ID ACE_DROME Reviewed; 615 AA. AC Q10714; A4V0P3; Q27572; Q9NKE4; Q9TX66; Q9VJV3; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 3. DT 27-MAR-2024, entry version 196. DE RecName: Full=Angiotensin-converting enzyme; DE EC=3.4.15.1; DE AltName: Full=Dipeptidyl carboxypeptidase I; DE AltName: Full=Kininase II; DE Flags: Precursor; GN Name=Ance; Synonyms=Race; ORFNames=CG8827; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; OC Drosophilidae; Drosophila; Sophophora. OX NCBI_TaxID=7227; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Embryo; RX PubMed=8224398; DOI=10.1042/bst021243s; RA Cornell M.J., Coates D., Isaac R.E.; RT "Characterisation of putative Drosophila angiotensin converting enzyme cDNA RT clones."; RL Biochem. Soc. Trans. 21:243-243(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, RP AND ACTIVITY REGULATION. RX PubMed=7775412; DOI=10.1074/jbc.270.23.13613; RA Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P., RA Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.; RT "Cloning and expression of an evolutionary conserved single-domain RT angiotensin converting enzyme from Drosophila melanogaster."; RL J. Biol. Chem. 270:13613-13619(1995). RN [3] RP SEQUENCE REVISION. RA Cornell M.J.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Canton-S; RX PubMed=7547464; DOI=10.1016/0925-4773(95)00349-5; RA Tatei K., Cai H., Ip Y.T., Levine M.; RT "Race: a Drosophila homologue of the angiotensin converting enzyme."; RL Mech. Dev. 51:157-168(1995). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10471707; DOI=10.1093/genetics/153.1.179; RA Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., RA Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., RA Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R., RA Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., RA Celniker S.E., Rubin G.M.; RT "An exploration of the sequence of a 2.9-Mb region of the genome of RT Drosophila melanogaster: the Adh region."; RL Genetics 153:179-219(1999). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Berkeley; RX PubMed=10731132; DOI=10.1126/science.287.5461.2185; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C., RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., RA Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). RN [7] RP GENOME REANNOTATION. RC STRAIN=Berkeley; RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083; RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A., RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.; RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic RT review."; RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Berkeley; TISSUE=Embryo; RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080; RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., RA Celniker S.E.; RT "A Drosophila full-length cDNA resource."; RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002). RN [9] RP CLEAVAGE SITE, GLYCOSYLATION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=8761461; DOI=10.1042/bj3180125; RA Williams T.A., Michaud A., Houard X., Chauvet M.-T., Soubrier F., RA Corvol P.; RT "Drosophila melanogaster angiotensin I-converting enzyme expressed in RT Pichia pastoris resembles the C domain of the mammalian homologue and does RT not require glycosylation for secretion and enzymic activity."; RL Biochem. J. 318:125-131(1996). RN [10] RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=9839949; DOI=10.1046/j.1432-1327.1998.2570599.x; RA Houard X., Williams T.A., Michaud A., Dani P., Isaac R.E., Shirras A.D., RA Coates D., Corvol P.; RT "The Drosophila melanogaster-related angiotensin-I-converting enzymes Acer RT and Ance -- distinct enzymic characteristics and alternative expression RT during pupal development."; RL Eur. J. Biochem. 257:599-606(1998). RN [11] RP TISSUE SPECIFICITY, FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=12591244; DOI=10.1016/s0012-1606(02)00082-9; RA Hurst D., Rylett C.M., Isaac R.E., Shirras A.D.; RT "The Drosophila angiotensin-converting enzyme homologue Ance is required RT for spermiogenesis."; RL Dev. Biol. 254:238-247(2003). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-615, X-RAY CRYSTALLOGRAPHY (2.4 RP ANGSTROMS) OF 14-615 IN COMPLEX WITH CAPTOPRIL, AND X-RAY CRYSTALLOGRAPHY RP (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH LISINOPRIL. RX PubMed=12633854; DOI=10.1016/s0014-5793(03)00128-5; RA Kim H.M., Shin D.R., Yoo O.J., Lee H., Lee J.-O.; RT "Crystal structure of Drosophila angiotensin I-converting enzyme bound to RT captopril and lisinopril."; RL FEBS Lett. 538:65-70(2003). CC -!- FUNCTION: May be involved in the specific maturation or degradation of CC a number of bioactive peptides. May play a role in the contractions of CC the heart, gut and testes, and in spermatid differentiation. CC {ECO:0000269|PubMed:12591244}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, CC when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion CC of angiotensin I to angiotensin II, with increase in vasoconstrictor CC activity, but no action on angiotensin II.; EC=3.4.15.1; CC Evidence={ECO:0000269|PubMed:7775412}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- ACTIVITY REGULATION: Inhibited by captopril and, to a lesser extent, by CC lisinopril, trandolaprilat, fosinoprilat and enalaprilat. CC {ECO:0000269|PubMed:7775412, ECO:0000269|PubMed:8761461}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=33.5 uM for angiotensin I {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC KM=53.4 uM for N-acetyl-Ser-Asp-Lys-Pro {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC KM=2.59 mM for Hip-His-Leu {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC KM=10.26 mM for Hip-His-Leu-NH(2) {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC KM=372 uM for (Leu5)enkephalin {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC KM=1.88 mM for (Leu5)enkephalinamide {ECO:0000269|PubMed:7775412, CC ECO:0000269|PubMed:8761461, ECO:0000269|PubMed:9839949}; CC -!- INTERACTION: CC Q10714; P01019: AGT; Xeno; NbExp=2; IntAct=EBI-115736, EBI-751728; CC Q10714; P01042: KNG1; Xeno; NbExp=2; IntAct=EBI-115736, EBI-6378713; CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space. CC -!- TISSUE SPECIFICITY: Expressed in vesicular structures in spermatocytes CC and early spermatids (at protein level). {ECO:0000269|PubMed:12591244}. CC -!- DEVELOPMENTAL STAGE: Expressed in the amnioserosa during germ band CC elongation, shortening and heart morphogenesis. Expressed in midgut CC throughout embryogenesis. CC -!- PTM: Glycosylated. {ECO:0000269|PubMed:8761461}. CC -!- DISRUPTION PHENOTYPE: Male flies are sterile. CC {ECO:0000269|PubMed:12591244}. CC -!- SIMILARITY: Belongs to the peptidase M2 family. {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; U25344; AAB02171.1; -; mRNA. DR EMBL; U34599; AAC46902.1; -; mRNA. DR EMBL; AE014134; AAF53353.2; -; Genomic_DNA. DR EMBL; AE014134; AAN10856.1; -; Genomic_DNA. DR EMBL; AY061129; AAL28677.1; -; mRNA. DR RefSeq; NP_001285915.1; NM_001298986.1. DR RefSeq; NP_477046.1; NM_057698.5. DR RefSeq; NP_723852.1; NM_165070.3. DR PDB; 1J36; X-ray; 2.40 A; A/B=14-615. DR PDB; 1J37; X-ray; 2.40 A; A/B=14-615. DR PDB; 1J38; X-ray; 2.60 A; A/B=14-615. DR PDB; 2X8Y; X-ray; 1.90 A; A=17-614. DR PDB; 2X8Z; X-ray; 1.98 A; A=17-614. DR PDB; 2X90; X-ray; 1.98 A; A=17-614. DR PDB; 2X91; X-ray; 1.98 A; A=17-614. DR PDB; 2X92; X-ray; 2.11 A; A=17-615. DR PDB; 2X93; X-ray; 1.98 A; A=17-615. DR PDB; 2X94; X-ray; 1.88 A; A=17-615. DR PDB; 2X95; X-ray; 1.96 A; A=17-615. DR PDB; 2X96; X-ray; 1.85 A; A=17-614. DR PDB; 2X97; X-ray; 1.85 A; A=17-614. DR PDB; 2XHM; X-ray; 1.96 A; A=17-614. DR PDB; 3ZQZ; X-ray; 2.35 A; A=17-614. DR PDB; 4AA1; X-ray; 1.99 A; A=17-614. DR PDB; 4AA2; X-ray; 1.99 A; A=17-614. DR PDB; 4ASQ; X-ray; 1.99 A; A=17-614. DR PDB; 4ASR; X-ray; 1.90 A; A=17-614. DR PDB; 4CA7; X-ray; 1.82 A; A=17-614. DR PDB; 4CA8; X-ray; 1.99 A; A=17-614. DR PDB; 5A2R; X-ray; 1.85 A; A=18-615. DR PDBsum; 1J36; -. DR PDBsum; 1J37; -. DR PDBsum; 1J38; -. DR PDBsum; 2X8Y; -. DR PDBsum; 2X8Z; -. DR PDBsum; 2X90; -. DR PDBsum; 2X91; -. DR PDBsum; 2X92; -. DR PDBsum; 2X93; -. DR PDBsum; 2X94; -. DR PDBsum; 2X95; -. DR PDBsum; 2X96; -. DR PDBsum; 2X97; -. DR PDBsum; 2XHM; -. DR PDBsum; 3ZQZ; -. DR PDBsum; 4AA1; -. DR PDBsum; 4AA2; -. DR PDBsum; 4ASQ; -. DR PDBsum; 4ASR; -. DR PDBsum; 4CA7; -. DR PDBsum; 4CA8; -. DR PDBsum; 5A2R; -. DR AlphaFoldDB; Q10714; -. DR SMR; Q10714; -. DR BioGRID; 60835; 2. DR IntAct; Q10714; 7. DR MINT; Q10714; -. DR STRING; 7227.FBpp0080130; -. DR MEROPS; M02.003; -. DR GlyCosmos; Q10714; 3 sites, No reported glycans. DR GlyGen; Q10714; 3 sites. DR iPTMnet; Q10714; -. DR PaxDb; 7227-FBpp0080129; -. DR DNASU; 34805; -. DR EnsemblMetazoa; FBtr0080552; FBpp0080129; FBgn0012037. DR EnsemblMetazoa; FBtr0080553; FBpp0080130; FBgn0012037. DR EnsemblMetazoa; FBtr0343667; FBpp0310259; FBgn0012037. DR GeneID; 34805; -. DR KEGG; dme:Dmel_CG8827; -. DR AGR; FB:FBgn0012037; -. DR CTD; 34805; -. DR FlyBase; FBgn0012037; Ance. DR VEuPathDB; VectorBase:FBgn0012037; -. DR eggNOG; KOG3690; Eukaryota. DR HOGENOM; CLU_014364_3_3_1; -. DR InParanoid; Q10714; -. DR OMA; KPSKMFE; -. DR OrthoDB; 2898149at2759; -. DR PhylomeDB; Q10714; -. DR BRENDA; 3.4.15.1; 1994. DR Reactome; R-DME-2022377; Metabolism of Angiotensinogen to Angiotensins. DR SABIO-RK; Q10714; -. DR SignaLink; Q10714; -. DR BioGRID-ORCS; 34805; 0 hits in 3 CRISPR screens. DR EvolutionaryTrace; Q10714; -. DR GenomeRNAi; 34805; -. DR PRO; PR:Q10714; -. DR Proteomes; UP000000803; Chromosome 2L. DR Bgee; FBgn0012037; Expressed in eye disc (Drosophila) and 71 other cell types or tissues. DR ExpressionAtlas; Q10714; baseline and differential. DR GO; GO:0005615; C:extracellular space; IDA:FlyBase. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IDA:FlyBase. DR GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:FlyBase. DR GO; GO:0007552; P:metamorphosis; IEP:FlyBase. DR GO; GO:0016486; P:peptide hormone processing; IDA:FlyBase. DR GO; GO:0006508; P:proteolysis; IDA:FlyBase. DR GO; GO:0009609; P:response to symbiotic bacterium; IEP:FlyBase. DR GO; GO:0019953; P:sexual reproduction; IEP:FlyBase. DR CDD; cd06461; M2_ACE; 1. DR Gene3D; 1.10.1370.30; -; 1. DR InterPro; IPR001548; Peptidase_M2. DR PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1. DR PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1. DR Pfam; PF01401; Peptidase_M2; 1. DR PRINTS; PR00791; PEPDIPTASEA. DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1. DR PROSITE; PS52011; PEPTIDASE_M2; 1. DR PROSITE; PS00142; ZINC_PROTEASE; 1. DR Genevisible; Q10714; DM. PE 1: Evidence at protein level; KW 3D-structure; Carboxypeptidase; Disulfide bond; Glycoprotein; Hydrolase; KW Metal-binding; Metalloprotease; Protease; Reference proteome; Secreted; KW Signal; Zinc. FT SIGNAL 1..17 FT CHAIN 18..615 FT /note="Angiotensin-converting enzyme" FT /id="PRO_0000028563" FT DOMAIN 19..607 FT /note="Peptidase M2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT ACT_SITE 368 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT ACT_SITE 497 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT BINDING 367 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT BINDING 371 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT BINDING 395 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT CARBOHYD 53 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:8761461" FT CARBOHYD 196 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:8761461" FT CARBOHYD 311 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000305|PubMed:8761461" FT DISULFID 133..141 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT DISULFID 336..354 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT DISULFID 522..540 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01355" FT CONFLICT 48..51 FT /note="WAYG -> GPMR (in Ref. 4; AAC46902)" FT /evidence="ECO:0000305" FT CONFLICT 141 FT /note="C -> S (in Ref. 4; AAC46902)" FT /evidence="ECO:0000305" FT CONFLICT 293 FT /note="G -> A (in Ref. 2; AAB02171)" FT /evidence="ECO:0000305" FT CONFLICT 346 FT /note="T -> I (in Ref. 1, 2; AAB02171, 4; AAC46902 and 5)" FT /evidence="ECO:0000305" FT CONFLICT 365 FT /note="V -> E (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 402 FT /note="S -> A (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 414 FT /note="I -> T (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="S -> T (in Ref. 4; AAC46902)" FT /evidence="ECO:0000305" FT CONFLICT 533 FT /note="V -> M (in Ref. 4; AAC46902)" FT /evidence="ECO:0000305" FT CONFLICT 547 FT /note="A -> R (in Ref. 2; AAB02171)" FT /evidence="ECO:0000305" FT HELIX 20..22 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 26..51 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 56..80 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 85..87 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 104..107 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 110..129 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 145..147 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 148..155 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 159..173 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 175..177 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 178..194 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 200..205 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 213..243 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 250..252 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 256..258 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 259..261 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 268..270 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 271..274 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:1J37" FT HELIX 286..291 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 296..309 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 317..322 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 329..331 FT /evidence="ECO:0007829|PDB:2X96" FT STRAND 339..342 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 344..347 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 349..352 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 359..377 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 378..380 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 383..385 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 391..405 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 408..413 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 416..419 FT /evidence="ECO:0007829|PDB:1J36" FT HELIX 424..438 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 441..456 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 457..459 FT /evidence="ECO:0007829|PDB:1J37" FT HELIX 462..464 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 465..477 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 492..494 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 496..499 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 505..524 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 525..527 FT /evidence="ECO:0007829|PDB:1J37" FT STRAND 530..535 FT /evidence="ECO:0007829|PDB:1J37" FT HELIX 537..539 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 546..556 FT /evidence="ECO:0007829|PDB:4CA7" FT TURN 557..560 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 564..572 FT /evidence="ECO:0007829|PDB:4CA7" FT HELIX 580..599 FT /evidence="ECO:0007829|PDB:4CA7" FT STRAND 611..613 FT /evidence="ECO:0007829|PDB:4CA7" SQ SEQUENCE 615 AA; 70914 MW; 9E3691BCC51D6C48 CRC64; MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN NVHIGWTTSN KCVSS //