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Q10714 (ACE_DROME) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme

EC=3.4.15.1
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
Gene names
Name:Ance
Synonyms:Race
ORF Names:CG8827
OrganismDrosophila melanogaster (Fruit fly) [Reference proteome]
Taxonomic identifier7227 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora

Protein attributes

Sequence length615 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 play a role in the contractions of the heart, gut and testes, and in spermatid differentiation. Ref.11

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. Ref.2

Cofactor

Binds 1 zinc ion per subunit.

Enzyme regulation

Inhibited by captopril and, to a lesser extent, by lisinopril, trandolaprilat, fosinoprilat and enalaprilat. Ref.2 Ref.9

Subcellular location

Secretedextracellular space.

Tissue specificity

Expressed in vesicular structures in spermatocytes and early spermatids (at protein level). Ref.11

Developmental stage

Expressed in the amnioserosa during germ band elongation, shortening and heart morphogenesis. Expressed in midgut throughout embryogenesis.

Post-translational modification

Glycosylated. Ref.9

Disruption phenotype

Male flies are sterile. Ref.11

Sequence similarities

Belongs to the peptidase M2 family.

Biophysicochemical properties

Kinetic parameters:

KM=33.5 µM for angiotensin I Ref.2 Ref.9 Ref.10

KM=53.4 µM for N-acetyl-Ser-Asp-Lys-Pro

KM=2.59 mM for Hip-His-Leu

KM=10.26 mM for Hip-His-Leu-NH2

KM=372 µM for (Leu5)enkephalin

KM=1.88 mM for (Leu5)enkephalinamide

Binary interactions

With

Entry

#Exp.

IntAct

Notes

AGTP010192EBI-115736,EBI-751728From a different organism.
KNG1P010422EBI-115736,EBI-6378713From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717
Chain18 – 615598Angiotensin-converting enzyme
PRO_0000028563

Sites

Active site3681
Metal binding3671Zinc; catalytic
Metal binding3711Zinc; catalytic
Metal binding3951Zinc; catalytic

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Probable
Glycosylation1961N-linked (GlcNAc...) Probable
Glycosylation3111N-linked (GlcNAc...) Probable
Disulfide bond133 ↔ 141
Disulfide bond336 ↔ 354
Disulfide bond467 ↔ 612
Disulfide bond522 ↔ 540

Experimental info

Sequence conflict48 – 514WAYG → GPMR in AAC46902. Ref.4
Sequence conflict1411C → S in AAC46902. Ref.4
Sequence conflict2931G → A in AAB02171. Ref.2
Sequence conflict3461T → I Ref.1
Sequence conflict3461T → I in AAB02171. Ref.2
Sequence conflict3461T → I in AAC46902. Ref.4
Sequence conflict3461T → I Ref.5
Sequence conflict3651V → E Ref.1
Sequence conflict4021S → A Ref.1
Sequence conflict4141I → T Ref.1
Sequence conflict4861S → T in AAC46902. Ref.4
Sequence conflict5331V → M in AAC46902. Ref.4
Sequence conflict5471A → R in AAB02171. Ref.2

Secondary structure

............................................................................................. 615
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q10714 [UniParc].

Last modified September 11, 2007. Version 3.
Checksum: 9E3691BCC51D6C48

FASTA61570,914
        10         20         30         40         50         60 
MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY GSNITDENEK 

        70         80         90        100        110        120 
KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL TKLGYAALPE DDYAELLDTL 

       130        140        150        160        170        180 
SAMESNFAKV KVCDYKDSTK CDLALDPEIE EVISKSRDHE ELAYYWREFY DKAGTAVRSQ 

       190        200        210        220        230        240 
FERYVELNTK AAKLNNFTSG AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR 

       250        260        270        280        290        300 
KHYGDAVVSE TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF 

       310        320        330        340        350        360 
QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR IKQCTRVTQD 

       370        380        390        400        410        420 
QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LEKIGLLKDY 

       430        440        450        460        470        480 
VRDDEARINQ LFLTALDKIV FLPFAFTMDK YRWSLFRGEV DKANWNCAFW KLRDEYSGIE 

       490        500        510        520        530        540 
PPVVRSEKDF DAPAKYHISA DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC 

       550        560        570        580        590        600 
DIYGSAAAGA AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN 

       610 
NVHIGWTTSN KCVSS 

« Hide

References

« Hide 'large scale' references
[1]"Characterisation of putative Drosophila angiotensin converting enzyme cDNA clones."
Cornell M.J., Coates D., Isaac R.E.
Biochem. Soc. Trans. 21:243-243(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]"Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster."
Cornell M.J., Williams T.A., Lamango N.S., Coates D., Corvol P., Soubrier F., Hoheisel J., Lehrach H., Isaac R.E.
J. Biol. Chem. 270:13613-13619(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[3]Cornell M.J.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Race: a Drosophila homologue of the angiotensin converting enzyme."
Tatei K., Cai H., Ip Y.T., Levine M.
Mech. Dev. 51:157-168(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Canton-S.
[5]"An exploration of the sequence of a 2.9-Mb region of the genome of Drosophila melanogaster: the Adh region."
Ashburner M., Misra S., Roote J., Lewis S.E., Blazej R.G., Davis T., Doyle C., Galle R.F., George R.A., Harris N.L., Hartzell G., Harvey D.A., Hong L., Houston K.A., Hoskins R.A., Johnson G., Martin C., Moshrefi A.R. expand/collapse author list , Palazzolo M., Reese M.G., Spradling A.C., Tsang G., Wan K.H., Whitelaw K., Celniker S.E., Rubin G.M.
Genetics 153:179-219(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Berkeley.
[6]"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.
[7]"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.
[8]"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.
[9]"Drosophila melanogaster angiotensin I-converting enzyme expressed in Pichia pastoris resembles the C domain of the mammalian homologue and does not require glycosylation for secretion and enzymic activity."
Williams T.A., Michaud A., Houard X., Chauvet M.-T., Soubrier F., Corvol P.
Biochem. J. 318:125-131(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE SITE, GLYCOSYLATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
[10]"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.
[11]"The Drosophila angiotensin-converting enzyme homologue Ance is required for spermiogenesis."
Hurst D., Rylett C.M., Isaac R.E., Shirras A.D.
Dev. Biol. 254:238-247(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, FUNCTION, DISRUPTION PHENOTYPE.
[12]"Crystal structure of Drosophila angiotensin I-converting enzyme bound to captopril and lisinopril."
Kim H.M., Shin D.R., Yoo O.J., Lee H., Lee J.-O.
FEBS Lett. 538:65-70(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 14-615, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH CAPTOPRIL, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 14-615 IN COMPLEX WITH LISINOPRIL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_477046.1. NM_057698.4.
NP_723852.1. NM_165070.2.
UniGeneDm.2157.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ10714.
SMRQ10714. Positions 17-614.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid60835. 2 interactions.
IntActQ10714. 3 interactions.
MINTMINT-808657.

Protein family/group databases

MEROPSM02.003.

Proteomic databases

PaxDbQ10714.
PRIDEQ10714.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaFBtr0080552; FBpp0080129; FBgn0012037.
FBtr0080553; FBpp0080130; FBgn0012037.
GeneID34805.
KEGGdme:Dmel_CG8827.

Organism-specific databases

CTD34805.
FlyBaseFBgn0012037. Ance.

Phylogenomic databases

eggNOGNOG71044.
GeneTreeENSGT00520000055576.
InParanoidQ10714.
KOK01283.
OMASAMLEYF.
OrthoDBEOG76HQ13.
PhylomeDBQ10714.

Enzyme and pathway databases

SABIO-RKQ10714.

Gene expression databases

BgeeQ10714.

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

EvolutionaryTraceQ10714.
GenomeRNAi34805.
NextBio790306.

Entry information

Entry nameACE_DROME
AccessionPrimary (citable) accession number: Q10714
Secondary accession number(s): A4V0P3 expand/collapse secondary AC list , Q27572, Q9NKE4, Q9TX66, Q9VJV3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: March 19, 2014
This is version 131 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Drosophila

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