CFAD_HUMAN
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 03-AUG-2022, entry version 218.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., 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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 8-253.
RX PubMed=1374388; DOI=10.1016/s0021-9258(19)50409-4;
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 high
RT 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 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. Similarity
RT in sequence between factor D and proteases of non-plasma 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. Purification,
RT alignment and N-terminal amino acid sequences of the major cyanogen bromide
RT fragments, and localization of the serine 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., Fischer-Posovszky P.,
RA Mariman E.C., Renes J.;
RT "Resveratrol-induced changes of the human adipocyte secretion 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., Mollnes T.E.,
RA 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 family
RT with meningococcal infections.";
RL Blood 107:4865-4870(2006).
CC -!- FUNCTION: Factor D cleaves factor B when the latter is complexed with
CC factor C3b, activating the C3bbb complex, which then becomes the C3
CC convertase of the alternate pathway. Its function is homologous to that
CC of C1s in the classical pathway.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of Arg-|-Lys bond in complement factor B
CC when in complex with complement subcomponent C3b or with cobra venom
CC 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 variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA35527.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=CFDbase; Note=CFD mutation db;
CC URL="http://structure.bmc.lu.se/idbase/CFDbase/";
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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 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 PDB; 6QMR; X-ray; 2.00 A; A/B/C/D/E/F=2-253.
DR PDB; 6QMT; X-ray; 1.80 A; A/B=2-253.
DR PDB; 6VMJ; X-ray; 2.95 A; W/X/Y/Z=26-253.
DR PDB; 6VMK; X-ray; 3.01 A; C/F/I/N/Q/T/W/X/a/d/g/j/m/p/s/v=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 PDBsum; 6QMR; -.
DR PDBsum; 6QMT; -.
DR PDBsum; 6VMJ; -.
DR PDBsum; 6VMK; -.
DR AlphaFoldDB; P00746; -.
DR SMR; P00746; -.
DR BioGRID; 108039; 3.
DR IntAct; P00746; 3.
DR STRING; 9606.ENSP00000332139; -.
DR BindingDB; P00746; -.
DR ChEMBL; CHEMBL2176771; -.
DR DrugBank; DB03058; 2-Aminobenzyl alcohol.
DR DrugBank; DB04459; 3,4-Dichloroisocoumarin.
DR GuidetoPHARMACOLOGY; 2842; -.
DR MEROPS; S01.191; -.
DR iPTMnet; P00746; -.
DR PhosphoSitePlus; P00746; -.
DR BioMuta; CFD; -.
DR DMDM; 158515408; -.
DR jPOST; P00746; -.
DR MassIVE; P00746; -.
DR PaxDb; P00746; -.
DR PeptideAtlas; P00746; -.
DR PRIDE; P00746; -.
DR ProteomicsDB; 51276; -.
DR ABCD; P00746; 1 sequenced antibody.
DR Antibodypedia; 4290; 566 antibodies from 33 providers.
DR DNASU; 1675; -.
DR Ensembl; ENST00000327726.11; ENSP00000332139.4; ENSG00000197766.8.
DR Ensembl; ENST00000617994.2; ENSP00000478745.1; ENSG00000274619.2.
DR GeneID; 1675; -.
DR KEGG; hsa:1675; -.
DR MANE-Select; ENST00000327726.11; ENSP00000332139.4; NM_001928.4; NP_001919.2.
DR UCSC; uc002lqc.4; human.
DR CTD; 1675; -.
DR DisGeNET; 1675; -.
DR GeneCards; CFD; -.
DR HGNC; HGNC:2771; CFD.
DR HPA; ENSG00000197766; Tissue enhanced (adipose tissue, breast).
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 VEuPathDB; HostDB:ENSG00000197766; -.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000162255; -.
DR HOGENOM; CLU_006842_1_0_1; -.
DR InParanoid; P00746; -.
DR OMA; ISHYTQW; -.
DR OrthoDB; 1314811at2759; -.
DR PhylomeDB; P00746; -.
DR TreeFam; TF333630; -.
DR BRENDA; 3.4.21.46; 2681.
DR PathwayCommons; P00746; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR Reactome; R-HSA-173736; Alternative complement activation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P00746; -.
DR SIGNOR; P00746; -.
DR BioGRID-ORCS; 1675; 260 hits in 1073 CRISPR screens.
DR ChiTaRS; CFD; human.
DR EvolutionaryTrace; P00746; -.
DR GenomeRNAi; 1675; -.
DR Pharos; P00746; Tchem.
DR PRO; PR:P00746; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P00746; protein.
DR Bgee; ENSG00000197766; Expressed in subcutaneous adipose tissue and 94 other tissues.
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:0007219; P:Notch signaling pathway; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; TAS:ProtInc.
DR GO; GO:0009617; P:response to bacterium; IEA:Ensembl.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.10.10; -; 2.
DR InterPro; IPR037561; Complement_factor_D.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24271:SF54; PTHR24271:SF54; 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; Direct protein sequencing;
KW Disease variant; Disulfide bond; Hydrolase; Immunity; Innate immunity;
KW Protease; Reference proteome; Secreted; Serine protease; Signal; Zymogen.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..25
FT /note="Activation peptide"
FT /evidence="ECO:0000255"
FT /id="PRO_0000027560"
FT CHAIN 26..253
FT /note="Complement factor D"
FT /id="PRO_0000027561"
FT DOMAIN 26..253
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 66
FT /note="Charge relay system"
FT ACT_SITE 114
FT /note="Charge relay system"
FT ACT_SITE 208
FT /note="Charge relay system"
FT DISULFID 51..67
FT DISULFID 148..214
FT DISULFID 179..195
FT DISULFID 204..229
FT VARIANT 213
FT /note="V -> G (in CFDD; dbSNP:rs267606720)"
FT /evidence="ECO:0000269|PubMed:16527897"
FT /id="VAR_034866"
FT VARIANT 214
FT /note="C -> R (in CFDD; dbSNP:rs267606721)"
FT /evidence="ECO:0000269|PubMed:16527897"
FT /id="VAR_034867"
FT VARIANT 248
FT /note="I -> M (in dbSNP:rs2230216)"
FT /id="VAR_034868"
FT CONFLICT 21
FT /note="P -> R (in Ref. 5; AAA35527)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="I -> M (in Ref. 5; AAA35527)"
FT /evidence="ECO:0000305"
FT CONFLICT 35
FT /note="H -> F (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 40
FT /note="M -> V (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="H -> E (in Ref. 7; AA sequence and 10; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 52
FT /note="G -> A (in Ref. 5; AAA35527)"
FT /evidence="ECO:0000305"
FT CONFLICT 59
FT /note="Q -> R (in Ref. 5; AAA35527)"
FT /evidence="ECO:0000305"
FT CONFLICT 63
FT /note="S -> T (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..86
FT /note="HSLS -> THLP (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 83..84
FT /note="HS -> ST (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 94..95
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="D -> E (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="Q -> G (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..191
FT /note="TCNRRTHHDGAITE -> KCRLYDVL (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="S -> T (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="S -> H (in Ref. 6; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="Missing (in Ref. 7; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 30..32
FT /evidence="ECO:0007829|PDB:1FDP"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 48..57
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:5NAT"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5NAT"
FT TURN 69..71
FT /evidence="ECO:0007829|PDB:5TCA"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:1BIO"
FT STRAND 76..81
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:5NAT"
FT HELIX 108..113
FT /evidence="ECO:0007829|PDB:1DSU"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4D9R"
FT STRAND 147..154
FT /evidence="ECO:0007829|PDB:5NAT"
FT TURN 156..159
FT /evidence="ECO:0007829|PDB:4CBO"
FT STRAND 167..174
FT /evidence="ECO:0007829|PDB:5NAT"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:5NAT"
FT TURN 182..187
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:5NB7"
FT TURN 205..209
FT /evidence="ECO:0007829|PDB:5NB7"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5NAT"
FT STRAND 225..227
FT /evidence="ECO:0007829|PDB:6FUT"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:4CBO"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:5NAT"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:5NAT"
FT HELIX 245..252
FT /evidence="ECO:0007829|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
