GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

DROME:ACE

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) Ance (synonyms: Race)
Protein Name(s) Angiotensin-converting enzyme

Dipeptidyl carboxypeptidase I Kininase II

External Links
UniProt Q10714
EMBL U25344
U34599
AE014134
AE014134
AY061129
RefSeq NP_001285915.1
NP_477046.1
NP_723852.1
UniGene Dm.2157
PDB 1J36
1J37
1J38
2X8Y
2X8Z
2X90
2X91
2X92
2X93
2X94
2X95
2X96
2X97
2XHM
3ZQZ
4AA1
4AA2
4ASQ
4ASR
4CA7
4CA8
PDBsum 1J36
1J37
1J38
2X8Y
2X8Z
2X90
2X91
2X92
2X93
2X94
2X95
2X96
2X97
2XHM
3ZQZ
4AA1
4AA2
4ASQ
4ASR
4CA7
4CA8
ProteinModelPortal Q10714
SMR Q10714
BioGrid 60835
IntAct Q10714
MINT MINT-808657
MEROPS M02.003
PaxDb Q10714
PRIDE Q10714
EnsemblMetazoa FBtr0080552
FBtr0080553
GeneID 34805
KEGG dme:Dmel_CG8827
CTD 34805
FlyBase FBgn0012037
eggNOG NOG71044
GeneTree ENSGT00520000055576
InParanoid Q10714
KO K01283
OMA PFAYLMD
OrthoDB EOG76HQ13
PhylomeDB Q10714
SABIO-RK Q10714
EvolutionaryTrace Q10714
GenomeRNAi 34805
NextBio 790306
Proteomes UP000000803
Bgee Q10714
GO GO:0005615
GO:0016020
GO:0004180
GO:0046872
GO:0008237
GO:0008241
GO:0007552
GO:0006508
GO:0009609
GO:0007291
GO:0007289
InterPro IPR001548
PANTHER PTHR10514
Pfam PF01401
PRINTS PR00791
PROSITE PS00142

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0008241

peptidyl-dipeptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0012037
FB:FBgn0016122
MGI:MGI:87874
PANTHER:PTN000053976
RGD:2493
UniProtKB:P12821

F

Seeded From UniProt

complete

enables

GO:0008239

dipeptidyl-peptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000053976
UniProtKB:F1NYM0
UniProtKB:Q10751

F

Seeded From UniProt

complete

enables

GO:0008238

exopeptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001630211
UniProtKB:P12821

F

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:87874
PANTHER:PTN000053976
RGD:2493
UniProtKB:P12821

F

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1917258
MGI:MGI:87874
PANTHER:PTN001630211
RGD:2493
UniProtKB:P12821
UniProtKB:Q9BYF1

C

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0012037
FB:FBgn0016122
PANTHER:PTN001630211
RGD:2493
RGD:728890
UniProtKB:F1NYM0
UniProtKB:P12821
UniProtKB:Q9BYF1

C

Seeded From UniProt

complete

involved_in

GO:0009609

response to symbiotic bacterium

PMID:18171476[2]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0009609

response to symbiotic bacterium

PMID:18171476[2]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

PMID:17921161[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0008241

peptidyl-dipeptidase activity

PMID:17921161[3]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

PMID:17921161[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007289

spermatid nucleus differentiation

PMID:12591244[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007291

sperm individualization

PMID:12591244[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0007552

metamorphosis

PMID:12093364[5]

ECO:0000270

expression pattern evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008241

peptidyl-dipeptidase activity

PMID:10913309[6]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008241

peptidyl-dipeptidase activity

PMID:7775412[7]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001548

P

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001548

F

Seeded From UniProt

complete

enables

GO:0008241

peptidyl-dipeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001548

F

Seeded From UniProt

complete

part_of

GO:0016020

membrane

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001548

C

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

enables

GO:0008233

peptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0645

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

enables

GO:0004180

carboxypeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0121

F

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0482

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964

C

Seeded From UniProt

complete

part_of

GO:0005615

extracellular space

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0112

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 1.3 1.4 1.5 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. ↑ 2.0 2.1 Xi, Z et al. (2008) Genome-wide analysis of the interaction between the endosymbiotic bacterium Wolbachia and its Drosophila host. BMC Genomics 9 1 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Rylett, CM et al. (2007) Male accessory glands of Drosophila melanogaster make a secreted angiotensin I-converting enzyme (ANCE), suggesting a role for the peptide-processing enzyme in seminal fluid. J. Exp. Biol. 210 3601-6 PubMed GONUTS page
  4. ↑ 4.0 4.1 Hurst, D et al. (2003) The drosophila angiotensin-converting enzyme homologue Ance is required for spermiogenesis. Dev. Biol. 254 238-47 PubMed GONUTS page
  5. ↑ Siviter, RJ et al. (2002) Ance, a Drosophila angiotensin-converting enzyme homologue, is expressed in imaginal cells during metamorphosis and is regulated by the steroid, 20-hydroxyecdysone. Biochem. J. 367 187-93 PubMed GONUTS page
  6. ↑ Coates, D et al. (2000) Functional conservation of the active sites of human and Drosophila angiotensin I-converting enzyme. Biochemistry 39 8963-9 PubMed GONUTS page
  7. ↑ Cornell, MJ et al. (1995) Cloning and expression of an evolutionary conserved single-domain angiotensin converting enzyme from Drosophila melanogaster. J. Biol. Chem. 270 13613-9 PubMed GONUTS page
Retrieved from "https://gowiki.tamu.edu/wiki/index.php?title=DROME:ACE&oldid=5939613"