Q9VLJ6 (ACER_DROME) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiotensin-converting enzyme-related protein
EC=3.4.15.1

Gene names

Name:	Acer
ORF Names:	CG10593

Organism

Drosophila melanogaster (Fruit fly) [Reference proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Protostomia › Ecdysozoa › Panarthropoda › Arthropoda › Mandibulata › Pancrustacea › Hexapoda › Insecta › Dicondylia › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Eremoneura › Cyclorrhapha › Schizophora › Acalyptratae › Ephydroidea › Drosophilidae › Drosophilinae › Drosophilini › Drosophilina › Drosophiliti › Drosophila › Sophophora › melanogaster group › melanogaster subgroup

Protein attributes

Sequence length	630 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular 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.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	heart development Inferred from mutant phenotype Ref.6. Source: UniProtKB positive regulation of circadian sleep/wake cycle, sleep Inferred from mutant phenotype PubMed 21270318. Source: FlyBase proteolysis Traceable author statement PubMed 10961941. Source: UniProtKB sleep Inferred from mutant phenotype PubMed 21270318. Source: FlyBase
Cellular_component	extracellular space Inferred from direct assay PubMed 21270318. Source: FlyBase membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metalloendopeptidase activity Inferred from sequence or structural similarity Ref.1. Source: FlyBase peptidyl-dipeptidase activity Inferred from direct assay PubMed 10913309. Source: FlyBase zinc ion binding Inferred from sequence model Ref.1. Source: FlyBase
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CG5844	Q9VG69	1	EBI-176681,EBI-184553

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 22	22	Potential
	Chain	23 – 630	608	Angiotensin-converting enzyme-related protein		PRO_0000028564
Sites
	Active site	376	1	By similarity
	Metal binding	375	1	Zinc; catalytic By similarity
	Metal binding	379	1	Zinc; catalytic By similarity
	Metal binding	403	1	Zinc; catalytic By similarity
Amino acid modifications
	Disulfide bond	142 ↔ 150		By similarity
	Disulfide bond	344 ↔ 362		By similarity
	Disulfide bond	530 ↔ 548		By similarity
Experimental info
	Sequence conflict	236	1	F → L in CAA65632. Ref.1
	Sequence conflict	341	1	H → Q in CAA65632. Ref.1
	Sequence conflict	528	1	A → V in CAA65632. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9VLJ6 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 6D9355EB57773289	FASTA	630	73,057
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
PIR	JC5374.
RefSeq	NP_001260258.1. NM_001273329.1. NP_477195.1. NM_057847.4.
UniGene	Dm.1852.
3D structure databases
ProteinModelPortal	Q9VLJ6.
SMR	Q9VLJ6. Positions 32-622.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9VLJ6. 1 interaction.
MINT	MINT-1717838.
Protein family/group databases
MEROPS	M02.002.
Proteomic databases
PaxDb	Q9VLJ6.
PRIDE	Q9VLJ6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblMetazoa	FBtr0079685; FBpp0079297; FBgn0016122. FBtr0333416; FBpp0305608; FBgn0016122.
GeneID	34189.
KEGG	dme:Dmel_CG10593.
Organism-specific databases
CTD	34189.
FlyBase	FBgn0016122. Acer.
Phylogenomic databases
eggNOG	NOG71044.
GeneTree	ENSGT00520000055576.
InParanoid	Q9VLJ6.
KO	K01283.
OMA	YITDDTE.
OrthoDB	EOG41C5B8.
PhylomeDB	Q9VLJ6.
Gene expression databases
Bgee	Q9VLJ6.
GermOnline	CG10593. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001548. Peptidase_M2. [Graphical view]
PANTHER	PTHR10514. PTHR10514. 1 hit.
Pfam	PF01401. Peptidase_M2. 1 hit. [Graphical view]
PRINTS	PR00791. PEPDIPTASEA.
PROSITE	PS00142. ZINC_PROTEASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	34189.
NextBio	787315.

Entry information

Entry name

ACER_DROME

Accession

Primary (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:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Drosophila annotation project