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Protein

Angiotensin-converting enzyme

Gene

Ance

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the specific maturation or degradation of a number of bioactive peptides. May play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.1 Publication

Catalytic activityi

Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Enzyme regulationi

Inhibited by captopril and, to a lesser extent, by lisinopril, trandolaprilat, fosinoprilat and enalaprilat.2 Publications

Kineticsi

  1. KM=33.5 µM for angiotensin I3 Publications
  2. KM=53.4 µM for N-acetyl-Ser-Asp-Lys-Pro3 Publications
  3. KM=2.59 mM for Hip-His-Leu3 Publications
  4. KM=10.26 mM for Hip-His-Leu-NH23 Publications
  5. KM=372 µM for (Leu5)enkephalin3 Publications
  6. KM=1.88 mM for (Leu5)enkephalinamide3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi367 – 3671Zinc; catalytic
    Active sitei368 – 3681
    Metal bindingi371 – 3711Zinc; catalytic
    Metal bindingi395 – 3951Zinc; catalytic

    GO - Molecular functioni

    GO - Biological processi

    • metamorphosis Source: FlyBase
    • proteolysis Source: FlyBase
    • response to symbiotic bacterium Source: FlyBase
    • spermatid nucleus differentiation Source: FlyBase
    • sperm individualization Source: FlyBase
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 1994.
    SABIO-RKQ10714.

    Protein family/group databases

    MEROPSiM02.003.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiotensin-converting enzyme (EC:3.4.15.1)
    Alternative name(s):
    Dipeptidyl carboxypeptidase I
    Kininase II
    Gene namesi
    Name:Ance
    Synonyms:Race
    ORF Names:CG8827
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803 Componenti: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0012037. Ance.

    Subcellular locationi

    GO - Cellular componenti

    • extracellular space Source: FlyBase
    • membrane Source: InterPro
    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Male flies are sterile.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Add
    BLAST
    Chaini18 – 615598Angiotensin-converting enzymePRO_0000028563Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi53 – 531N-linked (GlcNAc...)1 Publication
    Disulfide bondi133 ↔ 141
    Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
    Glycosylationi311 – 3111N-linked (GlcNAc...)1 Publication
    Disulfide bondi336 ↔ 354
    Disulfide bondi467 ↔ 612
    Disulfide bondi522 ↔ 540

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ10714.
    PRIDEiQ10714.

    Expressioni

    Tissue specificityi

    Expressed in vesicular structures in spermatocytes and early spermatids (at protein level).1 Publication

    Developmental stagei

    Expressed in the amnioserosa during germ band elongation, shortening and heart morphogenesis. Expressed in midgut throughout embryogenesis.

    Gene expression databases

    BgeeiQ10714.
    ExpressionAtlasiQ10714. differential.
    GenevisibleiQ10714. DM.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGTP010192EBI-115736,EBI-751728From a different organism.
    KNG1P010422EBI-115736,EBI-6378713From a different organism.

    Protein-protein interaction databases

    BioGridi60835. 2 interactions.
    IntActiQ10714. 7 interactions.
    MINTiMINT-808657.
    STRINGi7227.FBpp0080129.

    Structurei

    Secondary structure

    1
    615
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi20 – 223Combined sources
    Helixi26 – 5126Combined sources
    Helixi56 – 8025Combined sources
    Helixi85 – 873Combined sources
    Helixi91 – 10111Combined sources
    Helixi104 – 1074Combined sources
    Helixi110 – 12920Combined sources
    Turni145 – 1473Combined sources
    Helixi148 – 1558Combined sources
    Helixi159 – 17315Combined sources
    Helixi175 – 1773Combined sources
    Helixi178 – 19417Combined sources
    Helixi200 – 2056Combined sources
    Helixi206 – 2083Combined sources
    Helixi213 – 24331Combined sources
    Turni245 – 2473Combined sources
    Beta strandi250 – 2523Combined sources
    Helixi256 – 2583Combined sources
    Beta strandi259 – 2613Combined sources
    Helixi268 – 2703Combined sources
    Helixi271 – 2744Combined sources
    Beta strandi278 – 2803Combined sources
    Helixi286 – 2916Combined sources
    Helixi296 – 30914Combined sources
    Helixi317 – 3226Combined sources
    Beta strandi329 – 3313Combined sources
    Beta strandi339 – 3424Combined sources
    Beta strandi344 – 3474Combined sources
    Beta strandi349 – 3524Combined sources
    Helixi359 – 37719Combined sources
    Turni378 – 3803Combined sources
    Helixi383 – 3853Combined sources
    Helixi391 – 40515Combined sources
    Helixi408 – 4136Combined sources
    Beta strandi416 – 4194Combined sources
    Helixi424 – 43815Combined sources
    Helixi441 – 45616Combined sources
    Turni457 – 4593Combined sources
    Helixi462 – 4643Combined sources
    Helixi465 – 47713Combined sources
    Helixi492 – 4943Combined sources
    Helixi496 – 4994Combined sources
    Helixi505 – 52420Combined sources
    Turni525 – 5273Combined sources
    Beta strandi530 – 5356Combined sources
    Helixi537 – 5393Combined sources
    Helixi546 – 55611Combined sources
    Turni557 – 5604Combined sources
    Helixi564 – 5729Combined sources
    Helixi580 – 59920Combined sources
    Beta strandi611 – 6133Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J36X-ray2.40A/B14-615[»]
    1J37X-ray2.40A/B14-615[»]
    1J38X-ray2.60A/B14-615[»]
    2X8YX-ray1.90A17-614[»]
    2X8ZX-ray1.98A17-614[»]
    2X90X-ray1.98A17-614[»]
    2X91X-ray1.98A17-614[»]
    2X92X-ray2.11A17-615[»]
    2X93X-ray1.98A17-615[»]
    2X94X-ray1.88A17-615[»]
    2X95X-ray1.96A17-615[»]
    2X96X-ray1.85A17-614[»]
    2X97X-ray1.85A17-614[»]
    2XHMX-ray1.96A17-614[»]
    3ZQZX-ray2.35A17-614[»]
    4AA1X-ray1.99A17-614[»]
    4AA2X-ray1.99A17-614[»]
    4ASQX-ray1.99A17-614[»]
    4ASRX-ray1.90A17-614[»]
    4CA7X-ray1.82A17-614[»]
    4CA8X-ray1.99A17-614[»]
    ProteinModelPortaliQ10714.
    SMRiQ10714. Positions 19-614.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ10714.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG71044.
    InParanoidiQ10714.
    KOiK01283.
    OMAiMEATWNY.
    OrthoDBiEOG76HQ13.
    PhylomeDBiQ10714.

    Family and domain databases

    InterProiIPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 1 hit.
    PfamiPF01401. Peptidase_M2. 1 hit.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q10714-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY
    60 70 80 90 100
    GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL
    110 120 130 140 150
    TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE
    160 170 180 190 200
    EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG
    210 220 230 240 250
    AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE
    260 270 280 290 300
    TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF
    310 320 330 340 350
    QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR
    360 370 380 390 400
    IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV
    410 420 430 440 450
    LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK
    460 470 480 490 500
    YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA
    510 520 530 540 550
    DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA
    560 570 580 590 600
    AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN
    610
    NVHIGWTTSN KCVSS
    Length:615
    Mass (Da):70,914
    Last modified:September 11, 2007 - v3
    Checksum:i9E3691BCC51D6C48
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti48 – 514WAYG → GPMR in AAC46902 (PubMed:7547464).Curated
    Sequence conflicti141 – 1411C → S in AAC46902 (PubMed:7547464).Curated
    Sequence conflicti293 – 2931G → A in AAB02171 (PubMed:7775412).Curated
    Sequence conflicti346 – 3461T → I (PubMed:8224398).Curated
    Sequence conflicti346 – 3461T → I in AAB02171 (PubMed:7775412).Curated
    Sequence conflicti346 – 3461T → I in AAC46902 (PubMed:7547464).Curated
    Sequence conflicti346 – 3461T → I (PubMed:10471707).Curated
    Sequence conflicti365 – 3651V → E (PubMed:8224398).Curated
    Sequence conflicti402 – 4021S → A (PubMed:8224398).Curated
    Sequence conflicti414 – 4141I → T (PubMed:8224398).Curated
    Sequence conflicti486 – 4861S → T in AAC46902 (PubMed:7547464).Curated
    Sequence conflicti533 – 5331V → M in AAC46902 (PubMed:7547464).Curated
    Sequence conflicti547 – 5471A → R in AAB02171 (PubMed:7775412).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U25344 mRNA. Translation: AAB02171.1.
    U34599 mRNA. Translation: AAC46902.1.
    AE014134 Genomic DNA. Translation: AAF53353.2.
    AE014134 Genomic DNA. Translation: AAN10856.1.
    AY061129 mRNA. Translation: AAL28677.1.
    RefSeqiNP_001285915.1. NM_001298986.1.
    NP_477046.1. NM_057698.5.
    NP_723852.1. NM_165070.3.
    UniGeneiDm.2157.

    Genome annotation databases

    EnsemblMetazoaiFBtr0080552; FBpp0080129; FBgn0012037.
    FBtr0080553; FBpp0080130; FBgn0012037.
    FBtr0343667; FBpp0310259; FBgn0012037.
    GeneIDi34805.
    KEGGidme:Dmel_CG8827.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U25344 mRNA. Translation: AAB02171.1.
    U34599 mRNA. Translation: AAC46902.1.
    AE014134 Genomic DNA. Translation: AAF53353.2.
    AE014134 Genomic DNA. Translation: AAN10856.1.
    AY061129 mRNA. Translation: AAL28677.1.
    RefSeqiNP_001285915.1. NM_001298986.1.
    NP_477046.1. NM_057698.5.
    NP_723852.1. NM_165070.3.
    UniGeneiDm.2157.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J36X-ray2.40A/B14-615[»]
    1J37X-ray2.40A/B14-615[»]
    1J38X-ray2.60A/B14-615[»]
    2X8YX-ray1.90A17-614[»]
    2X8ZX-ray1.98A17-614[»]
    2X90X-ray1.98A17-614[»]
    2X91X-ray1.98A17-614[»]
    2X92X-ray2.11A17-615[»]
    2X93X-ray1.98A17-615[»]
    2X94X-ray1.88A17-615[»]
    2X95X-ray1.96A17-615[»]
    2X96X-ray1.85A17-614[»]
    2X97X-ray1.85A17-614[»]
    2XHMX-ray1.96A17-614[»]
    3ZQZX-ray2.35A17-614[»]
    4AA1X-ray1.99A17-614[»]
    4AA2X-ray1.99A17-614[»]
    4ASQX-ray1.99A17-614[»]
    4ASRX-ray1.90A17-614[»]
    4CA7X-ray1.82A17-614[»]
    4CA8X-ray1.99A17-614[»]
    ProteinModelPortaliQ10714.
    SMRiQ10714. Positions 19-614.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi60835. 2 interactions.
    IntActiQ10714. 7 interactions.
    MINTiMINT-808657.
    STRINGi7227.FBpp0080129.

    Protein family/group databases

    MEROPSiM02.003.

    Proteomic databases

    PaxDbiQ10714.
    PRIDEiQ10714.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiFBtr0080552; FBpp0080129; FBgn0012037.
    FBtr0080553; FBpp0080130; FBgn0012037.
    FBtr0343667; FBpp0310259; FBgn0012037.
    GeneIDi34805.
    KEGGidme:Dmel_CG8827.

    Organism-specific databases

    CTDi34805.
    FlyBaseiFBgn0012037. Ance.

    Phylogenomic databases

    eggNOGiNOG71044.
    InParanoidiQ10714.
    KOiK01283.
    OMAiMEATWNY.
    OrthoDBiEOG76HQ13.
    PhylomeDBiQ10714.

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 1994.
    SABIO-RKQ10714.

    Miscellaneous databases

    EvolutionaryTraceiQ10714.
    GenomeRNAii34805.
    NextBioi790306.
    PROiQ10714.

    Gene expression databases

    BgeeiQ10714.
    ExpressionAtlasiQ10714. differential.
    GenevisibleiQ10714. DM.

    Family and domain databases

    InterProiIPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 1 hit.
    PfamiPF01401. Peptidase_M2. 1 hit.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Characterisation of putative Drosophila angiotensin converting enzyme cDNA clones."
      Cornell M.J., Coates D., Isaac R.E.
      Biochem. Soc. Trans. 21:243-243(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Embryo.
    2. "Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster."
      Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P., Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.
      J. Biol. Chem. 270:13613-13619(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
    3. Cornell M.J.
      Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Race: a Drosophila homologue of the angiotensin converting enzyme."
      Tatei K., Cai H., Ip Y.T., Levine M.
      Mech. Dev. 51:157-168(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Canton-S.
    5. "An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
      Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R.
      , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
      Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    6. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    7. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    9. "Drosophila melanogaster angiotensin I-converting enzyme expressed in Pichia pastoris resembles the C domain of the mammalian homologue and does not require glycosylation for secretion and enzymic activity."
      Williams T.A., Michaud A., Houard X., Chauvet M.-T., Soubrier F., Corvol P.
      Biochem. J. 318:125-131(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE SITE, GLYCOSYLATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    10. "The Drosophila melanogaster-related angiotensin-I-converting enzymes Acer and Ance -- distinct enzymic characteristics and alternative expression during pupal development."
      Houard X., Williams T.A., Michaud A., Dani P., Isaac R.E., Shirras A.D., Coates D., Corvol P.
      Eur. J. Biochem. 257:599-606(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
    11. "The Drosophila angiotensin-converting enzyme homologue Ance is required for spermiogenesis."
      Hurst D., Rylett C.M., Isaac R.E., Shirras A.D.
      Dev. Biol. 254:238-247(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
    12. "Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril."
      Kim H.M., Shin D.R., Yoo O.J., Lee H., Lee J.-O.
      FEBS Lett. 538:65-70(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-615, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH CAPTOPRIL, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH LISINOPRIL.

    Entry informationi

    Entry nameiACE_DROME
    AccessioniPrimary (citable) accession number: Q10714
    Secondary accession number(s): A4V0P3
    , Q27572, Q9NKE4, Q9TX66, Q9VJV3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: September 11, 2007
    Last modified: July 22, 2015
    This is version 143 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.