ID CFAD_HUMAN Reviewed; 253 AA. AC P00746; B4DV76; Q5U5S1; Q86VJ5; Q8N4E0; Q8WZB4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 5. DT 13-FEB-2019, entry version 200. DE RecName: Full=Complement factor D; DE EC=3.4.21.46; DE AltName: Full=Adipsin; DE AltName: Full=C3 convertase activator; DE AltName: Full=Properdin factor D; DE Flags: Precursor; GN Name=CFD; Synonyms=DF, PFD; 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]. RA Relle M.; RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Small intestine; 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 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Placenta, Skin, Spleen, and Testis; 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-253. RX PubMed=1374388; RA White R.T., Damm D., Hancock N., Rosen B.S., Lowell B.B., Usher P., RA Flier J.S., Spiegelman B.M.; RT "Human adipsin is identical to complement factor D and is expressed at RT high levels in adipose tissue."; RL J. Biol. Chem. 267:9210-9213(1992). RN [6] RP PROTEIN SEQUENCE OF 26-252. RX PubMed=6383466; DOI=10.1021/bi00306a025; RA Niemann M.A., Bhown A.S., Bennett J.C., Volanakis J.E.; RT "Amino acid sequence of human D of the alternative complement RT pathway."; RL Biochemistry 23:2482-2486(1984). RN [7] RP PROTEIN SEQUENCE OF 26-252. RX PubMed=6363133; DOI=10.1016/0014-5793(84)80110-6; RA Johnson D.M.A., Gagnon J., Reid K.B.M.; RT "Amino acid sequence of human factor D of the complement system. RT Similarity in sequence between factor D and proteases of non-plasma RT origin."; RL FEBS Lett. 166:347-351(1984). RN [8] RP PROTEIN SEQUENCE OF 26-82. RX PubMed=6987665; DOI=10.1073/pnas.77.2.1116; RA Volanakis J.E., Bhown A.S., Bennett J.C., Mole J.E.; RT "Partial amino acid sequence of human factor D: homology with serine RT proteases."; RL Proc. Natl. Acad. Sci. U.S.A. 77:1116-1119(1980). RN [9] RP PROTEIN SEQUENCE OF 26-78. RX PubMed=6776531; DOI=10.1073/pnas.77.8.4938; RA Davis A.E. III; RT "Active site amino acid sequence of human factor D."; RL Proc. Natl. Acad. Sci. U.S.A. 77:4938-4942(1980). RN [10] RP PROTEIN SEQUENCE OF 26-61 AND 194-220. RX PubMed=6821372; DOI=10.1042/bj1870863; RA Johnson D.M.A., Gagnon J., Reid K.B.M.; RT "Factor D of the alternative pathway of human complement. RT Purification, alignment and N-terminal amino acid sequences of the RT major cyanogen bromide fragments, and localization of the serine RT residue at the active site."; RL Biochem. J. 187:863-874(1980). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., RA Fischer-Posovszky P., Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion RT profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=8289289; DOI=10.1006/jmbi.1994.1021; RA Narayana S.V.L., Carson M., El-Kabbani O., Kilpatrick J.M., Moore D., RA Chen X., Bugg C.E., Volanakis J.E., Delucas L.J.; RT "Structure of human factor D. A complement system protein at 2.0-A RT resolution."; RL J. Mol. Biol. 235:695-708(1994). RN [13] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=7592653; DOI=10.1074/jbc.270.41.24399; RA Kim S., Narayana S.V., Volanakis J.E.; RT "Crystal structure of a complement factor D mutant expressing enhanced RT catalytic activity."; RL J. Biol. Chem. 270:24399-24405(1995). RN [14] RP VARIANTS CFDD DEFICIENCY GLY-213 AND ARG-214. RX PubMed=16527897; DOI=10.1182/blood-2005-07-2820; RA Sprong T., Roos D., Weemaes C., Neeleman C., Geesing C.L., RA Mollnes T.E., van Deuren M.; RT "Deficient alternative complement pathway activation due to factor D RT deficiency by 2 novel mutations in the complement factor D gene in a RT family with meningococcal infections."; RL Blood 107:4865-4870(2006). CC -!- FUNCTION: Factor D cleaves factor B when the latter is complexed CC with factor C3b, activating the C3bbb complex, which then becomes CC the C3 convertase of the alternate pathway. Its function is CC homologous to that of C1s in the classical pathway. CC -!- CATALYTIC ACTIVITY: CC Reaction=Selective cleavage of Arg-|-Lys bond in complement factor CC B when in complex with complement subcomponent C3b or with cobra CC venom factor.; EC=3.4.21.46; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- DISEASE: Complement factor D deficiency (CFDD) [MIM:613912]: An CC immunologic disorder characterized by increased susceptibility to CC bacterial infections, particularly Neisseria infections, due to a CC defect in the alternative complement pathway. CC {ECO:0000269|PubMed:16527897}. Note=The disease is caused by CC mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the peptidase S1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00274}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA35527.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=CFDbase; Note=CFD mutation db; CC URL="http://structure.bmc.lu.se/idbase/CFDbase/"; 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; AJ313463; CAC48304.1; -; mRNA. DR EMBL; AK300963; BAG62588.1; -; mRNA. DR EMBL; CH471139; EAW69588.1; -; Genomic_DNA. DR EMBL; BC034529; AAH34529.1; -; mRNA. DR EMBL; BC040146; AAH40146.1; -; mRNA. DR EMBL; BC051001; AAH51001.1; -; mRNA. DR EMBL; BC057807; AAH57807.1; -; mRNA. DR EMBL; M84526; AAA35527.1; ALT_INIT; mRNA. DR CCDS; CCDS12046.1; -. DR PIR; A40197; DBHU. DR RefSeq; NP_001304264.1; NM_001317335.1. DR RefSeq; NP_001919.2; NM_001928.3. DR UniGene; Hs.155597; -. DR PDB; 1BIO; X-ray; 1.50 A; A=26-253. DR PDB; 1DFP; X-ray; 2.40 A; A/B=26-253. DR PDB; 1DIC; X-ray; 1.80 A; A=26-253. DR PDB; 1DST; X-ray; 2.00 A; A=26-253. DR PDB; 1DSU; X-ray; 2.00 A; A/B=26-253. DR PDB; 1FDP; X-ray; 2.10 A; A/B/C/D=19-253. DR PDB; 1HFD; X-ray; 2.30 A; A=26-253. DR PDB; 2XW9; X-ray; 1.20 A; A=26-253. DR PDB; 2XWA; X-ray; 2.80 A; A/B=26-253. DR PDB; 2XWB; X-ray; 3.49 A; I/J=26-253. DR PDB; 4CBN; X-ray; 1.80 A; A/B=26-253. DR PDB; 4CBO; X-ray; 1.80 A; A/B=26-253. DR PDB; 4D9R; X-ray; 2.42 A; A/B=26-253. DR PDB; 5FBE; X-ray; 1.43 A; A=26-253. DR PDB; 5FBI; X-ray; 1.47 A; A=26-253. DR PDB; 5FCK; X-ray; 1.86 A; A=26-253. DR PDB; 5MT0; X-ray; 1.29 A; A=26-253. DR PDB; 5MT4; X-ray; 1.65 A; A=26-253. DR PDB; 5NAR; X-ray; 1.55 A; A=26-253. DR PDB; 5NAT; X-ray; 1.17 A; A=26-253. DR PDB; 5NAW; X-ray; 1.25 A; A=26-253. DR PDB; 5NB6; X-ray; 1.75 A; A=26-253. DR PDB; 5NB7; X-ray; 1.33 A; A=26-253. DR PDB; 5NBA; X-ray; 1.87 A; A=26-253. DR PDB; 5TCA; X-ray; 3.15 A; A/B/C/D/E/F/G=26-253. DR PDB; 5TCC; X-ray; 3.37 A; A/B/C/D/E/F/G=26-253. DR PDB; 6FTY; X-ray; 1.67 A; A=26-253. DR PDB; 6FTZ; X-ray; 1.67 A; A=26-253. DR PDB; 6FUG; X-ray; 2.21 A; A/B/C/D/E/F=26-253. DR PDB; 6FUH; X-ray; 1.37 A; A=26-253. DR PDB; 6FUI; X-ray; 1.38 A; A=26-253. DR PDB; 6FUJ; X-ray; 2.25 A; A/B/C/D/E/F=26-253. DR PDB; 6FUT; X-ray; 1.50 A; A=26-253. DR PDBsum; 1BIO; -. DR PDBsum; 1DFP; -. DR PDBsum; 1DIC; -. DR PDBsum; 1DST; -. DR PDBsum; 1DSU; -. DR PDBsum; 1FDP; -. DR PDBsum; 1HFD; -. DR PDBsum; 2XW9; -. DR PDBsum; 2XWA; -. DR PDBsum; 2XWB; -. DR PDBsum; 4CBN; -. DR PDBsum; 4CBO; -. DR PDBsum; 4D9R; -. DR PDBsum; 5FBE; -. DR PDBsum; 5FBI; -. DR PDBsum; 5FCK; -. DR PDBsum; 5MT0; -. DR PDBsum; 5MT4; -. DR PDBsum; 5NAR; -. DR PDBsum; 5NAT; -. DR PDBsum; 5NAW; -. DR PDBsum; 5NB6; -. DR PDBsum; 5NB7; -. DR PDBsum; 5NBA; -. DR PDBsum; 5TCA; -. DR PDBsum; 5TCC; -. DR PDBsum; 6FTY; -. DR PDBsum; 6FTZ; -. DR PDBsum; 6FUG; -. DR PDBsum; 6FUH; -. DR PDBsum; 6FUI; -. DR PDBsum; 6FUJ; -. DR PDBsum; 6FUT; -. DR ProteinModelPortal; P00746; -. DR SMR; P00746; -. DR BioGrid; 108039; 2. DR IntAct; P00746; 2. DR STRING; 9606.ENSP00000332139; -. DR BindingDB; P00746; -. DR ChEMBL; CHEMBL2176771; -. DR DrugBank; DB03058; 2-Aminobenzyl alcohol. DR GuidetoPHARMACOLOGY; 2842; -. DR MEROPS; S01.191; -. DR iPTMnet; P00746; -. DR PhosphoSitePlus; P00746; -. DR BioMuta; CFD; -. DR DMDM; 158515408; -. DR jPOST; P00746; -. DR PaxDb; P00746; -. DR PeptideAtlas; P00746; -. DR PRIDE; P00746; -. DR ProteomicsDB; 51276; -. DR Ensembl; ENST00000327726; ENSP00000332139; ENSG00000197766. DR Ensembl; ENST00000617994; ENSP00000478745; ENSG00000274619. DR GeneID; 1675; -. DR KEGG; hsa:1675; -. DR UCSC; uc002lqc.4; human. DR CTD; 1675; -. DR DisGeNET; 1675; -. DR EuPathDB; HostDB:ENSG00000197766.7; -. DR GeneCards; CFD; -. DR HGNC; HGNC:2771; CFD. DR HPA; HPA052799; -. DR MalaCards; CFD; -. DR MIM; 134350; gene. DR MIM; 613912; phenotype. DR neXtProt; NX_P00746; -. DR OpenTargets; ENSG00000197766; -. DR Orphanet; 169467; Recurrent Neisseria infections due to factor D deficiency. DR PharmGKB; PA142; -. DR eggNOG; KOG3627; Eukaryota. DR eggNOG; COG5640; LUCA. DR GeneTree; ENSGT00940000162255; -. DR HOVERGEN; HBG013304; -. DR InParanoid; P00746; -. DR KO; K01334; -. DR OrthoDB; 1383895at2759; -. DR PhylomeDB; P00746; -. DR TreeFam; TF333630; -. DR BRENDA; 3.4.21.46; 2681. DR Reactome; R-HSA-114608; Platelet degranulation. DR Reactome; R-HSA-173736; Alternative complement activation. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR ChiTaRS; CFD; human. DR EvolutionaryTrace; P00746; -. DR GenomeRNAi; 1675; -. DR PRO; PR:P00746; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000197766; Expressed in 194 organ(s), highest expression level in adipose tissue of abdominal region. DR ExpressionAtlas; P00746; baseline and differential. DR Genevisible; P00746; HS. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005576; C:extracellular region; TAS:Reactome. DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome. DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome. DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome. DR GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome. DR GO; GO:0008236; F:serine-type peptidase activity; TAS:ProtInc. DR GO; GO:0006956; P:complement activation; TAS:ProtInc. DR GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome. DR GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome. DR GO; GO:0002576; P:platelet degranulation; TAS:Reactome. DR GO; GO:0006508; P:proteolysis; TAS:ProtInc. DR CDD; cd00190; Tryp_SPc; 1. DR InterPro; IPR037561; Complement_factor_D. DR InterPro; IPR009003; Peptidase_S1_PA. DR InterPro; IPR001314; Peptidase_S1A. DR InterPro; IPR001254; Trypsin_dom. DR InterPro; IPR018114; TRYPSIN_HIS. DR InterPro; IPR033116; TRYPSIN_SER. DR PANTHER; PTHR43890:SF17; PTHR43890:SF17; 1. DR Pfam; PF00089; Trypsin; 1. DR PRINTS; PR00722; CHYMOTRYPSIN. DR SMART; SM00020; Tryp_SPc; 1. DR SUPFAM; SSF50494; SSF50494; 1. DR PROSITE; PS50240; TRYPSIN_DOM; 1. DR PROSITE; PS00134; TRYPSIN_HIS; 1. DR PROSITE; PS00135; TRYPSIN_SER; 1. PE 1: Evidence at protein level; KW 3D-structure; Complement alternate pathway; Complete proteome; KW Direct protein sequencing; Disease mutation; Disulfide bond; KW Hydrolase; Immunity; Innate immunity; Polymorphism; Protease; KW Reference proteome; Secreted; Serine protease; Signal; Zymogen. FT SIGNAL 1 20 {ECO:0000255}. FT PROPEP 21 25 Activation peptide. {ECO:0000255}. FT /FTId=PRO_0000027560. FT CHAIN 26 253 Complement factor D. FT /FTId=PRO_0000027561. FT DOMAIN 26 253 Peptidase S1. {ECO:0000255|PROSITE- FT ProRule:PRU00274}. FT ACT_SITE 66 66 Charge relay system. FT ACT_SITE 114 114 Charge relay system. FT ACT_SITE 208 208 Charge relay system. FT DISULFID 51 67 FT DISULFID 148 214 FT DISULFID 179 195 FT DISULFID 204 229 FT VARIANT 213 213 V -> G (in CFDD; dbSNP:rs267606720). FT {ECO:0000269|PubMed:16527897}. FT /FTId=VAR_034866. FT VARIANT 214 214 C -> R (in CFDD; dbSNP:rs267606721). FT {ECO:0000269|PubMed:16527897}. FT /FTId=VAR_034867. FT VARIANT 248 248 I -> M (in dbSNP:rs2230216). FT /FTId=VAR_034868. FT CONFLICT 21 21 P -> R (in Ref. 5; AAA35527). FT {ECO:0000305}. FT CONFLICT 26 26 I -> M (in Ref. 5; AAA35527). FT {ECO:0000305}. FT CONFLICT 35 35 H -> F (in Ref. 8; AA sequence). FT {ECO:0000305}. FT CONFLICT 40 40 M -> V (in Ref. 8; AA sequence). FT {ECO:0000305}. FT CONFLICT 49 49 H -> E (in Ref. 7; AA sequence and 10; AA FT sequence). {ECO:0000305}. FT CONFLICT 52 52 G -> A (in Ref. 5; AAA35527). FT {ECO:0000305}. FT CONFLICT 59 59 Q -> R (in Ref. 5; AAA35527). FT {ECO:0000305}. FT CONFLICT 63 63 S -> T (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 73 73 D -> G (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 83 86 HSLS -> THLP (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 83 84 HS -> ST (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 94 95 Missing (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 96 96 D -> E (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 136 136 Q -> G (in Ref. 7; AA sequence). FT {ECO:0000305}. FT CONFLICT 178 191 TCNRRTHHDGAITE -> KCRLYDVL (in Ref. 7; AA FT sequence). {ECO:0000305}. FT CONFLICT 243 243 S -> T (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 250 250 S -> H (in Ref. 6; AA sequence). FT {ECO:0000305}. FT CONFLICT 250 250 Missing (in Ref. 7; AA sequence). FT {ECO:0000305}. FT STRAND 30 32 {ECO:0000244|PDB:1FDP}. FT STRAND 40 45 {ECO:0000244|PDB:5NAT}. FT STRAND 48 57 {ECO:0000244|PDB:5NAT}. FT STRAND 60 63 {ECO:0000244|PDB:5NAT}. FT HELIX 65 68 {ECO:0000244|PDB:5NAT}. FT TURN 69 71 {ECO:0000244|PDB:5TCA}. FT STRAND 72 74 {ECO:0000244|PDB:1BIO}. FT STRAND 76 81 {ECO:0000244|PDB:5NAT}. FT STRAND 83 87 {ECO:0000244|PDB:5NAT}. FT STRAND 93 102 {ECO:0000244|PDB:5NAT}. FT HELIX 108 113 {ECO:0000244|PDB:1DSU}. FT STRAND 116 122 {ECO:0000244|PDB:5NAT}. FT STRAND 127 129 {ECO:0000244|PDB:4D9R}. FT STRAND 147 154 {ECO:0000244|PDB:5NAT}. FT TURN 156 159 {ECO:0000244|PDB:4CBO}. FT STRAND 167 174 {ECO:0000244|PDB:5NAT}. FT HELIX 176 179 {ECO:0000244|PDB:5NAT}. FT TURN 182 187 {ECO:0000244|PDB:5NAT}. FT STRAND 193 196 {ECO:0000244|PDB:5NAT}. FT STRAND 199 202 {ECO:0000244|PDB:5NB7}. FT TURN 205 209 {ECO:0000244|PDB:5NB7}. FT STRAND 211 214 {ECO:0000244|PDB:5NAT}. FT STRAND 217 222 {ECO:0000244|PDB:5NAT}. FT STRAND 225 227 {ECO:0000244|PDB:6FUT}. FT STRAND 231 233 {ECO:0000244|PDB:4CBO}. FT STRAND 236 240 {ECO:0000244|PDB:5NAT}. FT HELIX 241 244 {ECO:0000244|PDB:5NAT}. FT HELIX 245 252 {ECO:0000244|PDB:5NAT}. SQ SEQUENCE 253 AA; 27033 MW; 78B06C209DEEA362 CRC64; MHSWERLAVL VLLGAAACAA PPRGRILGGR EAEAHARPYM ASVQLNGAHL CGGVLVAEQW VLSAAHCLED AADGKVQVLL GAHSLSQPEP SKRLYDVLRA VPHPDSQPDT IDHDLLLLQL SEKATLGPAV RPLPWQRVDR DVAPGTLCDV AGWGIVNHAG RRPDSLQHVL LPVLDRATCN RRTHHDGAIT ERLMCAESNR RDSCKGDSGG PLVCGGVLEG VVTSGSRVCG NRKKPGIYTR VASYAAWIDS VLA //