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Angiotensin-converting enzyme-related protein (EC 3.4.15.1)

 ACER_DROME              Reviewed;         630 AA.
Q9VLJ6; Q24222;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
28-MAR-2018, entry version 132.
RecName: Full=Angiotensin-converting enzyme-related protein;
EC=3.4.15.1;
Flags: Precursor;
Name=Acer; ORFNames=CG10593;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND DEVELOPMENTAL STAGE.
PubMed=8973330; DOI=10.1016/S0378-1119(96)00503-3;
Taylor C.A.M., Coates D., Shirras A.D.;
"The Acer gene of Drosophila codes for an angiotensin-converting
enzyme homologue.";
Gene 181:191-197(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
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.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
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.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
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.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[5]
BIOPHYSICOCHEMICAL PROPERTIES, GLYCOSYLATION, SUBCELLULAR LOCATION,
AND ENZYME REGULATION.
PubMed=9839949; DOI=10.1046/j.1432-1327.1998.2570599.x;
Houard X., Williams T.A., Michaud A., Dani P., Isaac R.E.,
Shirras A.D., Coates D., Corvol P.;
"The Drosophila melanogaster-related angiotensin-I-converting enzymes
Acer and Ance -- distinct enzymic characteristics and alternative
expression during pupal development.";
Eur. J. Biochem. 257:599-606(1998).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12075344; DOI=10.1038/nature00786;
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.;
"Angiotensin-converting enzyme 2 is an essential regulator of heart
function.";
Nature 417:822-828(2002).
-!- 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.
{ECO:0000269|PubMed:12075344}.
-!- 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:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by captopril, lisinopril,
trandolaprilat, fosinoprilat and enalaprilat.
{ECO:0000269|PubMed:9839949}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.2 mM for Hip-His-Leu {ECO:0000269|PubMed:9839949};
KM=4.35 mM for Hip-His-Leu-NH(2) {ECO:0000269|PubMed:9839949};
KM=40.6 uM for (Leu5)enkephalin {ECO:0000269|PubMed:9839949};
KM=949 uM for (Leu5)enkephalinamide
{ECO:0000269|PubMed:9839949};
pH dependence:
Optimum pH is 8.6. {ECO:0000269|PubMed:9839949};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:9839949}.
-!- DEVELOPMENTAL STAGE: Expressed in presumptive heart cells during
dorsal closure. {ECO:0000269|PubMed:8973330}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:9839949}.
-!- DISRUPTION PHENOTYPE: Defective heart morphogenesis leading to
lethality. {ECO:0000269|PubMed:12075344}.
-!- MISCELLANEOUS: In contrast to ance, does not hydrolyze angiotensin
I.
-!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X96913; CAA65632.1; -; mRNA.
EMBL; AE014134; AAF52693.1; -; Genomic_DNA.
EMBL; AY051750; AAK93174.1; -; mRNA.
PIR; JC5374; JC5374.
RefSeq; NP_001260258.1; NM_001273329.1.
RefSeq; NP_477195.1; NM_057847.4.
UniGene; Dm.1852; -.
ProteinModelPortal; Q9VLJ6; -.
SMR; Q9VLJ6; -.
BioGrid; 60309; 2.
IntAct; Q9VLJ6; 2.
STRING; 7227.FBpp0305608; -.
MEROPS; M02.002; -.
PaxDb; Q9VLJ6; -.
PRIDE; Q9VLJ6; -.
EnsemblMetazoa; FBtr0079685; FBpp0079297; FBgn0016122.
EnsemblMetazoa; FBtr0333416; FBpp0305608; FBgn0016122.
GeneID; 34189; -.
KEGG; dme:Dmel_CG10593; -.
CTD; 34189; -.
FlyBase; FBgn0016122; Acer.
eggNOG; KOG3690; Eukaryota.
eggNOG; ENOG410XPJ3; LUCA.
GeneTree; ENSGT00520000055576; -.
InParanoid; Q9VLJ6; -.
KO; K01283; -.
OMA; NCDIFGS; -.
OrthoDB; EOG091G033S; -.
PhylomeDB; Q9VLJ6; -.
SABIO-RK; Q9VLJ6; -.
GenomeRNAi; 34189; -.
PRO; PR:Q9VLJ6; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0016122; -.
ExpressionAtlas; Q9VLJ6; differential.
Genevisible; Q9VLJ6; DM.
GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:FlyBase.
GO; GO:0016020; C:membrane; IEA:InterPro.
GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; ISS:FlyBase.
GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:FlyBase.
GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
GO; GO:0007507; P:heart development; IMP:UniProtKB.
GO; GO:0003007; P:heart morphogenesis; IMP:FlyBase.
GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
GO; GO:0006508; P:proteolysis; TAS:UniProtKB.
GO; GO:0002027; P:regulation of heart rate; IMP:FlyBase.
GO; GO:0030431; P:sleep; IMP:FlyBase.
CDD; cd06461; M2_ACE; 1.
InterPro; IPR001548; Peptidase_M2.
PANTHER; PTHR10514; PTHR10514; 1.
Pfam; PF01401; Peptidase_M2; 1.
PRINTS; PR00791; PEPDIPTASEA.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Carboxypeptidase; Complete proteome; Disulfide bond; Glycoprotein;
Hydrolase; Metal-binding; Metalloprotease; Protease;
Reference proteome; Secreted; Signal; Zinc.
SIGNAL 1 22 {ECO:0000255}.
CHAIN 23 630 Angiotensin-converting enzyme-related
protein.
/FTId=PRO_0000028564.
ACT_SITE 376 376 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 375 375 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 379 379 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 403 403 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
DISULFID 142 150 {ECO:0000250}.
DISULFID 344 362 {ECO:0000250}.
DISULFID 530 548 {ECO:0000250}.
CONFLICT 236 236 F -> L (in Ref. 1; CAA65632).
{ECO:0000305}.
CONFLICT 341 341 H -> Q (in Ref. 1; CAA65632).
{ECO:0000305}.
CONFLICT 528 528 A -> V (in Ref. 1; CAA65632).
{ECO:0000305}.
SEQUENCE 630 AA; 73057 MW; 6D9355EB57773289 CRC64;
MGACNITVLL LVIMLWLPHG LSMGNSCSAS VLEARRFFEL ENEQLRRRFH EEFLSGYNYN
TNVTEANRQA MIEVYARNAE LNKRLAQQIK SSDYVQSEDA DIRRQAEHLS KLGASALNAD
DYLALQNAIS SMQTNYATAT VCSYTNRSDC SLTLEPHIQE RLSHSRDPAE LAWYWREWHD
KSGTPMRQNF AEYVRLTRKA SQLNGHRSYA DYWVQFYEDP DFERQLDATF KQLLPFYRQL
HGYVRFRLRQ HYGPDVMPAE GNIPISLLGN MWGQSWNELL DLFTPYPEKP FVDVKAEMEK
QGYTVQKLFE LGDQFFQSLG MRALPPSFWN LSVLTRPDDR HVVCHASAWD FYQDSDVRIK
MCTEVDSHYF YVVHHELGHI QYYLQYEQQP AVYRGAPNPG FHEAVGDVIA LSVMSAKHLK
AIGLIENGRL DEKSRINQLF KQALSKIVFL PFGYAVDKYR YAVFRNELDE SQWNCGFWQM
RSEFGGVEPP VFRTEKDFDP PAKYHIDADV EYLRYFAAHI FQFQFHKALC RKAGQYAPNN
SRLTLDNCDI FGSKAAGRSL SQFLSKGNSR HWKEVLEEFT GETEMDPAAL LEYFEPLYQW
LKQENSRLGV PLGWGPTDKI PSDCCGTFST


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