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Protein

Angiotensin-converting enzyme-related protein

Gene

Acer

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 have a role in the specification of heart progenitors.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.

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Enzyme regulationi

Inhibited by captopril, lisinopril, trandolaprilat, fosinoprilat and enalaprilat.1 Publication

Kineticsi

  1. KM=1.2 mM for Hip-His-Leu1 Publication
  2. KM=4.35 mM for Hip-His-Leu-NH21 Publication
  3. KM=40.6 µM for (Leu5)enkephalin1 Publication
  4. KM=949 µM for (Leu5)enkephalinamide1 Publication

    pH dependencei

    Optimum pH is 8.6.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi375 – 3751Zinc; catalyticPROSITE-ProRule annotation
    Active sitei376 – 3761PROSITE-ProRule annotation
    Metal bindingi379 – 3791Zinc; catalyticPROSITE-ProRule annotation
    Metal bindingi403 – 4031Zinc; catalyticPROSITE-ProRule annotation

    GO - Molecular functioni

    • carboxypeptidase activity Source: UniProtKB-KW
    • metalloendopeptidase activity Source: FlyBase
    • peptidyl-dipeptidase activity Source: FlyBase
    • zinc ion binding Source: FlyBase

    GO - Biological processi

    • heart development Source: UniProtKB
    • heart morphogenesis Source: FlyBase
    • positive regulation of circadian sleep/wake cycle, sleep Source: FlyBase
    • proteolysis Source: UniProtKB
    • regulation of heart rate Source: FlyBase
    • sleep Source: FlyBase
    Complete GO annotation...

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKQ9VLJ6.

    Protein family/group databases

    MEROPSiM02.002.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiotensin-converting enzyme-related protein (EC:3.4.15.1)
    Gene namesi
    Name:Acer
    ORF Names:CG10593
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803 Componenti: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0016122. Acer.

    Subcellular locationi

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Defective heart morphogenesis leading to lethality.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 630608Angiotensin-converting enzyme-related proteinPRO_0000028564Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi142 ↔ 150By similarity
    Disulfide bondi344 ↔ 362By similarity
    Disulfide bondi530 ↔ 548By similarity

    Post-translational modificationi

    Glycosylated.1 Publication

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiQ9VLJ6.
    PRIDEiQ9VLJ6.

    Expressioni

    Developmental stagei

    Expressed in presumptive heart cells during dorsal closure.1 Publication

    Gene expression databases

    BgeeiQ9VLJ6.
    ExpressionAtlasiQ9VLJ6. differential.

    Interactioni

    Protein-protein interaction databases

    BioGridi60309. 2 interactions.
    IntActiQ9VLJ6. 2 interactions.
    MINTiMINT-1717838.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9VLJ6.
    SMRiQ9VLJ6. Positions 34-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG71044.
    GeneTreeiENSGT00520000055576.
    InParanoidiQ9VLJ6.
    KOiK01283.
    OMAiYITDDTE.
    OrthoDBiEOG76HQ13.
    PhylomeDBiQ9VLJ6.

    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.

    Q9VLJ6-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MGACNITVLL LVIMLWLPHG LSMGNSCSAS VLEARRFFEL ENEQLRRRFH
    60 70 80 90 100
    EEFLSGYNYN TNVTEANRQA MIEVYARNAE LNKRLAQQIK SSDYVQSEDA
    110 120 130 140 150
    DIRRQAEHLS KLGASALNAD DYLALQNAIS SMQTNYATAT VCSYTNRSDC
    160 170 180 190 200
    SLTLEPHIQE RLSHSRDPAE LAWYWREWHD KSGTPMRQNF AEYVRLTRKA
    210 220 230 240 250
    SQLNGHRSYA DYWVQFYEDP DFERQLDATF KQLLPFYRQL HGYVRFRLRQ
    260 270 280 290 300
    HYGPDVMPAE GNIPISLLGN MWGQSWNELL DLFTPYPEKP FVDVKAEMEK
    310 320 330 340 350
    QGYTVQKLFE LGDQFFQSLG MRALPPSFWN LSVLTRPDDR HVVCHASAWD
    360 370 380 390 400
    FYQDSDVRIK MCTEVDSHYF YVVHHELGHI QYYLQYEQQP AVYRGAPNPG
    410 420 430 440 450
    FHEAVGDVIA LSVMSAKHLK AIGLIENGRL DEKSRINQLF KQALSKIVFL
    460 470 480 490 500
    PFGYAVDKYR YAVFRNELDE SQWNCGFWQM RSEFGGVEPP VFRTEKDFDP
    510 520 530 540 550
    PAKYHIDADV EYLRYFAAHI FQFQFHKALC RKAGQYAPNN SRLTLDNCDI
    560 570 580 590 600
    FGSKAAGRSL SQFLSKGNSR HWKEVLEEFT GETEMDPAAL LEYFEPLYQW
    610 620 630
    LKQENSRLGV PLGWGPTDKI PSDCCGTFST
    Length:630
    Mass (Da):73,057
    Last modified:May 1, 2000 - v1
    Checksum:i6D9355EB57773289
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti236 – 2361F → L in CAA65632 (PubMed:8973330).Curated
    Sequence conflicti341 – 3411H → Q in CAA65632 (PubMed:8973330).Curated
    Sequence conflicti528 – 5281A → V in CAA65632 (PubMed:8973330).Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X96913 mRNA. Translation: CAA65632.1.
    AE014134 Genomic DNA. Translation: AAF52693.1.
    AY051750 mRNA. Translation: AAK93174.1.
    PIRiJC5374.
    RefSeqiNP_001260258.1. NM_001273329.1.
    NP_477195.1. NM_057847.4.
    UniGeneiDm.1852.

    Genome annotation databases

    EnsemblMetazoaiFBtr0079685; FBpp0079297; FBgn0016122.
    FBtr0333416; FBpp0305608; FBgn0016122.
    GeneIDi34189.
    KEGGidme:Dmel_CG10593.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    X96913 mRNA. Translation: CAA65632.1.
    AE014134 Genomic DNA. Translation: AAF52693.1.
    AY051750 mRNA. Translation: AAK93174.1.
    PIRiJC5374.
    RefSeqiNP_001260258.1. NM_001273329.1.
    NP_477195.1. NM_057847.4.
    UniGeneiDm.1852.

    3D structure databases

    ProteinModelPortaliQ9VLJ6.
    SMRiQ9VLJ6. Positions 34-622.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi60309. 2 interactions.
    IntActiQ9VLJ6. 2 interactions.
    MINTiMINT-1717838.

    Protein family/group databases

    MEROPSiM02.002.

    Proteomic databases

    PaxDbiQ9VLJ6.
    PRIDEiQ9VLJ6.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblMetazoaiFBtr0079685; FBpp0079297; FBgn0016122.
    FBtr0333416; FBpp0305608; FBgn0016122.
    GeneIDi34189.
    KEGGidme:Dmel_CG10593.

    Organism-specific databases

    CTDi34189.
    FlyBaseiFBgn0016122. Acer.

    Phylogenomic databases

    eggNOGiNOG71044.
    GeneTreeiENSGT00520000055576.
    InParanoidiQ9VLJ6.
    KOiK01283.
    OMAiYITDDTE.
    OrthoDBiEOG76HQ13.
    PhylomeDBiQ9VLJ6.

    Enzyme and pathway databases

    SABIO-RKQ9VLJ6.

    Miscellaneous databases

    GenomeRNAii34189.
    NextBioi787315.
    PROiQ9VLJ6.

    Gene expression databases

    BgeeiQ9VLJ6.
    ExpressionAtlasiQ9VLJ6. differential.

    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. "The Acer gene of Drosophila codes for an angiotensin-converting enzyme homologue."
      Taylor C.A.M., Coates D., Shirras A.D.
      Gene 181:191-197(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    2. "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.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.
      Tissue: Embryo.
    5. "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, GLYCOSYLATION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    6. Cited for: FUNCTION, DISRUPTION PHENOTYPE.

    Entry informationi

    Entry nameiACER_DROME
    AccessioniPrimary (citable) accession number: Q9VLJ6
    Secondary accession number(s): Q24222
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: May 1, 2000
    Last modified: May 27, 2015
    This is version 110 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Miscellaneous

    In contrast to ance, does not hydrolyze angiotensin I.

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. 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.