEPVFD VDEIFKYLLK WPDVRQLFEL CGTNEKIIDN ITEEGRQLMA TAESVFQKVA GELENGTIVV GQLELILEHQ SQFLDIWNLN RRRLPSQEKA CDVRSLLKRR RDDLLFLKQE KRYVESLLRQ LGRVKHLVQV DFGNIEIIHS QDLSNKKLNE AVIKLPNSSS YKRETHYCLS PDIREMASKL DSLKDSHIFQ DFWQETAESL NTLDKDPREL KVSLPEVLEY LYNPCYDNFY TLYENLKSGK ITFAEVDAIF KDFVDKYDEL KNDLKFMCTM NPQDQKGWIS ERVGQIKEYH TLHQAVSSAK VILQVRRALG VTGDFSVLNP LLNFADSFED FGNEKLDQIS PQFIKAKQLL QDISEPRQRC LEELARQTEL VAWLHKALED INELKVFVDL ASISAGENDI DVDRVACFHD AVQGYASLLY KMDERTNFSD FMNHLQELWR ALDNDQHLPD KLKDSARNLE WLKTVKESHG SVELSSLSLA TAINSRGVYV IEAPKDGQKI SPDTVLRLLL PDGHGYPEAL RTYSTEELKE LLNKLMLMSG KKDHNSNTEV EKFSEVFSNM QRLVHVFIKL HCAGNMLFRT WTAKVYCCPD GGIFMNFGLE LLSQLTEKGD VIQLLGALCR QMEDFLDNWK TVVAQKRAEH FYLNFYTAEQ LVYLSSELRK PRPSEAALMM LSFIKGKCTV QDLVQATSAC ESKADRYCLR EVMKKLPQQL LSEPSLMGKL QVIMMQSLVY MSAFLPHCLD LDALGRCLAH LATMGGTPVE RPLPKGLQAG QPNLILCGHS EVLPAALAIY MQAPRQPLPT FDEVLLCTPA TTIEEVELLL RRCLTSGSQG HKVYSLLFAD QLSYEVGCQA EEFFQSLCTR AHREDYQLVI LCDAAREHCY IPSTFSQYKV PLVPQAPLPN IQAYLQSHYQ VPKRLLSAAT VFRDGLCVGI VTSERAGVGK SLYVNTLHTK LKAKLRDETV PLKIIRLTEP HLDENQVLSA LLPFLKEKYQ KMPVIFHIDI STSVQTGIPI FLFKLLILQY LMDINGKIWR RSPGHLYLVE IPQGLSVQPK RSSKLNARAP LFKFLDLFPK VTCRPPKEVI DMELTPERSH TDPAMDPVEF CSEAFQRPYQ YLKRFHQQQN LDTFQYEKGS VEGSPEECLQ HFLIYCGLIN PSWSELRNFA WFLNCQLKDC EASIFCKSAF TGDTLRGFKN FVVTFMILMA RDFATPTLHT SDQSPGRQSV TIGEVVEEDL APFSLRKRWE SEPHPYVFFN GDHMTMTFIG FHLETNNNGY VDAINPSNGK VIKKDVMTKE LFDGLRLQRV PFNIDFDNLP RYEKLERLCL ALGIEWPIDP DETYELTTDN MLKILAIEMR FRCGIPVIIM GETGCGKTRL IKFLSDLKRG SVEAETMKLV KVHGGTTPSM IYSKVKEAER TAFSNKAQHK LDTILFFDEA NTTEAVSCIK EILCDRTVDG EHLHEDSGLH IIAACNPYRK HSQEMILRLE SAGLGYRVSA EETADRLGSI PLRQLVYRVH ALPPSLIPLV WDFGQLNDSA EKLYIQQIVQ RLVDSVSVNP SETCVIADVL SASQMFMRKR ENECGFVSLR DVERCVKVFR WFHDHSDMLL KELDKFLHES SDSTHTFERD PVLWSLVMAI GVCYHASLEE KASYRTAIAR CFPKPYNSSR AILDEVTHVQ DLFLRGAPIR TNIARNLALK ENVFMMVICI ELKIPLFLVG KPGSSKSLAK IIVADAMQGQ AAFSELFRCL KQVHLVSFQC SPHSTPQGII STFKQCARFQ QGKDLGQYVS VVVLDEVGLA EDSPKMPLKT LHPLLEDGCI EDDPAPYKKV GFVGISNWAL DPAKMNRGIF VSRGSPNEKE LIESAEGICS SDRLVQDKIR GYFAPFAKAY ETVCQKQDKE FFGLRDYYSL IKMVFAKAKA SKRGLSPQDI THAVLRNFSG KDNIQALSIF TASLPEARYK EEVSTVELIK QNIYPGPQAS SRGLDGAESR YLLVLTRNYV ALQILQQTFF EGQQPEIIFG SSFPQDQEYT QICRNINRVK ICMETGKMVV LLNLQNLYES LYDALNQYYV YLGGQKYVDL GLGTHRVKCR VHTAFRLIVI EEKDVVYKQF PVPLINRLEK HYLDMNTVLQ PWQKSIVQEL QQWAHEFADV KADQFIARHK YSPADVFIGY HSDACASVVL QAVERQGCRD LTEELYRKVS EEARSILLDC ATPDAVVRLS GSSLGSFTAK QLSQEYYYAQ QHNSFVDFLQ AHLRMTHHEC RAVFTEITTF SRLLTGNDCD VLASELRGLA SKPVVLSLQQ YDTEYSFLKD VRSWLTNPGK RKVLVIQADF DDGTRSAQLV ASAKYTAINE INKTQGTKDF VFVYFVTKLS RMGSGTSYVG FHGGLWRSVH IDDLRRSTIM ASDVTKLQNV TISQLFKPED KPEQEEMEIE TSQSKELAEE QMEVEDSEEM KKASDPRSCD CSQFLDTTRL VQSCVQGAVG MLRDQNESCA RNMRRVTILL DLLNEDNTRN ASFLRESKMR LHVLLNKQEE NQVRSLKEWV TREAANQDAL QEAGTFRHTL WKRVQDVVTP ILASMIAHID RDGNLELLAQ PDSPAWVQDL WMFIYSDIKF LNISLVLNNT RSNSEMSFIL VQSHMNLLKD AYNAVPFSWR IRDYLEELWV QAQYITDTEG LSKKFVEIFQ KTPLGVFLAQ FPVAQQQKLL QSYLKDFLLL TMKVSSREEL MFLQMALWSC LRELQEASGT PDETYKFPLS LPWVHLAFQH FRTRLQNFSR ILTIHPQVLS SLSQAAEKHS LAGCEMTLDA FAAMACAEML KGDLLKPSPK AWLQLVKNLS TPLELVCSEG YLCDSGSMTR SVIQEVRALW NRIFSIALFV EHVLLGTESH IPELSPLVTT YVSLLDKCLE EDSNLKTCRP FVAVMTTLCD CKDKASKKFS RFGIQPCFIC HGDAQDPVCL PCDHVYCLRC IQTWLIPGQM MCPYCLTDLP DKFSPTVSQD HRKAIEKHAQ FRHMCNSFFV DLVSTMCFKD NTPPEKSVID TLLSLLFVQK ELLRDASQKH REHTKSLSPF DDVVDQTPVI RSVLLKLLLK YSFHEVKDYI QNYLTQLEKK AFLTEDKTEL YLLFISCLED SVHQKTSAGC RNLEQVLREE GHFLRTYSPG LQGQEPVRIA SVEYLQEVAR VRLCLDLAAD FLSELQEGSE LAEDKRRFLK HVEEFCTRVN NDWHRVYLVR KLSSQRGMEF VQSFSKQGHP CQWVFPRKVI AQQKDHVSLM DRYLVHGNEY KAVRDATAKA VLECKTLDIG NALMACRSPK PQQTAYLLLA LYTEVAALYR SPNGSLHPEA KQLEAVNKFI KESKILSDPN IRCFARSLVD NTLPLLKIRS ANSILKGTVT EMAVHVATIL LCGHNQILKP LRNLAFYPVN MANAFLPTMP EDLLVHARTW RGLENVTWYT CPRGHPCSVG ECGRPMQEST CLDCGLPVGG LNHTPHEGFS AIRNNEDRTQ TGHVLGSPQS SGVAEVSDRG QSPVVFILTR LLTHLAMLVG ATHNPQALTV IIKPWVQDPQ GFLQQHIQRD LEQLTKMLGR SADETIHVVH LILSSLLRVQ SHGVLNFNAE LSTKGCRNNW EKHFETLLLR ELKHLDKNLP AINALISQDE RISSNPVTKI IYGDPATFLP HLPQKSIIHC SKIWSCRRKI TVEYLQHIVE QKNGKETVPV LWHFLQKEAE LRLVKFLPEI LALQRDLVKQ FQNVSRVEYS SIRGFIHSHS SDGLRKLLHD RITIFLSTWN ALRRSLETNG EIKLPKDYCC SDLDLDAEFE VILPRRQGLG LCGTALVSYL ISLHNNMVYT VQKFSNEDNS YSVDISEVAD LHVISYEVER DLNPLILSNC QYQVQQGGET SQEFDLEKIQ RQISSRFLQG KPRLTLKGIP TLVYRRDWNY EHLFMDIKNK MAQSSLPNLA ISTISGQLQS YSDACEALSI IEITLGFLST AGGDPGMDLN VYIEEVLRMC DQTAQVLKAF SRCQLRHIIA LWQFLSAHKS EQRLRLNKEL FREIDVQYKE ELSTQHQRLL GTFLNEAGLD AFLLELHEMI VLKLKGPRAA NSFNPNWSLK DTLVSYMETK DSDILSEVES QFPEEILMSS CISVWKIAAT RKWDRQSR //