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Q6Q4G4

- ACE_THETS

UniProt

Q6Q4G4 - ACE_THETS

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Protein
Angiotensin-converting enzyme
Gene
ACE
Organism
Theromyzon tessulatum (Duck leech)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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.1 Publication

Cofactori

Binds 1 zinc ion per subunit By similarity.
Chloride By similarity.

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi376 – 3761Zinc; catalytic By similarity
Active sitei377 – 3771 By similarity
Metal bindingi380 – 3801Zinc; catalytic By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: UniProtKB-KW
  4. peptidyl-dipeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM02.005.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.4.15.1)
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
TtACE
Gene namesi
Name:ACE
OrganismiTheromyzon tessulatum (Duck leech)
Taxonomic identifieri13286 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaAnnelidaClitellataHirudinidaHirudineaRhynchobdellidaGlossiphoniidaeTheromyzon

Subcellular locationi

GO - Cellular componenti

  1. extracellular space Source: UniProtKB-SubCell
  2. membrane Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323 Reviewed prediction
Add
BLAST
Chaini24 – 616593Angiotensin-converting enzyme
PRO_0000028566Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi61 – 611N-linked (GlcNAc...) Reviewed prediction
Glycosylationi96 – 961N-linked (GlcNAc...) Reviewed prediction
Glycosylationi303 – 3031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi428 – 4281N-linked (GlcNAc...) Reviewed prediction
Glycosylationi535 – 5351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi573 – 5731N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Expressioni

Tissue specificityi

Epithelial cells of the midgut.1 Publication

Developmental stagei

Expressed at stages 1 and 2.

Structurei

3D structure databases

ProteinModelPortaliQ6Q4G4.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M2 family.

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6Q4G4-1 [UniParc]FASTAAdd to Basket

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MNLINFSYLN LLFGAGLFSV LESATILNTE SDAKKWLTTY NDEAGKYIYD    50
ATEAEWNYNT NLTDHNLGIS IKKSNDLATF TEQKAIEANK KFVWKNFTDP 100
LLKREFSKIT DIGTASLSDE DFQKMSGLNS DLTKIYSTAK VCNKPNDPSG 150
KCYPLDPDLS DIISKSNDLE ELTWAWKGWR DASGKHMPDK YDEFVQLLNK 200
AANINGYEDN GDYWRSWYES PTFRKDCEDL WQEIKPFYEQ LHAYVRRKLQ 250
KKYPQIAFPK EGHIPAHLLG NMWAQSWENI EYLLRPAPDL PSMDITEELV 300
KQNYTALKLF QLSDTFFKSL GLIQMPQPFW EKSMIEKPAD RDVVCHASAW 350
DFYNRKDFRI KQCTVVDMHW FMTTHHEMGH IEYYLHYKDQ PISFRSGANP 400
GFHEAIADIA SLSVATPEYM QSVSLLPNFT DDPNGDLNFL MNQALTKVAF 450
LPFGYLIDQW RWDVFSGDTP RPKYNSKWWH NRCKYQGVYP PVIRSEQDFD 500
AGSKFHVPNN TPYIRYFVAH IIQFQFHEAL CKAANNSRPL HRCNIANSKE 550
AGKKLAELMK SGSSIPWPKV LENLTGSEKM SAKSLMAYYK PLIDWPEKRK 600
PRAENWMGGK MSSWIV 616
Length:616
Mass (Da):71,481
Last modified:July 5, 2004 - v1
Checksum:i70171D38354349FC
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY560004 mRNA. Translation: AAS57725.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY560004 mRNA. Translation: AAS57725.1 .

3D structure databases

ProteinModelPortali Q6Q4G4.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

MEROPSi M02.005.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 1 hit.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiACE_THETS
AccessioniPrimary (citable) accession number: Q6Q4G4
Entry historyi
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 statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi