ID FCN3_HUMAN Reviewed; 299 AA. AC O75636; Q6IBJ5; Q8WW86; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 07-MAR-2006, sequence version 2. DT 13-FEB-2019, entry version 190. DE RecName: Full=Ficolin-3; DE AltName: Full=Collagen/fibrinogen domain-containing lectin 3 p35; DE AltName: Full=Collagen/fibrinogen domain-containing protein 3; DE AltName: Full=Hakata antigen; DE Flags: Precursor; GN Name=FCN3; Synonyms=FCNH, HAKA1; 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), PARTIAL PROTEIN SEQUENCE, AND RP HYDROXYLATION AT PRO-50; PRO-53; PRO-59; PRO-65; PRO-68 AND PRO-77. RC TISSUE=Lung; RX PubMed=9694814; DOI=10.1074/jbc.273.33.20721; RA Sugimoto R., Yae Y., Akaiwa M., Kitajima S., Shibata Y., Sato H., RA Hirata J., Okochi K., Izuhara K., Hamasaki N.; RT "Cloning and characterization of the Hakata antigen, a member of the RT ficolin/opsonin p35 lectin family."; RL J. Biol. Chem. 273:20721-20727(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Placenta; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RG SeattleSNPs variation discovery resource; RL Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; 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 [7] RP PROTEIN SEQUENCE OF 24-38. RX PubMed=15340161; DOI=10.1110/ps.04682504; RA Zhang Z., Henzel W.J.; RT "Signal peptide prediction based on analysis of experimentally RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [8] RP TISSUE SPECIFICITY. RX PubMed=10330454; DOI=10.1177/002215549904700607; RA Akaiwa M., Yae Y., Sugimoto R., Suzuki S.O., Iwaki T., Izuhara K., RA Hamasaki N.; RT "Hakata antigen, a new member of the ficolin/opsonin p35 family, is a RT novel human lectin secreted into bronchus/alveolus and bile."; RL J. Histochem. Cytochem. 47:777-786(1999). RN [9] RP FUNCTION, AND INTERACTION WITH MASP1 AND MASP2. RX PubMed=11907111; DOI=10.4049/jimmunol.168.7.3502; RA Matsushita M., Kuraya M., Hamasaki N., Tsujimura M., Shiraki H., RA Fujita T.; RT "Activation of the lectin complement pathway by H-ficolin (Hakata RT antigen)."; RL J. Immunol. 168:3502-3506(2002). RN [10] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189. RC TISSUE=Plasma; RX PubMed=16335952; DOI=10.1021/pr0502065; RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., RA Moore R.J., Smith R.D.; RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, RT hydrazide chemistry, and mass spectrometry."; RL J. Proteome Res. 4:2070-2080(2005). RN [11] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-189. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [12] RP GLYCOSYLATION AT ASN-189. RX PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200; RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., RA Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., RA Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.; RT "A strategy for precise and large scale identification of core RT fucosylated glycoproteins."; RL Mol. Cell. Proteomics 8:913-923(2009). RN [13] RP INVOLVEMENT IN FCN3D. RX PubMed=19535802; DOI=10.1056/NEJMoa0900381; RA Munthe-Fog L., Hummelshoj T., Honore C., Madsen H.O., Permin H., RA Garred P.; RT "Immunodeficiency associated with FCN3 mutation and ficolin-3 RT deficiency."; RL N. Engl. J. Med. 360:2637-2644(2009). RN [14] RP 3D-STRUCTURE MODELING. RA Mallena S.C., Yadugiri K.; RT "In silico designed structure of ficolin precursor."; RL Submitted (NOV-2002) to the PDB data bank. RN [15] RP X-RAY CRYSTALLOGRAPHY (1.73 ANGSTROMS) OF 79-299 IN COMPLEX WITH RP CALCIUM AND GALACTOSE, DISULFIDE BONDS, SUBUNIT, AND FUNCTION. RX PubMed=17215869; DOI=10.1038/sj.emboj.7601500; RA Garlatti V., Belloy N., Martin L., Lacroix M., Matsushita M., Endo Y., RA Fujita T., Fontecilla-Camps J.C., Arlaud G.J., Thielens N.M., RA Gaboriaud C.; RT "Structural insights into the innate immune recognition specificities RT of L- and H-ficolins."; RL EMBO J. 26:623-633(2007). CC -!- FUNCTION: May function in innate immunity through activation of CC the lectin complement pathway. Calcium-dependent and GlcNAc- CC binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as CC mono/oligosaccharide and lipopolysaccharides from S.typhimurium CC and S.minnesota. {ECO:0000269|PubMed:11907111, CC ECO:0000269|PubMed:17215869}. CC -!- SUBUNIT: Homotrimer (PubMed:17215869). May form an octadecamer CC consisting of an elementary trimer unit. Does not interact with CC fibronectin, elastin or zymosan. Interacts with MASP1 and MASP2. CC {ECO:0000269|PubMed:11907111, ECO:0000269|PubMed:17215869}. CC -!- SUBCELLULAR LOCATION: Secreted. Note=Found in blood plasma, CC bronchus, alveolus and bile duct. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=O75636-1; Sequence=Displayed; CC Name=2; CC IsoId=O75636-2; Sequence=VSP_001541; CC -!- TISSUE SPECIFICITY: Liver and lung. In liver it is produced by CC bile duct epithelial cells and hepatocytes. In lung it is produced CC by both ciliated bronchial epithelial cells and type II alveolar CC epithelial cells. {ECO:0000269|PubMed:10330454}. CC -!- PTM: The N-terminus is blocked. CC -!- DISEASE: Ficolin 3 deficiency (FCN3D) [MIM:613860]: A disorder CC characterized by immunodeficiency, recurrent infections, brain CC abscesses and recurrent warts on the fingers. Affected individuals CC have normal levels of lymphocytes, normal T-cell responses, and CC normal antibodies, but a selective deficient antibody response to CC pneumococcal polysaccharide vaccine. CC {ECO:0000269|PubMed:19535802}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ficolin lectin family. {ECO:0000305}. CC -!- WEB RESOURCE: Name=SeattleSNPs; CC URL="http://pga.gs.washington.edu/data/fcn3/"; 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; D88587; BAA32277.1; -; mRNA. DR EMBL; AK075140; BAC11429.1; -; mRNA. DR EMBL; CR456808; CAG33089.1; -; mRNA. DR EMBL; AY756173; AAU85296.1; -; Genomic_DNA. DR EMBL; FO393419; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC020731; AAH20731.1; -; mRNA. DR CCDS; CCDS300.1; -. [O75636-1] DR CCDS; CCDS301.1; -. [O75636-2] DR RefSeq; NP_003656.2; NM_003665.3. [O75636-1] DR RefSeq; NP_775628.1; NM_173452.2. [O75636-2] DR UniGene; Hs.333383; -. DR PDB; 1LA5; Model; -; A=1-299. DR PDB; 2J5Z; X-ray; 1.73 A; A/B/C=79-299. DR PDB; 2J60; X-ray; 1.80 A; A/B/C=79-299. DR PDB; 2J64; X-ray; 2.20 A; A/B/C=79-299. DR PDBsum; 1LA5; -. DR PDBsum; 2J5Z; -. DR PDBsum; 2J60; -. DR PDBsum; 2J64; -. DR ProteinModelPortal; O75636; -. DR SMR; O75636; -. DR BioGrid; 114117; 1. DR IntAct; O75636; 1. DR STRING; 9606.ENSP00000270879; -. DR UniLectin; O75636; -. DR GlyConnect; 1247; -. DR iPTMnet; O75636; -. DR PhosphoSitePlus; O75636; -. DR BioMuta; FCN3; -. DR jPOST; O75636; -. DR PaxDb; O75636; -. DR PeptideAtlas; O75636; -. DR PRIDE; O75636; -. DR ProteomicsDB; 50132; -. DR ProteomicsDB; 50133; -. [O75636-2] DR DNASU; 8547; -. DR Ensembl; ENST00000270879; ENSP00000270879; ENSG00000142748. [O75636-1] DR Ensembl; ENST00000354982; ENSP00000347077; ENSG00000142748. [O75636-2] DR GeneID; 8547; -. DR KEGG; hsa:8547; -. DR UCSC; uc001boa.4; human. [O75636-1] DR CTD; 8547; -. DR DisGeNET; 8547; -. DR EuPathDB; HostDB:ENSG00000142748.12; -. DR GeneCards; FCN3; -. DR HGNC; HGNC:3625; FCN3. DR HPA; CAB025945; -. DR MalaCards; FCN3; -. DR MIM; 604973; gene. DR MIM; 613860; phenotype. DR neXtProt; NX_O75636; -. DR OpenTargets; ENSG00000142748; -. DR Orphanet; 331190; Immunodeficiency due to ficolin3 deficiency. DR PharmGKB; PA28071; -. DR eggNOG; KOG2579; Eukaryota. DR eggNOG; ENOG410ZYS4; LUCA. DR GeneTree; ENSGT00940000163188; -. DR HOGENOM; HOG000037127; -. DR HOVERGEN; HBG001644; -. DR InParanoid; O75636; -. DR KO; K10104; -. DR OMA; RPWSSYK; -. DR OrthoDB; 1035379at2759; -. DR PhylomeDB; O75636; -. DR TreeFam; TF351983; -. DR Reactome; R-HSA-166662; Lectin pathway of complement activation. DR Reactome; R-HSA-166663; Initial triggering of complement. DR Reactome; R-HSA-2855086; Ficolins bind to repetitive carbohydrate structures on the target cell surface. DR ChiTaRS; FCN3; human. DR EvolutionaryTrace; O75636; -. DR GeneWiki; FCN3; -. DR GenomeRNAi; 8547; -. DR PRO; PR:O75636; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; ENSG00000142748; Expressed in 106 organ(s), highest expression level in right lung. DR Genevisible; O75636; HS. DR GO; GO:0072562; C:blood microparticle; HDA:UniProtKB. DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:0003823; F:antigen binding; IDA:UniProtKB. DR GO; GO:0030246; F:carbohydrate binding; TAS:ProtInc. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0006956; P:complement activation; IDA:UniProtKB. DR GO; GO:0001867; P:complement activation, lectin pathway; IDA:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:1902679; P:negative regulation of RNA biosynthetic process; IDA:UniProtKB. DR GO; GO:0046597; P:negative regulation of viral entry into host cell; IMP:UniProtKB. DR GO; GO:0043654; P:recognition of apoptotic cell; IDA:UniProtKB. DR CDD; cd00087; FReD; 1. DR Gene3D; 3.90.215.10; -; 1. DR Gene3D; 4.10.530.10; -; 1. 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 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; Calcium; Collagen; KW Complement activation lectin pathway; Complete proteome; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Hydroxylation; Immunity; Innate immunity; Lectin; Metal-binding; KW Reference proteome; Repeat; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000269|PubMed:15340161}. FT CHAIN 24 299 Ficolin-3. FT /FTId=PRO_0000009142. FT DOMAIN 48 80 Collagen-like. FT DOMAIN 84 299 Fibrinogen C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00739}. FT REGION 258 259 Carbohydrate binding. FT {ECO:0000305|PubMed:17215869}. FT METAL 237 237 Calcium. {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT METAL 239 239 Calcium. {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT METAL 241 241 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT METAL 243 243 Calcium; via carbonyl oxygen. FT {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT MOD_RES 50 50 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT MOD_RES 53 53 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT MOD_RES 59 59 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT MOD_RES 65 65 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT MOD_RES 68 68 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT MOD_RES 77 77 Hydroxyproline. FT {ECO:0000269|PubMed:9694814}. FT CARBOHYD 189 189 N-linked (GlcNAc...) (complex) FT asparagine. {ECO:0000269|PubMed:16335952, FT ECO:0000269|PubMed:19139490, FT ECO:0000269|PubMed:19159218}. FT DISULFID 86 110 {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT DISULFID 93 121 {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT DISULFID 245 258 {ECO:0000244|PDB:2J5Z, FT ECO:0000244|PDB:2J60, FT ECO:0000269|PubMed:17215869}. FT VAR_SEQ 79 89 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_001541. FT CONFLICT 271 271 E -> D (in Ref. 1; BAA32277 and 6; FT AAH20731). {ECO:0000305}. FT HELIX 93 98 {ECO:0000244|PDB:2J5Z}. FT STRAND 103 110 {ECO:0000244|PDB:2J5Z}. FT STRAND 116 122 {ECO:0000244|PDB:2J5Z}. FT HELIX 125 127 {ECO:0000244|PDB:2J5Z}. FT STRAND 130 139 {ECO:0000244|PDB:2J5Z}. FT HELIX 147 152 {ECO:0000244|PDB:2J5Z}. FT STRAND 154 156 {ECO:0000244|PDB:2J5Z}. FT HELIX 165 172 {ECO:0000244|PDB:2J5Z}. FT STRAND 173 175 {ECO:0000244|PDB:2J5Z}. FT STRAND 178 184 {ECO:0000244|PDB:2J5Z}. FT STRAND 190 196 {ECO:0000244|PDB:2J5Z}. FT STRAND 198 200 {ECO:0000244|PDB:2J5Z}. FT HELIX 203 205 {ECO:0000244|PDB:2J5Z}. FT STRAND 209 211 {ECO:0000244|PDB:2J5Z}. FT STRAND 214 216 {ECO:0000244|PDB:2J60}. FT HELIX 224 226 {ECO:0000244|PDB:2J5Z}. FT STRAND 239 243 {ECO:0000244|PDB:2J5Z}. FT HELIX 245 249 {ECO:0000244|PDB:2J5Z}. FT STRAND 256 258 {ECO:0000244|PDB:2J5Z}. FT STRAND 269 271 {ECO:0000244|PDB:2J5Z}. FT TURN 282 285 {ECO:0000244|PDB:2J5Z}. FT STRAND 292 299 {ECO:0000244|PDB:2J5Z}. SQ SEQUENCE 299 AA; 32903 MW; 5CB8A7D3668FA364 CRC64; MDLLWILPSL WLLLLGGPAC LKTQEHPSCP GPRELEASKV VLLPSCPGAP GSPGEKGAPG PQGPPGPPGK MGPKGEPGDP VNLLRCQEGP RNCRELLSQG ATLSGWYHLC LPEGRALPVF CDMDTEGGGW LVFQRRQDGS VDFFRSWSSY RAGFGNQESE FWLGNENLHQ LTLQGNWELR VELEDFNGNR TFAHYATFRL LGEVDHYQLA LGKFSEGTAG DSLSLHSGRP FTTYDADHDS SNSNCAVIVH GAWWYASCYR SNLNGRYAVS EAAAHKYGID WASGRGVGHP YRRVRMMLR //