Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9VLJ6

- ACER_DROME

UniProt

Q9VLJ6 - ACER_DROME

Protein

Angiotensin-converting enzyme-related protein

Gene

Acer

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 104 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    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

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. metalloendopeptidase activity Source: FlyBase
    3. peptidyl-dipeptidase activity Source: FlyBase
    4. zinc ion binding Source: FlyBase

    GO - Biological processi

    1. heart development Source: UniProtKB
    2. positive regulation of circadian sleep/wake cycle, sleep Source: FlyBase
    3. proteolysis Source: UniProtKB
    4. sleep Source: FlyBase

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    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: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0016122. Acer.

    Subcellular locationi

    Secretedextracellular space 1 Publication

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB
    2. extracellular space Source: FlyBase
    3. membrane Source: InterPro

    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.

    Interactioni

    Protein-protein interaction databases

    BioGridi60309. 2 interactions.
    IntActiQ9VLJ6. 1 interaction.
    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.
    OMAiHIDADVE.
    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

    MGACNITVLL LVIMLWLPHG LSMGNSCSAS VLEARRFFEL ENEQLRRRFH    50
    EEFLSGYNYN TNVTEANRQA MIEVYARNAE LNKRLAQQIK SSDYVQSEDA 100
    DIRRQAEHLS KLGASALNAD DYLALQNAIS SMQTNYATAT VCSYTNRSDC 150
    SLTLEPHIQE RLSHSRDPAE LAWYWREWHD KSGTPMRQNF AEYVRLTRKA 200
    SQLNGHRSYA DYWVQFYEDP DFERQLDATF KQLLPFYRQL HGYVRFRLRQ 250
    HYGPDVMPAE GNIPISLLGN MWGQSWNELL DLFTPYPEKP FVDVKAEMEK 300
    QGYTVQKLFE LGDQFFQSLG MRALPPSFWN LSVLTRPDDR HVVCHASAWD 350
    FYQDSDVRIK MCTEVDSHYF YVVHHELGHI QYYLQYEQQP AVYRGAPNPG 400
    FHEAVGDVIA LSVMSAKHLK AIGLIENGRL DEKSRINQLF KQALSKIVFL 450
    PFGYAVDKYR YAVFRNELDE SQWNCGFWQM RSEFGGVEPP VFRTEKDFDP 500
    PAKYHIDADV EYLRYFAAHI FQFQFHKALC RKAGQYAPNN SRLTLDNCDI 550
    FGSKAAGRSL SQFLSKGNSR HWKEVLEEFT GETEMDPAAL LEYFEPLYQW 600
    LKQENSRLGV PLGWGPTDKI PSDCCGTFST 630
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X96913 mRNA. Translation: CAA65632.1 .
    AE014134 Genomic DNA. Translation: AAF52693.1 .
    AY051750 mRNA. Translation: AAK93174.1 .
    PIRi JC5374.
    RefSeqi NP_001260258.1. NM_001273329.1.
    NP_477195.1. NM_057847.4.
    UniGenei Dm.1852.

    3D structure databases

    ProteinModelPortali Q9VLJ6.
    SMRi Q9VLJ6. Positions 34-622.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 60309. 2 interactions.
    IntActi Q9VLJ6. 1 interaction.
    MINTi MINT-1717838.

    Protein family/group databases

    MEROPSi M02.002.

    Proteomic databases

    PaxDbi Q9VLJ6.
    PRIDEi Q9VLJ6.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0079685 ; FBpp0079297 ; FBgn0016122 .
    FBtr0333416 ; FBpp0305608 ; FBgn0016122 .
    GeneIDi 34189.
    KEGGi dme:Dmel_CG10593.

    Organism-specific databases

    CTDi 34189.
    FlyBasei FBgn0016122. Acer.

    Phylogenomic databases

    eggNOGi NOG71044.
    GeneTreei ENSGT00520000055576.
    InParanoidi Q9VLJ6.
    KOi K01283.
    OMAi HIDADVE.
    OrthoDBi EOG76HQ13.
    PhylomeDBi Q9VLJ6.

    Miscellaneous databases

    GenomeRNAii 34189.
    NextBioi 787315.

    Gene expression databases

    Bgeei Q9VLJ6.

    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. "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: October 1, 2014
    This is version 104 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