Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
    Metal bindingi367Zinc; catalytic1
    Active sitei3681
    Metal bindingi371Zinc; catalytic1
    Metal bindingi395Zinc; catalytic1

    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
    Proteomesi
    • UP000000803 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)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 17Add BLAST17
    ChainiPRO_000002856318 – 615Angiotensin-converting enzymeAdd BLAST598

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Glycosylationi53N-linked (GlcNAc...)1 Publication1
    Disulfide bondi133 ↔ 141
    Glycosylationi196N-linked (GlcNAc...)1 Publication1
    Glycosylationi311N-linked (GlcNAc...)1 Publication1
    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

    BgeeiFBgn0012037.
    ExpressionAtlasiQ10714. baseline.
    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 interactors.
    IntActiQ10714. 7 interactors.
    MINTiMINT-808657.
    STRINGi7227.FBpp0080129.

    Structurei

    Secondary structure

    1615
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi20 – 22Combined sources3
    Helixi26 – 51Combined sources26
    Helixi56 – 80Combined sources25
    Helixi85 – 87Combined sources3
    Helixi91 – 101Combined sources11
    Helixi104 – 107Combined sources4
    Helixi110 – 129Combined sources20
    Turni145 – 147Combined sources3
    Helixi148 – 155Combined sources8
    Helixi159 – 173Combined sources15
    Helixi175 – 177Combined sources3
    Helixi178 – 194Combined sources17
    Helixi200 – 205Combined sources6
    Helixi206 – 208Combined sources3
    Helixi213 – 243Combined sources31
    Turni245 – 247Combined sources3
    Beta strandi250 – 252Combined sources3
    Helixi256 – 258Combined sources3
    Beta strandi259 – 261Combined sources3
    Helixi268 – 270Combined sources3
    Helixi271 – 274Combined sources4
    Beta strandi278 – 280Combined sources3
    Helixi286 – 291Combined sources6
    Helixi296 – 309Combined sources14
    Helixi317 – 322Combined sources6
    Beta strandi329 – 331Combined sources3
    Beta strandi339 – 342Combined sources4
    Beta strandi344 – 347Combined sources4
    Beta strandi349 – 352Combined sources4
    Helixi359 – 377Combined sources19
    Turni378 – 380Combined sources3
    Helixi383 – 385Combined sources3
    Helixi391 – 405Combined sources15
    Helixi408 – 413Combined sources6
    Beta strandi416 – 419Combined sources4
    Helixi424 – 438Combined sources15
    Helixi441 – 456Combined sources16
    Turni457 – 459Combined sources3
    Helixi462 – 464Combined sources3
    Helixi465 – 477Combined sources13
    Helixi492 – 494Combined sources3
    Helixi496 – 499Combined sources4
    Helixi505 – 524Combined sources20
    Turni525 – 527Combined sources3
    Beta strandi530 – 535Combined sources6
    Helixi537 – 539Combined sources3
    Helixi546 – 556Combined sources11
    Turni557 – 560Combined sources4
    Helixi564 – 572Combined sources9
    Helixi580 – 599Combined sources20
    Beta strandi611 – 613Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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[»]
    5A2RX-ray1.85A18-615[»]
    ProteinModelPortaliQ10714.
    SMRiQ10714.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ10714.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiKOG3690. Eukaryota.
    ENOG410XPJ3. LUCA.
    InParanoidiQ10714.
    KOiK01283.
    OMAiADIRPLY.
    OrthoDBiEOG091G033S.
    PhylomeDBiQ10714.

    Family and domain databases

    CDDicd06461. M2_ACE. 1 hit.
    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)DescriptionActionsGraphical viewLength
    Sequence conflicti48 – 51WAYG → GPMR in AAC46902 (PubMed:7547464).Curated4
    Sequence conflicti141C → S in AAC46902 (PubMed:7547464).Curated1
    Sequence conflicti293G → A in AAB02171 (PubMed:7775412).Curated1
    Sequence conflicti346T → I (PubMed:8224398).Curated1
    Sequence conflicti346T → I in AAB02171 (PubMed:7775412).Curated1
    Sequence conflicti346T → I in AAC46902 (PubMed:7547464).Curated1
    Sequence conflicti346T → I (PubMed:10471707).Curated1
    Sequence conflicti365V → E (PubMed:8224398).Curated1
    Sequence conflicti402S → A (PubMed:8224398).Curated1
    Sequence conflicti414I → T (PubMed:8224398).Curated1
    Sequence conflicti486S → T in AAC46902 (PubMed:7547464).Curated1
    Sequence conflicti533V → M in AAC46902 (PubMed:7547464).Curated1
    Sequence conflicti547A → R in AAB02171 (PubMed:7775412).Curated1

    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
    PDB 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[»]
    5A2RX-ray1.85A18-615[»]
    ProteinModelPortaliQ10714.
    SMRiQ10714.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi60835. 2 interactors.
    IntActiQ10714. 7 interactors.
    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

    eggNOGiKOG3690. Eukaryota.
    ENOG410XPJ3. LUCA.
    InParanoidiQ10714.
    KOiK01283.
    OMAiADIRPLY.
    OrthoDBiEOG091G033S.
    PhylomeDBiQ10714.

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 1994.
    SABIO-RKQ10714.

    Miscellaneous databases

    EvolutionaryTraceiQ10714.
    GenomeRNAii34805.
    PROiQ10714.

    Gene expression databases

    BgeeiFBgn0012037.
    ExpressionAtlasiQ10714. baseline.
    GenevisibleiQ10714. DM.

    Family and domain databases

    CDDicd06461. M2_ACE. 1 hit.
    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...

    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: November 30, 2016
    This is version 155 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

    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 one 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.