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Q9VLJ6 (ACER_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 100. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme-related protein

EC=3.4.15.1
Gene names
Name:Acer
ORF Names:CG10593
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length630 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Catalytic activity

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.

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

Inhibited by captopril, lisinopril, trandolaprilat, fosinoprilat and enalaprilat. Ref.5

Subcellular location

Secretedextracellular space Ref.5.

Developmental stage

Expressed in presumptive heart cells during dorsal closure. Ref.1

Post-translational modification

Glycosylated. Ref.5

Disruption phenotype

Defective heart morphogenesis leading to lethality. Ref.6

Miscellaneous

In contrast to ance, does not hydrolyze angiotensin I.

Sequence similarities

Belongs to the peptidase M2 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.2 mM for Hip-His-Leu Ref.5

KM=4.35 mM for Hip-His-Leu-NH2

KM=40.6 µM for (Leu5)enkephalin

KM=949 µM for (Leu5)enkephalinamide

pH dependence:

Optimum pH is 8.6.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 630608Angiotensin-converting enzyme-related protein
PRO_0000028564

Sites

Active site3761 By similarity
Metal binding3751Zinc; catalytic By similarity
Metal binding3791Zinc; catalytic By similarity
Metal binding4031Zinc; catalytic By similarity

Amino acid modifications

Disulfide bond142 ↔ 150 By similarity
Disulfide bond344 ↔ 362 By similarity
Disulfide bond530 ↔ 548 By similarity

Experimental info

Sequence conflict2361F → L in CAA65632. Ref.1
Sequence conflict3411H → Q in CAA65632. Ref.1
Sequence conflict5281A → V in CAA65632. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9VLJ6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 6D9355EB57773289

FASTA63073,057
        10         20         30         40         50         60 
MGACNITVLL LVIMLWLPHG LSMGNSCSAS VLEARRFFEL ENEQLRRRFH EEFLSGYNYN 

        70         80         90        100        110        120 
TNVTEANRQA MIEVYARNAE LNKRLAQQIK SSDYVQSEDA DIRRQAEHLS KLGASALNAD 

       130        140        150        160        170        180 
DYLALQNAIS SMQTNYATAT VCSYTNRSDC SLTLEPHIQE RLSHSRDPAE LAWYWREWHD 

       190        200        210        220        230        240 
KSGTPMRQNF AEYVRLTRKA SQLNGHRSYA DYWVQFYEDP DFERQLDATF KQLLPFYRQL 

       250        260        270        280        290        300 
HGYVRFRLRQ HYGPDVMPAE GNIPISLLGN MWGQSWNELL DLFTPYPEKP FVDVKAEMEK 

       310        320        330        340        350        360 
QGYTVQKLFE LGDQFFQSLG MRALPPSFWN LSVLTRPDDR HVVCHASAWD FYQDSDVRIK 

       370        380        390        400        410        420 
MCTEVDSHYF YVVHHELGHI QYYLQYEQQP AVYRGAPNPG FHEAVGDVIA LSVMSAKHLK 

       430        440        450        460        470        480 
AIGLIENGRL DEKSRINQLF KQALSKIVFL PFGYAVDKYR YAVFRNELDE SQWNCGFWQM 

       490        500        510        520        530        540 
RSEFGGVEPP VFRTEKDFDP PAKYHIDADV EYLRYFAAHI FQFQFHKALC RKAGQYAPNN 

       550        560        570        580        590        600 
SRLTLDNCDI FGSKAAGRSL SQFLSKGNSR HWKEVLEEFT GETEMDPAAL LEYFEPLYQW 

       610        620        630 
LKQENSRLGV PLGWGPTDKI PSDCCGTFST 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review."
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. expand/collapse author list , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: Berkeley.
[4]"A Drosophila full-length cDNA resource."
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
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]"Angiotensin-converting enzyme 2 is an essential regulator of heart function."
Crackower M.A., Sarao R., Oudit G.Y., Yagil C., Kozieradzki I., Scanga S.E., Oliveira-dos-Santos A.J., da Costa J., Zhang L., Pei Y., Scholey J., Ferrario C.M., Manoukian A.S., Chappell M.C., Backx P.H., Yagil Y., Penninger J.M.
Nature 417:822-828(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X96913 mRNA. Translation: CAA65632.1.
AE014134 Genomic DNA. Translation: AAF52693.1.
AY051750 mRNA. Translation: AAK93174.1.
PIRJC5374.
RefSeqNP_001260258.1. NM_001273329.1.
NP_477195.1. NM_057847.4.
UniGeneDm.1852.

3D structure databases

ProteinModelPortalQ9VLJ6.
SMRQ9VLJ6. Positions 32-622.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60309. 2 interactions.
IntActQ9VLJ6. 1 interaction.
MINTMINT-1717838.

Protein family/group databases

MEROPSM02.002.

Proteomic databases

PaxDbQ9VLJ6.
PRIDEQ9VLJ6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0079685; FBpp0079297; FBgn0016122.
FBtr0333416; FBpp0305608; FBgn0016122.
GeneID34189.
KEGGdme:Dmel_CG10593.

Organism-specific databases

CTD34189.
FlyBaseFBgn0016122. Acer.

Phylogenomic databases

eggNOGNOG71044.
GeneTreeENSGT00520000055576.
InParanoidQ9VLJ6.
KOK01283.
OMAYVVHHEL.
OrthoDBEOG76HQ13.
PhylomeDBQ9VLJ6.

Gene expression databases

BgeeQ9VLJ6.

Family and domain databases

InterProIPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi34189.
NextBio787315.

Entry information

Entry nameACER_DROME
AccessionPrimary (citable) accession number: Q9VLJ6
Secondary accession number(s): Q24222
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 100 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Drosophila

Drosophila: entries, gene names and cross-references to FlyBase