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Q10714

- ACE_DROME

UniProt

Q10714 - ACE_DROME

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Protein

Angiotensin-converting enzyme

Gene

Ance

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - 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 play a role in the contractions of the heart, gut and testes, and in spermatid differentiation.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.1 Publication

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Enzyme regulationi

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

Kineticsi

  1. KM=33.5 µM for angiotensin I3 Publications
  2. KM=53.4 µM for N-acetyl-Ser-Asp-Lys-Pro3 Publications
  3. KM=2.59 mM for Hip-His-Leu3 Publications
  4. KM=10.26 mM for Hip-His-Leu-NH23 Publications
  5. KM=372 µM for (Leu5)enkephalin3 Publications
  6. KM=1.88 mM for (Leu5)enkephalinamide3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi367 – 3671Zinc; catalytic
Active sitei368 – 3681
Metal bindingi371 – 3711Zinc; catalytic
Metal bindingi395 – 3951Zinc; catalytic

GO - Molecular functioni

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

GO - Biological processi

  1. metamorphosis Source: FlyBase
  2. proteolysis Source: FlyBase
  3. response to symbiotic bacterium Source: FlyBase
  4. spermatid nucleus differentiation Source: FlyBase
  5. sperm individualization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

SABIO-RKQ10714.

Protein family/group databases

MEROPSiM02.003.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.4.15.1)
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
Gene namesi
Name:Ance
Synonyms:Race
ORF Names:CG8827
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0012037. Ance.

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: FlyBase
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Disruption phenotypei

Male flies are sterile.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Add
BLAST
Chaini18 – 615598Angiotensin-converting enzymePRO_0000028563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)1 Publication
Disulfide bondi133 ↔ 141
Glycosylationi196 – 1961N-linked (GlcNAc...)1 Publication
Glycosylationi311 – 3111N-linked (GlcNAc...)1 Publication
Disulfide bondi336 ↔ 354
Disulfide bondi467 ↔ 612
Disulfide bondi522 ↔ 540

Post-translational modificationi

Glycosylated.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ10714.
PRIDEiQ10714.

Expressioni

Tissue specificityi

Expressed in vesicular structures in spermatocytes and early spermatids (at protein level).1 Publication

Developmental stagei

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

Gene expression databases

BgeeiQ10714.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTP010192EBI-115736,EBI-751728From a different organism.
KNG1P010422EBI-115736,EBI-6378713From a different organism.

Protein-protein interaction databases

BioGridi60835. 2 interactions.
IntActiQ10714. 3 interactions.
MINTiMINT-808657.

Structurei

Secondary structure

1
615
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi20 – 223Combined sources
Helixi26 – 5126Combined sources
Helixi56 – 8025Combined sources
Helixi85 – 873Combined sources
Helixi91 – 10111Combined sources
Helixi104 – 1074Combined sources
Helixi110 – 12920Combined sources
Turni145 – 1473Combined sources
Helixi148 – 1558Combined sources
Helixi159 – 17315Combined sources
Helixi175 – 1773Combined sources
Helixi178 – 19417Combined sources
Helixi200 – 2056Combined sources
Helixi206 – 2083Combined sources
Helixi213 – 24331Combined sources
Turni245 – 2473Combined sources
Beta strandi250 – 2523Combined sources
Helixi256 – 2583Combined sources
Beta strandi259 – 2613Combined sources
Helixi268 – 2703Combined sources
Helixi271 – 2744Combined sources
Beta strandi278 – 2803Combined sources
Helixi286 – 2916Combined sources
Helixi296 – 30914Combined sources
Helixi317 – 3226Combined sources
Beta strandi329 – 3313Combined sources
Beta strandi339 – 3424Combined sources
Beta strandi344 – 3474Combined sources
Beta strandi349 – 3524Combined sources
Helixi359 – 37719Combined sources
Turni378 – 3803Combined sources
Helixi383 – 3853Combined sources
Helixi391 – 40515Combined sources
Helixi408 – 4136Combined sources
Beta strandi416 – 4194Combined sources
Helixi424 – 43815Combined sources
Helixi441 – 45616Combined sources
Turni457 – 4593Combined sources
Helixi462 – 4643Combined sources
Helixi465 – 47713Combined sources
Helixi492 – 4943Combined sources
Helixi496 – 4994Combined sources
Helixi505 – 52420Combined sources
Turni525 – 5273Combined sources
Beta strandi530 – 5356Combined sources
Helixi537 – 5393Combined sources
Helixi546 – 55611Combined sources
Turni557 – 5604Combined sources
Helixi564 – 5729Combined sources
Helixi580 – 59920Combined sources
Beta strandi611 – 6133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliQ10714.
SMRiQ10714. Positions 19-614.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ10714.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG71044.
GeneTreeiENSGT00520000055576.
InParanoidiQ10714.
KOiK01283.
OMAiWAYGSNI.
OrthoDBiEOG76HQ13.
PhylomeDBiQ10714.

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.

Q10714-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRLFLLALLA TLAVTQALVK EEIQAKEYLE NLNKELAKRT NVETEAAWAY
60 70 80 90 100
GSNITDENEK KKNEISAELA KFMKEVASDT TKFQWRSYQS EDLKRQFKAL
110 120 130 140 150
TKLGYAALPE DDYAELLDTL SAMESNFAKV KVCDYKDSTK CDLALDPEIE
160 170 180 190 200
EVISKSRDHE ELAYYWREFY DKAGTAVRSQ FERYVELNTK AAKLNNFTSG
210 220 230 240 250
AEAWLDEYED DTFEQQLEDI FADIRPLYQQ IHGYVRFRLR KHYGDAVVSE
260 270 280 290 300
TGPIPMHLLG NMWAQQWSEI ADIVSPFPEK PLVDVSAEME KQGYTPLKMF
310 320 330 340 350
QMGDDFFTSM NLTKLPQDFW DKSIIEKPTD GRDLVCHASA WDFYLTDDVR
360 370 380 390 400
IKQCTRVTQD QLFTVHHELG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV
410 420 430 440 450
LSLSVSTPKH LEKIGLLKDY VRDDEARINQ LFLTALDKIV FLPFAFTMDK
460 470 480 490 500
YRWSLFRGEV DKANWNCAFW KLRDEYSGIE PPVVRSEKDF DAPAKYHISA
510 520 530 540 550
DVEYLRYLVS FIIQFQFYKS ACIKAGQYDP DNVELPLDNC DIYGSAAAGA
560 570 580 590 600
AFHNMLSMGA SKPWPDALEA FNGERIMSGK AIAEYFEPLR VWLEAENIKN
610
NVHIGWTTSN KCVSS
Length:615
Mass (Da):70,914
Last modified:September 11, 2007 - v3
Checksum:i9E3691BCC51D6C48
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 514WAYG → GPMR in AAC46902. (PubMed:7547464)Curated
Sequence conflicti141 – 1411C → S in AAC46902. (PubMed:7547464)Curated
Sequence conflicti293 – 2931G → A in AAB02171. (PubMed:7775412)Curated
Sequence conflicti346 – 3461T → I(PubMed:8224398)Curated
Sequence conflicti346 – 3461T → I in AAB02171. (PubMed:7775412)Curated
Sequence conflicti346 – 3461T → I in AAC46902. (PubMed:7547464)Curated
Sequence conflicti346 – 3461T → I(PubMed:10471707)Curated
Sequence conflicti365 – 3651V → E(PubMed:8224398)Curated
Sequence conflicti402 – 4021S → A(PubMed:8224398)Curated
Sequence conflicti414 – 4141I → T(PubMed:8224398)Curated
Sequence conflicti486 – 4861S → T in AAC46902. (PubMed:7547464)Curated
Sequence conflicti533 – 5331V → M in AAC46902. (PubMed:7547464)Curated
Sequence conflicti547 – 5471A → R in AAB02171. (PubMed:7775412)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
RefSeqiNP_001285915.1. NM_001298986.1.
NP_477046.1. NM_057698.5.
NP_723852.1. NM_165070.3.
UniGeneiDm.2157.

Genome annotation databases

EnsemblMetazoaiFBtr0080552; FBpp0080129; FBgn0012037.
FBtr0080553; FBpp0080130; FBgn0012037.
GeneIDi34805.
KEGGidme:Dmel_CG8827.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
RefSeqi NP_001285915.1. NM_001298986.1.
NP_477046.1. NM_057698.5.
NP_723852.1. NM_165070.3.
UniGenei Dm.2157.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1J36 X-ray 2.40 A/B 14-615 [» ]
1J37 X-ray 2.40 A/B 14-615 [» ]
1J38 X-ray 2.60 A/B 14-615 [» ]
2X8Y X-ray 1.90 A 17-614 [» ]
2X8Z X-ray 1.98 A 17-614 [» ]
2X90 X-ray 1.98 A 17-614 [» ]
2X91 X-ray 1.98 A 17-614 [» ]
2X92 X-ray 2.11 A 17-615 [» ]
2X93 X-ray 1.98 A 17-615 [» ]
2X94 X-ray 1.88 A 17-615 [» ]
2X95 X-ray 1.96 A 17-615 [» ]
2X96 X-ray 1.85 A 17-614 [» ]
2X97 X-ray 1.85 A 17-614 [» ]
2XHM X-ray 1.96 A 17-614 [» ]
3ZQZ X-ray 2.35 A 17-614 [» ]
4AA1 X-ray 1.99 A 17-614 [» ]
4AA2 X-ray 1.99 A 17-614 [» ]
4ASQ X-ray 1.99 A 17-614 [» ]
4ASR X-ray 1.90 A 17-614 [» ]
4CA7 X-ray 1.82 A 17-614 [» ]
4CA8 X-ray 1.99 A 17-614 [» ]
ProteinModelPortali Q10714.
SMRi Q10714. Positions 19-614.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 60835. 2 interactions.
IntActi Q10714. 3 interactions.
MINTi MINT-808657.

Protein family/group databases

MEROPSi M02.003.

Proteomic databases

PaxDbi Q10714.
PRIDEi Q10714.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0080552 ; FBpp0080129 ; FBgn0012037 .
FBtr0080553 ; FBpp0080130 ; FBgn0012037 .
GeneIDi 34805.
KEGGi dme:Dmel_CG8827.

Organism-specific databases

CTDi 34805.
FlyBasei FBgn0012037. Ance.

Phylogenomic databases

eggNOGi NOG71044.
GeneTreei ENSGT00520000055576.
InParanoidi Q10714.
KOi K01283.
OMAi WAYGSNI.
OrthoDBi EOG76HQ13.
PhylomeDBi Q10714.

Enzyme and pathway databases

SABIO-RK Q10714.

Miscellaneous databases

EvolutionaryTracei Q10714.
GenomeRNAii 34805.
NextBioi 790306.

Gene expression databases

Bgeei Q10714.

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

« Hide 'large scale' publications
  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.
    , 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.
    , 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. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  8. 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.

Entry informationi

Entry nameiACE_DROME
AccessioniPrimary (citable) accession number: Q10714
Secondary accession number(s): A4V0P3
, Q27572, Q9NKE4, Q9TX66, Q9VJV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 11, 2007
Last modified: November 26, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3