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Q10714

- ACE_DROME

UniProt

Q10714 - ACE_DROME

Protein

Angiotensin-converting enzyme

Gene

Ance

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (11 Sep 2007)
      Previous versions | rss
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    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

    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

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB-KW
    4. peptidyl-dipeptidase activity Source: FlyBase
    5. protein binding Source: IntAct

    GO - Biological processi

    1. metamorphosis Source: FlyBase
    2. proteolysis Source: FlyBase
    3. response to symbiotic bacterium Source: FlyBase
    4. spermatid nucleus differentiation Source: FlyBase
    5. sperm individualization Source: FlyBase

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    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: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0012037. Ance.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular space Source: FlyBase
    2. membrane Source: InterPro

    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.

    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. 3 interactions.
    MINTiMINT-808657.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    GeneTreeiENSGT00520000055576.
    InParanoidiQ10714.
    KOiK01283.
    OMAiWAYGSNI.
    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

    MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY    50
    GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL 100
    TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE 150
    EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG 200
    AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE 250
    TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF 300
    QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR 350
    IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV 400
    LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK 450
    YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA 500
    DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA 550
    AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN 600
    NVHIGWTTSN KCVSS 615
    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:
    EMBL
    GenBank
    DDBJ
    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_477046.1. NM_057698.4.
    NP_723852.1. NM_165070.2.
    UniGeneiDm.2157.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    RefSeqi NP_477046.1. NM_057698.4.
    NP_723852.1. NM_165070.2.
    UniGenei Dm.2157.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J36 X-ray 2.40 A/B 14-615 [» ]
    1J37 X-ray 2.40 A/B 14-615 [» ]
    1J38 X-ray 2.60 A/B 14-615 [» ]
    2X8Y X-ray 1.90 A 17-614 [» ]
    2X8Z X-ray 1.98 A 17-614 [» ]
    2X90 X-ray 1.98 A 17-614 [» ]
    2X91 X-ray 1.98 A 17-614 [» ]
    2X92 X-ray 2.11 A 17-615 [» ]
    2X93 X-ray 1.98 A 17-615 [» ]
    2X94 X-ray 1.88 A 17-615 [» ]
    2X95 X-ray 1.96 A 17-615 [» ]
    2X96 X-ray 1.85 A 17-614 [» ]
    2X97 X-ray 1.85 A 17-614 [» ]
    2XHM X-ray 1.96 A 17-614 [» ]
    3ZQZ X-ray 2.35 A 17-614 [» ]
    4AA1 X-ray 1.99 A 17-614 [» ]
    4AA2 X-ray 1.99 A 17-614 [» ]
    4ASQ X-ray 1.99 A 17-614 [» ]
    4ASR X-ray 1.90 A 17-614 [» ]
    4CA7 X-ray 1.82 A 17-614 [» ]
    4CA8 X-ray 1.99 A 17-614 [» ]
    ProteinModelPortali Q10714.
    SMRi Q10714. Positions 19-614.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60835. 2 interactions.
    IntActi Q10714. 3 interactions.
    MINTi MINT-808657.

    Protein family/group databases

    MEROPSi M02.003.

    Proteomic databases

    PaxDbi Q10714.
    PRIDEi Q10714.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0080552 ; FBpp0080129 ; FBgn0012037 .
    FBtr0080553 ; FBpp0080130 ; FBgn0012037 .
    GeneIDi 34805.
    KEGGi dme:Dmel_CG8827.

    Organism-specific databases

    CTDi 34805.
    FlyBasei FBgn0012037. Ance.

    Phylogenomic databases

    eggNOGi NOG71044.
    GeneTreei ENSGT00520000055576.
    InParanoidi Q10714.
    KOi K01283.
    OMAi WAYGSNI.
    OrthoDBi EOG76HQ13.
    PhylomeDBi Q10714.

    Enzyme and pathway databases

    SABIO-RK Q10714.

    Miscellaneous databases

    EvolutionaryTracei Q10714.
    GenomeRNAii 34805.
    NextBioi 790306.

    Gene expression databases

    Bgeei Q10714.

    Family and domain databases

    InterProi IPR001548. Peptidase_M2.
    [Graphical view ]
    PANTHERi PTHR10514. PTHR10514. 1 hit.
    Pfami PF01401. Peptidase_M2. 1 hit.
    [Graphical view ]
    PRINTSi PR00791. PEPDIPTASEA.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 135 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