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Q6Q4G4 (ACE_THETS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 36. 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
TtACE
Gene names
Name:ACE
OrganismTheromyzon tessulatum (Duck leech)
Taxonomic identifier13286 [NCBI]
Taxonomic lineageEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaRhynchobdellidaGlossiphoniidaeTheromyzon

Protein attributes

Sequence length616 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

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. Ref.1

Cofactor

Binds 1 zinc ion per subunit By similarity.

Chloride By similarity.

Enzyme regulation

Activated by chloride. Inhibited by captopril and lisinopril, and to a lesser extent by delaprilat. Ref.1

Subcellular location

Secretedextracellular space Probable.

Tissue specificity

Epithelial cells of the midgut. Ref.1

Developmental stage

Expressed at stages 1 and 2.

Sequence similarities

Belongs to the peptidase M2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 616593Angiotensin-converting enzyme
PRO_0000028566

Sites

Active site3771 By similarity
Metal binding3761Zinc; catalytic By similarity
Metal binding3801Zinc; catalytic By similarity

Amino acid modifications

Glycosylation611N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation4281N-linked (GlcNAc...) Potential
Glycosylation5351N-linked (GlcNAc...) Potential
Glycosylation5731N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q6Q4G4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 70171D38354349FC

FASTA61671,481
        10         20         30         40         50         60 
MNLINFSYLN LLFGAGLFSV LESATILNTE SDAKKWLTTY NDEAGKYIYD ATEAEWNYNT 

        70         80         90        100        110        120 
NLTDHNLGIS IKKSNDLATF TEQKAIEANK KFVWKNFTDP LLKREFSKIT DIGTASLSDE 

       130        140        150        160        170        180 
DFQKMSGLNS DLTKIYSTAK VCNKPNDPSG KCYPLDPDLS DIISKSNDLE ELTWAWKGWR 

       190        200        210        220        230        240 
DASGKHMPDK YDEFVQLLNK AANINGYEDN GDYWRSWYES PTFRKDCEDL WQEIKPFYEQ 

       250        260        270        280        290        300 
LHAYVRRKLQ KKYPQIAFPK EGHIPAHLLG NMWAQSWENI EYLLRPAPDL PSMDITEELV 

       310        320        330        340        350        360 
KQNYTALKLF QLSDTFFKSL GLIQMPQPFW EKSMIEKPAD RDVVCHASAW DFYNRKDFRI 

       370        380        390        400        410        420 
KQCTVVDMHW FMTTHHEMGH IEYYLHYKDQ PISFRSGANP GFHEAIADIA SLSVATPEYM 

       430        440        450        460        470        480 
QSVSLLPNFT DDPNGDLNFL MNQALTKVAF LPFGYLIDQW RWDVFSGDTP RPKYNSKWWH 

       490        500        510        520        530        540 
NRCKYQGVYP PVIRSEQDFD AGSKFHVPNN TPYIRYFVAH IIQFQFHEAL CKAANNSRPL 

       550        560        570        580        590        600 
HRCNIANSKE AGKKLAELMK SGSSIPWPKV LENLTGSEKM SAKSLMAYYK PLIDWPEKRK 

       610 
PRAENWMGGK MSSWIV 

« Hide

References

[1]"Characterization of the first non-insect invertebrate functional angiotensin-converting enzyme (ACE): leech TtACE resembles the N-domain of mammalian ACE."
Riviere G., Michaud A., Deloffre L., Vandenbulcke F., Levoye A., Breton C., Corvol P., Salzet M., Vieau D.
Biochem. J. 382:565-573(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], ENZYME ACTIVITY, ENZYME REGULATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY560004 mRNA. Translation: AAS57725.1.

3D structure databases

ProteinModelPortalQ6Q4G4.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSM02.005.

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.
ProtoNetSearch...

Entry information

Entry nameACE_THETS
AccessionPrimary (citable) accession number: Q6Q4G4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: July 5, 2004
Last modified: May 14, 2014
This is version 36 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