Q10715 (ACE_HAEIX) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Angiotensin-converting enzyme
EC=3.4.15.1

Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II

Gene names

Name:

ACE

Organism

Haematobia irritans exigua (Buffalo fly)

Taxonomic identifier

34678 [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 › Calyptratae › Muscoidea › Muscidae › Muscinae › Stomoxyini › Haematobia › Haematobia irritans

Protein attributes

Sequence length	611 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Involved in the specific maturation or degradation of a number of bioactive peptides.
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.
Subcellular location	Secreted › extracellular space Probable.
Tissue specificity	Expressed in the compound ganglion and in the posterior region of the midgut.
Sequence similarities	Belongs to the peptidase M2 family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Carboxypeptidase Hydrolase Metalloprotease Protease
PTM	Glycoprotein
Gene Ontology (GO)
Biological_process	proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	carboxypeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW peptidyl-dipeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 611	594	Angiotensin-converting enzyme		PRO_0000028565
Sites
	Active site	368	1	By similarity
	Metal binding	367	1	Zinc; catalytic By similarity
	Metal binding	371	1	Zinc; catalytic By similarity
Amino acid modifications
	Glycosylation	53	1	N-linked (GlcNAc...) Potential
	Glycosylation	196	1	N-linked (GlcNAc...) Potential
	Glycosylation	531	1	N-linked (GlcNAc...) Potential

Sequences

	Sequence		Length	Mass (Da)
	Q10715 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: A43D6DF5A83ECB53	FASTA	611	70,506
	10 20 30 40 50 60 MKLLVVTILA GLAVCHGATK EEIVATEYLQ NINKELAKHT NVETEVSWAY ASNITDENER 70 80 90 100 110 120 LRNEISAENA KFLKEVAKDI QKFNWRTYGS ADVRRQFKSL SKTGYSALPA EDYAELLEVL 130 140 150 160 170 180 SAMESNFAKV RVCDYKNSAK CDLSLDPEIE EIITKSRDPE ELKYYWTQFY DKAGTPTRSN 190 200 210 220 230 240 FEKYVELNTK SAKLNNFTDG AEVWLDEYED ATFEDQLEAI FEDIKPLYDQ VHGYVRYRLN 250 260 270 280 290 300 KFYGDEVVSK TGPLPMHLLG NMWAQQWSSI ADIVSPFPEK PLVDVSDEMV AQGYTPLKMF 310 320 330 340 350 360 QMGDDFFQSM GLKKLPQEFW DKSILEKPDD GRDLVCHASA WDFYLTDDVR IKQCTRVTQD 370 380 390 400 410 420 QFFTVHHEMG HIQYFLQYQH QPFVYRTGAN PGFHEAVGDV LSLSVSTPKH LERVGLLKNY 430 440 450 460 470 480 VSDNEARINQ LFLTALDKIV FLPFAFTMDK YRWALFRGQA DKSEWNCAFW KLREEYSGIE 490 500 510 520 530 540 PPVVRTEKDF DAPAKYHVSA DVEYLRYLVS FIIQFQFYKS ACITAGEYVP NQTEYPLDNC 550 560 570 580 590 600 DIYGSKEAGK LFENMLSLGA SKPWPDALEA FNGERTMTGK AIAEYFEPLR VWLEAVAVES 610 LCHQRYKNVD L

References

[1]

"Cloning and characterisation of angiotensin-converting enzyme from the dipteran species, Haematobia irritans exigua, and its expression in the maturing male reproductive system." Wijffels G.L., Fitzgerald C., Gough J., Riding G.A., Elvin C., Kemp D.J., Willadsen P. Eur. J. Biochem. 237:414-423(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	L43965 Genomic DNA. Translation: AAA70427.1.
PIR	S65472.
3D structure databases
ProteinModelPortal	Q10715.
SMR	Q10715. Positions 23-603.
ModBase	Search...
Protein family/group databases
MEROPS	M02.003.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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...

Entry information

Entry name

ACE_HAEIX

Accession

Primary (citable) accession number: Q10715

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	April 3, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)