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Q10715 (ACE_HAEIX) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme

EC=3.4.15.1
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
Gene names
Name:ACE
OrganismHaematobia irritans exigua (Buffalo fly)
Taxonomic identifier34678 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaMuscoideaMuscidaeHaematobia

Protein attributes

Sequence length611 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 611594Angiotensin-converting enzyme
PRO_0000028565

Sites

Active site3681 By similarity
Metal binding3671Zinc; catalytic By similarity
Metal binding3711Zinc; catalytic By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation1961N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q10715 [UniParc].

Last modified November 1, 1997. Version 1.
Checksum: A43D6DF5A83ECB53

FASTA61170,506
        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 

« Hide

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.
PIRS65472.

3D structure databases

ProteinModelPortalQ10715.
SMRQ10715. Positions 23-603.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM02.003.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACE_HAEIX
AccessionPrimary (citable) accession number: Q10715
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: May 14, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries