Angiotensin-converting enzyme precursor - Theromyzon tessulatum (Duck leech)

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Q6Q4G4 (ACE_THETS) Reviewed, UniProtKB/Swiss-Prot

Last modified October 3, 2012. Version 35. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Angiotensin-converting enzyme
EC=3.4.15.1

Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
TtACE

Gene names

Name:

ACE

Organism

Theromyzon tessulatum (Duck leech)

Taxonomic identifier

Taxonomic lineage

Eukaryota › Metazoa › Lophotrochozoa › Annelida › Clitellata › Hirudinida › Hirudinea › Rhynchobdellida › Glossiphoniidae › Theromyzon

Protein attributes

Sequence length	616 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)

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	Secreted › extracellular 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.

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

23

Potential

Chain

593

Angiotensin-converting enzyme

PRO_0000028566

Sites

Active site

1

By similarity

Metal binding

1

Zinc; catalytic By similarity

Metal binding

1

Zinc; catalytic By similarity

Amino acid modifications

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Glycosylation

1

N-linked (GlcNAc...) Potential

Sequences

Sequence

Length

Mass (Da)

Tools

Q6Q4G4 [UniParc].

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

616

71,481

        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

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
ProteinModelPortal	Q6Q4G4.
ModBase	Search...
Protein family/group databases
MEROPS	M02.005.
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.
ProtoNet	Search...

Entry information

Entry name

ACE_THETS

Accession

Primary (citable) accession number: Q6Q4G4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	July 5, 2004
Last modified:	October 3, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents