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P47820

- ACE_RAT

UniProt

P47820 - ACE_RAT

Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      Previous versions | rss
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    Functioni

    Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. This GPIase activity seems to be crucial for the egg-binding ability of the sperm By similarity.By similarity

    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.

    Cofactori

    Binds 2 zinc ions per subunit. Isoform Testis-specific only binds 1 zinc ion per subunit By similarity.By similarity
    Binds 3 chloride ions per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei237 – 2371Chloride 1By similarity
    Metal bindingi396 – 3961Zinc 1; catalyticBy similarity
    Active sitei397 – 39711PROSITE-ProRule annotation
    Metal bindingi400 – 4001Zinc 1; catalyticBy similarity
    Metal bindingi424 – 4241Zinc 1; catalyticBy similarity
    Binding sitei535 – 5351Chloride 1By similarity
    Binding sitei797 – 7971Chloride 2By similarity
    Binding sitei835 – 8351Chloride 3By similarity
    Metal bindingi994 – 9941Zinc 2; catalyticBy similarity
    Active sitei995 – 99512PROSITE-ProRule annotation
    Metal bindingi998 – 9981Zinc 2; catalyticBy similarity
    Metal bindingi1022 – 10221Zinc 2; catalyticBy similarity
    Binding sitei1096 – 10961Chloride 2By similarity
    Binding sitei1100 – 11001Chloride 2By similarity
    Binding sitei1133 – 11331Chloride 3By similarity

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. drug binding Source: RGD
    3. metal ion binding Source: UniProtKB-KW
    4. metallopeptidase activity Source: RGD
    5. peptide binding Source: RGD
    6. peptidyl-dipeptidase activity Source: RGD

    GO - Biological processi

    1. aging Source: RGD
    2. angiogenesis involved in coronary vascular morphogenesis Source: RGD
    3. bradykinin catabolic process Source: RGD
    4. brain development Source: RGD
    5. cellular response to glucose stimulus Source: RGD
    6. eating behavior Source: RGD
    7. female pregnancy Source: RGD
    8. kidney development Source: RGD
    9. lung alveolus development Source: RGD
    10. lung development Source: RGD
    11. male gonad development Source: RGD
    12. negative regulation of calcium ion import Source: RGD
    13. organ regeneration Source: RGD
    14. peptide catabolic process Source: RGD
    15. peptide metabolic process Source: RGD
    16. positive regulation of apoptotic process Source: RGD
    17. positive regulation of inflammatory response Source: RGD
    18. positive regulation of neurogenesis Source: RGD
    19. positive regulation of systemic arterial blood pressure Source: RGD
    20. proteolysis Source: RGD
    21. regulation of blood pressure Source: BHF-UCL
    22. regulation of smooth muscle cell migration Source: BHF-UCL
    23. response to dexamethasone Source: RGD
    24. response to drug Source: RGD
    25. response to hypoxia Source: RGD
    26. response to laminar fluid shear stress Source: RGD
    27. response to lipopolysaccharide Source: RGD
    28. response to nutrient levels Source: RGD
    29. response to thyroid hormone Source: RGD
    30. sensory perception of pain Source: RGD
    31. vasoconstriction Source: RGD

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_198807. Metabolism of Angiotensinogen to Angiotensins.

    Protein family/group databases

    MEROPSiM02.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Angiotensin-converting enzyme (EC:3.2.1.-, EC:3.4.15.1)
    Short name:
    ACE
    Alternative name(s):
    Dipeptidyl carboxypeptidase I
    Kininase II
    CD_antigen: CD143
    Cleaved into the following chain:
    Gene namesi
    Name:Ace
    Synonyms:Dcp1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi2493. Ace.

    Subcellular locationi

    Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasm By similarity
    Note: Detected in both cell membrane and cytoplasm in neurons.By similarity

    GO - Cellular componenti

    1. basal plasma membrane Source: RGD
    2. brush border membrane Source: RGD
    3. extracellular space Source: RGD
    4. integral component of membrane Source: UniProtKB-KW
    5. plasma membrane Source: RGD
    6. vesicle Source: RGD

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535By similarityAdd
    BLAST
    Chaini36 – 13131278Angiotensin-converting enzymePRO_0000028557Add
    BLAST
    Chaini36 – 12381203Angiotensin-converting enzyme, soluble formPRO_0000028558Add
    BLAST
    Propeptidei1239 – 131375Removed in secreted formBy similarityPRO_0000028559Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1306 – 13061PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CK2 on Ser-1306; which allows membrane retention.By similarity

    Keywords - PTMi

    Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiP47820.

    PTM databases

    PhosphoSiteiP47820.

    Expressioni

    Tissue specificityi

    Testis-specific isoform is expressed in spermatocytes, adult testis. Also expressed in brain, kidney, lung, skeletal muscle and heart.1 Publication

    Inductioni

    Up-regulated after myocardial infarction.1 Publication

    Gene expression databases

    GenevestigatoriP47820.

    Interactioni

    Protein-protein interaction databases

    MINTiMINT-204637.

    Structurei

    3D structure databases

    ProteinModelPortaliP47820.
    SMRiP47820. Positions 36-647, 651-1234.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 12651230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1283 – 131331CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1266 – 128217HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni36 – 636601Peptidase M2 1Add
    BLAST
    Regioni637 – 1238602Peptidase M2 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71044.
    HOGENOMiHOG000007838.
    HOVERGENiHBG000264.
    InParanoidiP47820.
    KOiK01283.
    PhylomeDBiP47820.
    TreeFamiTF312861.

    Family and domain databases

    InterProiIPR001548. Peptidase_M2.
    [Graphical view]
    PANTHERiPTHR10514. PTHR10514. 1 hit.
    PfamiPF01401. Peptidase_M2. 2 hits.
    [Graphical view]
    PRINTSiPR00791. PEPDIPTASEA.
    PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Somatic (identifier: P47820-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MGAASGQRGR WPLSPPLLML SLLLLLLLPP SPAPALDPGL QPGNFSADEA     50
    GAQLFADSYN SSAEVVMFQS TAASWAHDTN ITEENARLQE EAALINQEFA 100
    EVWGKKAKEL YESIWQNFTD QKLRRIIGSV QTLGPANLPL TQRLQYNSLL 150
    SNMSRIYSTG KVCFPNKTAT CWSLDPELTN ILASSRNYAK VLFAWEGWHD 200
    AVGIPLRPLY QDFTALSNEA YRQDGFSDTG AYWRSWYESP SFEESLEHLY 250
    HQVEPLYLNL HAFVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWENIY 300
    DMVVPFPDKP NLDVTSTMVQ KGWNATHMFR VAEEFFTSLG LSPMPPEFWA 350
    ESMLEKPADG REVVCHASAW DFYNRKDFRI KQCTRVTMDQ LSTVHHEMGH 400
    VQYYLQYKDL HVSLRRGANP GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA 450
    NDIESDINYL LKMALEKIAF LPFGYLVDQW RWGVFSGRTP PSRYNYDWWY 500
    LRTKYQGICP PVARNETHFD AGAKFHIPSV TPYIRYFVSF VLQFQFHQAL 550
    CKEAGHQGPL HQCDIYQSTK AGAKLQQVLQ AGCSRPWQEV LKDLVGSDAL 600
    DASALMEYFQ PVSQWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLET 650
    DEAKANRFVE EYDRTAKVLW NEYAEANWHY NTNITIEGSK ILLQKNKEVS 700
    NHTLKYGTWA KTFDVSNFQN STIKRIIKKV QNVDRAVLPP NELEEYNQIL 750
    LDMETTYSVA NVCYTNGTCL SLEPDLTNIM ATSRKYEELL WVWKSWRDKV 800
    GRAILPFFPK YVDFSNKIAK LNGYSDAGDS WRSSYESDDL EQDLEKLYQE 850
    LQPLYLNLHA YVRRSLHRHY GSEYINLDGP IPAHLLGNMW AQTWSNIYDL 900
    VAPFPSAPSI DATEAMIKQG WTPRRIFKEA DNFFTSLGLL PVPPEFWNKS 950
    MLEKPTDGRE VVCHASAWDF YNGKDFRIKQ CTSVNMEELV IAHHEMGHIQ 1000
    YFMQYKDLPV TFREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGSG 1050
    YEHDINFLMK MALDKIAFIP FSYLIDQWRW RVFDGSITKE NYNQEWWSLR 1100
    LKYQGLCPPV PRSQGDFDPG SKFHVPANVP YIRYFISFII QFQFHEALCR 1150
    AAGHTGPLYK CDIYQSKEAG KLLADAMKLG YSKQWPEAMK IITGQPNMSA 1200
    SAIMNYFKPL TEWLVTENRR HGETLGWPEY TWTPNTARAE GSLPESSRVN 1250
    FLGMYLEPQQ ARVGQWVLLF LGVALLVATV GLAHRLYNIH NHHSLRRPHR 1300
    GPQFGSEVEL RHS 1313
    Length:1,313
    Mass (Da):150,908
    Last modified:February 1, 1996 - v1
    Checksum:i8CB5D0015F129591
    GO
    Isoform Testis-specific (identifier: P47820-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: ACE-T

    The sequence of this isoform differs from the canonical sequence as follows:
         1-581: Missing.
         582-646: GCSRPWQEVL...PLPDNYPEGI → MGQGWATPGL...ACLFSSSPPT

    Show »
    Length:775
    Mass (Da):88,170
    Checksum:i5967406D21CAD52A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti341 – 3411L → F in AAG35596. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti207 – 2071R → K.2 Publications

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 581581Missing in isoform Testis-specific. 1 PublicationVSP_037642Add
    BLAST
    Alternative sequencei582 – 64665GCSRP…YPEGI → MGQGWATPGLPRFLFLLLCC GHLLPVLSQVAADHVTANQG ITNQATTRSQTTHQSTISQT IQTSNGTPGRGQGHEGARSQ GPAGGNSNKTTPCGKEGEAC LFSSSPPT in isoform Testis-specific. 1 PublicationVSP_037643Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03708 mRNA. Translation: AAA82110.1.
    U03734 mRNA. Translation: AAA82111.1.
    AF201331 mRNA. Translation: AAG35596.1.
    AF201332 mRNA. Translation: AAG35597.1.
    AF539425 mRNA. Translation: AAN17280.1.
    BC085760 mRNA. Translation: AAH85760.1.
    AF532783 mRNA. Translation: AAP80808.1.
    AF532784 mRNA. Translation: AAP80809.1.
    PIRiJC2038.
    RefSeqiNP_036676.1. NM_012544.1.
    UniGeneiRn.10149.

    Genome annotation databases

    GeneIDi24310.
    KEGGirno:24310.
    UCSCiRGD:2493. rat. [P47820-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U03708 mRNA. Translation: AAA82110.1 .
    U03734 mRNA. Translation: AAA82111.1 .
    AF201331 mRNA. Translation: AAG35596.1 .
    AF201332 mRNA. Translation: AAG35597.1 .
    AF539425 mRNA. Translation: AAN17280.1 .
    BC085760 mRNA. Translation: AAH85760.1 .
    AF532783 mRNA. Translation: AAP80808.1 .
    AF532784 mRNA. Translation: AAP80809.1 .
    PIRi JC2038.
    RefSeqi NP_036676.1. NM_012544.1.
    UniGenei Rn.10149.

    3D structure databases

    ProteinModelPortali P47820.
    SMRi P47820. Positions 36-647, 651-1234.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    MINTi MINT-204637.

    Chemistry

    BindingDBi P47820.
    ChEMBLi CHEMBL2625.
    GuidetoPHARMACOLOGYi 1613.

    Protein family/group databases

    MEROPSi M02.001.

    PTM databases

    PhosphoSitei P47820.

    Proteomic databases

    PRIDEi P47820.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 24310.
    KEGGi rno:24310.
    UCSCi RGD:2493. rat. [P47820-1 ]

    Organism-specific databases

    CTDi 1636.
    RGDi 2493. Ace.

    Phylogenomic databases

    eggNOGi NOG71044.
    HOGENOMi HOG000007838.
    HOVERGENi HBG000264.
    InParanoidi P47820.
    KOi K01283.
    PhylomeDBi P47820.
    TreeFami TF312861.

    Enzyme and pathway databases

    Reactomei REACT_198807. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    NextBioi 602945.
    PROi P47820.

    Gene expression databases

    Genevestigatori P47820.

    Family and domain databases

    InterProi IPR001548. Peptidase_M2.
    [Graphical view ]
    PANTHERi PTHR10514. PTHR10514. 1 hit.
    Pfami PF01401. Peptidase_M2. 2 hits.
    [Graphical view ]
    PRINTSi PR00791. PEPDIPTASEA.
    PROSITEi PS00142. ZINC_PROTEASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Angiotensin converting enzyme and genetic hypertension: cloning of rat cDNAs and characterization of the enzyme."
      Koike G., Krieger J.E., Jacob H.J., Mukoyama M., Pratt R.E., Dzau V.J.
      Biochem. Biophys. Res. Commun. 198:380-386(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC), VARIANT LYS-207.
      Tissue: Lung.
    2. "Characterization of a missense mutation in the angiotensin I-converting enzyme cDNA in exudative inflammation resistant F344/N rats."
      Jafarian-Tehrani M., Listwak S., Barrientos R.M., Michaud A., Corvol P., Sternberg E.M.
      Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
      Strain: Fischer 344/N and Lewis/N.
      Tissue: Lung.
    3. "Species-specific splicing and expression of angiotensin converting enzyme."
      Tian X.-L., Paul M.
      Biochem. Pharmacol. 66:1037-1044(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), TISSUE SPECIFICITY.
      Strain: Sprague-Dawley.
      Tissue: Testis.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
      Tissue: Lung.
    5. "Analysis of the angiotensin converting enzyme (Ace) cDNA sequence and mRNA level of expression in WAG and ISIAH rats."
      Tsetsarkin K.A., Dymshits G.M., Markel A.L., Redina O.E.
      Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-1313 (ISOFORM SOMATIC), VARIANT LYS-207.
      Tissue: Kidney.
    6. Cited for: INDUCTION.

    Entry informationi

    Entry nameiACE_RAT
    AccessioniPrimary (citable) accession number: P47820
    Secondary accession number(s): Q7TMC6, Q8CFN1, Q9EQM9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3