ACE_DROME
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 03-AUG-2022, entry version 190.
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}.
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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.FBpp0080129; -.
DR MEROPS; M02.003; -.
DR GlyGen; Q10714; 3 sites.
DR iPTMnet; Q10714; -.
DR PaxDb; Q10714; -.
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 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; FHISASM; -.
DR OrthoDB; 422699at2759; -.
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 tissues.
DR ExpressionAtlas; Q10714; baseline and differential.
DR Genevisible; Q10714; DM.
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; IMP:FlyBase.
DR GO; GO:0019953; P:sexual reproduction; IEP:FlyBase.
DR GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
DR GO; GO:0007289; P:spermatid nucleus differentiation; IMP:FlyBase.
DR CDD; cd06461; M2_ACE; 1.
DR InterPro; IPR001548; Peptidase_M2.
DR PANTHER; PTHR10514; PTHR10514; 1.
DR Pfam; PF01401; Peptidase_M2; 1.
DR PRINTS; PR00791; PEPDIPTASEA.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
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 ACT_SITE 368
FT BINDING 367
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 371
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT BINDING 395
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 DISULFID 336..354
FT DISULFID 467..612
FT DISULFID 522..540
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
