ID ANGP2_HUMAN Reviewed; 496 AA. AC O15123; A0AV38; A8K205; B7ZLM7; Q9NRR7; Q9P2Y7; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 13-FEB-2019, entry version 163. DE RecName: Full=Angiopoietin-2; DE Short=ANG-2; DE Flags: Precursor; GN Name=ANGPT2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TEK/TIE2, AND RP FUNCTION. RC TISSUE=Lung; RX PubMed=9204896; DOI=10.1126/science.277.5322.55; RA Maisonpierre P.C., Suri C., Jones P.F., Bartunkova S., Wiegand S.J., RA Radziejewski C., Compton D.L., McClain J., Aldrich T.H., RA Papadopoulos N., Daly T.J., Davis S., Sato T.N., Yancopoulos G.D.; RT "Angiopoietin-2, a natural antagonist for Tie2 that disrupts in vivo RT angiogenesis."; RL Science 277:55-60(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=9927494; DOI=10.1172/JCI4891; RA Tanaka S., Mori M., Sakamoto Y., Makuuchi M., Sugimachi K., RA Wands J.R.; RT "Biologic significance of angiopoietin-2 expression in human RT hepatocellular carcinoma."; RL J. Clin. Invest. 103:341-345(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). RC TISSUE=Umbilical vein endothelial cell; RX PubMed=10766762; DOI=10.1074/jbc.M910084199; RA Kim I., Kim J.-H., Ryu Y.S., Jung S.H., Nah J.J., Koh G.Y.; RT "Characterization and expression of a novel alternatively spliced RT human angiopoietin-2."; RL J. Biol. Chem. 275:18550-18556(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Substantia nigra; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Colon; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP INTERACTION WITH TEK/TIE2. RX PubMed=12427764; DOI=10.1074/jbc.M208550200; RA Fiedler U., Krissl T., Koidl S., Weiss C., Koblizek T., Deutsch U., RA Martiny-Baron G., Marme D., Augustin H.G.; RT "Angiopoietin-1 and angiopoietin-2 share the same binding domains in RT the Tie-2 receptor involving the first Ig-like loop and the epidermal RT growth factor-like repeats."; RL J. Biol. Chem. 278:1721-1727(2003). RN [9] RP FUNCTION IN REGULATION OF ANGIOGENESIS; CELL SURVIVAL; CELL MIGRATION RP AND ACTIVATION OF AKT1, AND INTERACTION WITH TEK/TIE2. RX PubMed=15284220; DOI=10.1096/fj.03-1466com; RA Lee H.J., Cho C.H., Hwang S.J., Choi H.H., Kim K.T., Ahn S.Y., RA Kim J.H., Oh J.L., Lee G.M., Koh G.Y.; RT "Biological characterization of angiopoietin-3 and angiopoietin-4."; RL FASEB J. 18:1200-1208(2004). RN [10] RP FUNCTION. RX PubMed=19116766; DOI=10.1007/s10456-008-9126-0; RA Yacyshyn O.K., Lai P.F.H., Forse K., Teichert-Kuliszewska K., RA Jurasz P., Stewart D.J.; RT "Tyrosine phosphatase beta regulates angiopoietin-Tie2 signaling in RT human endothelial cells."; RL Angiogenesis 12:25-33(2009). RN [11] RP FUNCTION, AND INTERACTION WITH TEK/TIE2. RX PubMed=19223473; DOI=10.1128/MCB.01472-08; RA Yuan H.T., Khankin E.V., Karumanchi S.A., Parikh S.M.; RT "Angiopoietin 2 is a partial agonist/antagonist of Tie2 signaling in RT the endothelium."; RL Mol. Cell. Biol. 29:2011-2022(2009). RN [12] RP REVIEW. RX PubMed=19234476; DOI=10.1038/nrm2639; RA Augustin H.G., Koh G.Y., Thurston G., Alitalo K.; RT "Control of vascular morphogenesis and homeostasis through the RT angiopoietin-Tie system."; RL Nat. Rev. Mol. Cell Biol. 10:165-177(2009). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 281-496 IN COMPLEX WITH RP CALCIUM IONS, DISULFIDE BONDS, AND CALCIUM-BINDING SITES. RX PubMed=15893672; DOI=10.1016/j.str.2005.03.009; RA Barton W.A., Tzvetkova D., Nikolov D.B.; RT "Structure of the angiopoietin-2 receptor binding domain and RT identification of surfaces involved in Tie2 recognition."; RL Structure 13:825-832(2005). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.7 ANGSTROMS) OF 281-495 IN COMPLEX WITH RP CALCIUM IONS AND TEK, DISULFIDE BONDS, AND CALCIUM-BINDING SITES. RX PubMed=16732286; DOI=10.1038/nsmb1101; RA Barton W.A., Tzvetkova-Robev D., Miranda E.P., Kolev M.V., RA Rajashankar K.R., Himanen J.P., Nikolov D.B.; RT "Crystal structures of the Tie2 receptor ectodomain and the RT angiopoietin-2-Tie2 complex."; RL Nat. Struct. Mol. Biol. 13:524-532(2006). CC -!- FUNCTION: Binds to TEK/TIE2, competing for the ANGPT1 binding CC site, and modulating ANGPT1 signaling. Can induce tyrosine CC phosphorylation of TEK/TIE2 in the absence of ANGPT1. In the CC absence of angiogenic inducers, such as VEGF, ANGPT2-mediated CC loosening of cell-matrix contacts may induce endothelial cell CC apoptosis with consequent vascular regression. In concert with CC VEGF, it may facilitate endothelial cell migration and CC proliferation, thus serving as a permissive angiogenic signal. CC {ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:19116766, CC ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:9204896}. CC -!- SUBUNIT: Interacts with TEK/TIE2, competing for the same binding CC site as ANGPT1. {ECO:0000269|PubMed:12427764, CC ECO:0000269|PubMed:15284220, ECO:0000269|PubMed:16732286, CC ECO:0000269|PubMed:19223473, ECO:0000269|PubMed:9204896}. CC -!- INTERACTION: CC Q02763:TEK; NbExp=5; IntAct=EBI-15552475, EBI-2257090; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O15123-1; Sequence=Displayed; CC Name=3; CC IsoId=O15123-2; Sequence=VSP_001540; CC Name=2; CC IsoId=O15123-3; Sequence=VSP_040096; CC Note=No experimental confirmation available.; CC -!- DOMAIN: The Fibrinogen C-terminal domain mediates interaction with CC the TEK/TIE2 receptor. CC -!- WEB RESOURCE: Name=Wikipedia; Note=Angiopoietin entry; CC URL="https://en.wikipedia.org/wiki/Angiopoietin"; 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; AF004327; AAB63190.1; -; mRNA. DR EMBL; AB009865; BAA95590.1; -; mRNA. DR EMBL; AF187858; AAF76526.1; -; mRNA. DR EMBL; AK290070; BAF82759.1; -; mRNA. DR EMBL; AC018398; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471153; EAW80474.1; -; Genomic_DNA. DR EMBL; BC126200; AAI26201.1; -; mRNA. DR EMBL; BC126202; AAI26203.1; -; mRNA. DR EMBL; BC143902; AAI43903.1; -; mRNA. DR CCDS; CCDS47761.1; -. [O15123-2] DR CCDS; CCDS47762.1; -. [O15123-3] DR CCDS; CCDS5958.1; -. [O15123-1] DR RefSeq; NP_001112359.1; NM_001118887.1. [O15123-3] DR RefSeq; NP_001112360.1; NM_001118888.1. [O15123-2] DR RefSeq; NP_001138.1; NM_001147.2. [O15123-1] DR UniGene; Hs.583870; -. DR PDB; 1Z3S; X-ray; 2.35 A; A/B=281-496. DR PDB; 1Z3U; X-ray; 2.25 A; A/B/C/D=281-496. DR PDB; 2GY7; X-ray; 3.70 A; A=281-495. DR PDB; 4JZC; X-ray; 1.90 A; A=279-496. DR PDB; 4ZFG; X-ray; 2.27 A; A=277-496. DR PDBsum; 1Z3S; -. DR PDBsum; 1Z3U; -. DR PDBsum; 2GY7; -. DR PDBsum; 4JZC; -. DR PDBsum; 4ZFG; -. DR ProteinModelPortal; O15123; -. DR SMR; O15123; -. DR BioGrid; 106782; 13. DR DIP; DIP-6048N; -. DR IntAct; O15123; 7. DR MINT; O15123; -. DR STRING; 9606.ENSP00000314897; -. DR ChEMBL; CHEMBL3580489; -. DR GlyConnect; 664; -. DR iPTMnet; O15123; -. DR PhosphoSitePlus; O15123; -. DR SwissPalm; O15123; -. DR UniCarbKB; O15123; -. DR BioMuta; ANGPT2; -. DR EPD; O15123; -. DR jPOST; O15123; -. DR PaxDb; O15123; -. DR PeptideAtlas; O15123; -. DR PRIDE; O15123; -. DR ProteomicsDB; 48460; -. DR ProteomicsDB; 48461; -. [O15123-2] DR ProteomicsDB; 48462; -. [O15123-3] DR DNASU; 285; -. DR Ensembl; ENST00000325203; ENSP00000314897; ENSG00000091879. [O15123-1] DR Ensembl; ENST00000338312; ENSP00000343517; ENSG00000091879. [O15123-2] DR Ensembl; ENST00000629816; ENSP00000486858; ENSG00000091879. [O15123-3] DR GeneID; 285; -. DR KEGG; hsa:285; -. DR UCSC; uc003wqj.6; human. [O15123-1] DR CTD; 285; -. DR DisGeNET; 285; -. DR EuPathDB; HostDB:ENSG00000091879.13; -. DR GeneCards; ANGPT2; -. DR HGNC; HGNC:485; ANGPT2. DR HPA; CAB011437; -. DR HPA; CAB017626; -. DR MIM; 601922; gene. DR neXtProt; NX_O15123; -. DR OpenTargets; ENSG00000091879; -. DR PharmGKB; PA24792; -. DR eggNOG; KOG2579; Eukaryota. DR eggNOG; ENOG410ZYS4; LUCA. DR GeneTree; ENSGT00940000158430; -. DR HOGENOM; HOG000037128; -. DR HOVERGEN; HBG001644; -. DR InParanoid; O15123; -. DR KO; K05466; -. DR OMA; DLMETVH; -. DR OrthoDB; 357340at2759; -. DR PhylomeDB; O15123; -. DR TreeFam; TF336658; -. DR Reactome; R-HSA-210993; Tie2 Signaling. DR SignaLink; O15123; -. DR SIGNOR; O15123; -. DR EvolutionaryTrace; O15123; -. DR GeneWiki; ANGPT2; -. DR GenomeRNAi; 285; -. DR PRO; PR:O15123; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000091879; Expressed in 169 organ(s), highest expression level in placenta. DR ExpressionAtlas; O15123; baseline and differential. DR Genevisible; O15123; HS. DR GO; GO:0042995; C:cell projection; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB. DR GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc. DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW. DR GO; GO:0031100; P:animal organ regeneration; IEA:Ensembl. DR GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl. DR GO; GO:0007281; P:germ cell development; IEA:Ensembl. DR GO; GO:0072012; P:glomerulus vasculature development; ISS:UniProtKB. DR GO; GO:0050900; P:leukocyte migration; TAS:Reactome. DR GO; GO:0060135; P:maternal process involved in female pregnancy; IEA:Ensembl. DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0043537; P:negative regulation of blood vessel endothelial cell migration; IDA:UniProtKB. DR GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl. DR GO; GO:0050928; P:negative regulation of positive chemotaxis; IDA:UniProtKB. DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl. DR GO; GO:0014823; P:response to activity; IEA:Ensembl. DR GO; GO:0009749; P:response to glucose; IEA:Ensembl. DR GO; GO:0001666; P:response to hypoxia; IEA:Ensembl. DR GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl. DR GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl. DR GO; GO:0009314; P:response to radiation; IEA:Ensembl. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR GO; GO:0048014; P:Tie signaling pathway; IDA:UniProtKB. DR CDD; cd00087; FReD; 1. DR Gene3D; 3.90.215.10; -; 1. DR Gene3D; 4.10.530.10; -; 1. DR InterPro; IPR028844; Ang-2. DR InterPro; IPR036056; Fibrinogen-like_C. DR InterPro; IPR014716; Fibrinogen_a/b/g_C_1. DR InterPro; IPR014715; Fibrinogen_a/b/g_C_2. DR InterPro; IPR002181; Fibrinogen_a/b/g_C_dom. DR InterPro; IPR020837; Fibrinogen_CS. DR PANTHER; PTHR19143:SF199; PTHR19143:SF199; 1. DR Pfam; PF00147; Fibrinogen_C; 1. DR SMART; SM00186; FBG; 1. DR SUPFAM; SSF56496; SSF56496; 1. DR PROSITE; PS00514; FIBRINOGEN_C_1; 1. DR PROSITE; PS51406; FIBRINOGEN_C_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Angiogenesis; Calcium; KW Coiled coil; Complete proteome; Developmental protein; KW Differentiation; Disulfide bond; Glycoprotein; Metal-binding; KW Polymorphism; Reference proteome; Secreted; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 496 Angiopoietin-2. FT /FTId=PRO_0000009113. FT DOMAIN 275 495 Fibrinogen C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00739}. FT COILED 166 248 {ECO:0000255}. FT METAL 429 429 Calcium. {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT METAL 431 431 Calcium. {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT METAL 433 433 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT METAL 435 435 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT CARBOHYD 89 89 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 119 119 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 133 133 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 151 151 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 240 240 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 304 304 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT DISULFID 284 313 {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT DISULFID 433 435 {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT DISULFID 437 450 {ECO:0000244|PDB:1Z3U, FT ECO:0000269|PubMed:15893672, FT ECO:0000269|PubMed:16732286}. FT VAR_SEQ 97 148 Missing (in isoform 3). FT {ECO:0000303|PubMed:10766762}. FT /FTId=VSP_001540. FT VAR_SEQ 268 268 Missing (in isoform 2). FT {ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9927494}. FT /FTId=VSP_040096. FT VARIANT 333 333 V -> I (in dbSNP:rs7813215). FT /FTId=VAR_049069. FT STRAND 281 283 {ECO:0000244|PDB:4JZC}. FT HELIX 284 289 {ECO:0000244|PDB:4JZC}. FT STRAND 296 301 {ECO:0000244|PDB:4JZC}. FT STRAND 308 314 {ECO:0000244|PDB:4JZC}. FT HELIX 317 319 {ECO:0000244|PDB:4ZFG}. FT STRAND 322 331 {ECO:0000244|PDB:4JZC}. FT HELIX 339 344 {ECO:0000244|PDB:4JZC}. FT STRAND 351 354 {ECO:0000244|PDB:4JZC}. FT HELIX 357 364 {ECO:0000244|PDB:4JZC}. FT STRAND 369 376 {ECO:0000244|PDB:4JZC}. FT STRAND 378 380 {ECO:0000244|PDB:1Z3U}. FT STRAND 382 392 {ECO:0000244|PDB:4JZC}. FT HELIX 395 397 {ECO:0000244|PDB:4JZC}. FT STRAND 401 410 {ECO:0000244|PDB:4JZC}. FT STRAND 431 435 {ECO:0000244|PDB:4JZC}. FT HELIX 437 441 {ECO:0000244|PDB:4JZC}. FT STRAND 448 450 {ECO:0000244|PDB:4JZC}. FT STRAND 452 454 {ECO:0000244|PDB:4JZC}. FT STRAND 471 474 {ECO:0000244|PDB:4ZFG}. FT HELIX 475 478 {ECO:0000244|PDB:4JZC}. FT STRAND 485 493 {ECO:0000244|PDB:4JZC}. SQ SEQUENCE 496 AA; 56919 MW; 5642A58847A7385C CRC64; MWQIVFFTLS CDLVLAAAYN NFRKSMDSIG KKQYQVQHGS CSYTFLLPEM DNCRSSSSPY VSNAVQRDAP LEYDDSVQRL QVLENIMENN TQWLMKLENY IQDNMKKEMV EIQQNAVQNQ TAVMIEIGTN LLNQTAEQTR KLTDVEAQVL NQTTRLELQL LEHSLSTNKL EKQILDQTSE INKLQDKNSF LEKKVLAMED KHIIQLQSIK EEKDQLQVLV SKQNSIIEEL EKKIVTATVN NSVLQKQQHD LMETVNNLLT MMSTSNSAKD PTVAKEEQIS FRDCAEVFKS GHTTNGIYTL TFPNSTEEIK AYCDMEAGGG GWTIIQRRED GSVDFQRTWK EYKVGFGNPS GEYWLGNEFV SQLTNQQRYV LKIHLKDWEG NEAYSLYEHF YLSSEELNYR IHLKGLTGTA GKISSISQPG NDFSTKDGDN DKCICKCSQM LTGGWWFDAC GPSNLNGMYY PQRQNTNKFN GIKWYYWKGS GYSLKATTMM IRPADF //