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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

  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. heart morphogenesis Source: FlyBase
  3. positive regulation of circadian sleep/wake cycle, sleep Source: FlyBase
  4. proteolysis Source: UniProtKB
  5. regulation of heart rate Source: FlyBase
  6. 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: 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
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.

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: January 7, 2015
This is version 107 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.