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Q6Q4G4

- ACE_THETS

UniProt

Q6Q4G4 - ACE_THETS

Protein

Angiotensin-converting enzyme

Gene

ACE

Organism
Theromyzon tessulatum (Duck leech)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 37 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    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; catalyticBy similarity
    Active sitei377 – 3771By similarity
    Metal bindingi380 – 3801Zinc; catalyticBy 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

    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

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 616593Angiotensin-converting enzymePRO_0000028566Add
    BLAST

    Amino acid modifications

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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    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

    « Hide

    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: October 1, 2014
    This is version 37 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