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Q50JE5

- ACE_MESAU

UniProt

Q50JE5 - ACE_MESAU

Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Mesocricetus auratus (Golden hamster)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (07 Jun 2005)
      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.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. 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

    Enzyme and pathway databases

    BRENDAi3.4.15.1. 3239.

    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
    OrganismiMesocricetus auratus (Golden hamster)
    Taxonomic identifieri10036 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

    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. extracellular region Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535By similarityAdd
    BLAST
    Chaini36 – 13141279Angiotensin-converting enzymePRO_0000028536Add
    BLAST
    Chaini36 – 12381203Angiotensin-converting enzyme, soluble formPRO_0000028537Add
    BLAST
    Propeptidei1239 – 131476Removed in secreted formBy similarityPRO_0000028538Add
    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
    Disulfide bondi163 ↔ 171By similarity
    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
    Disulfide bondi763 ↔ 769By similarity
    Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi963 ↔ 981By similarity
    Disulfide bondi1149 ↔ 1161By similarity
    Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1307 – 13071PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CK2 on Ser-1307; which allows membrane retention.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Expressioni

    Tissue specificityi

    Widely expressed with dominant expression in lung and kidney.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ50JE5.
    SMRiQ50JE5. Positions 36-647, 651-1234.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini36 – 12651230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1283 – 131432CytoplasmicSequence 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

    HOVERGENiHBG000264.

    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: Q50JE5-1) [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

    MGAASGQRGQ GPPSPLLLLW LSLLLLLLPP SPAPALDPGL QPGNFSADEI     50
    GAHLFAESYN SSAEQVIFQS TVASWAYDTN MTEENARLQE EAELIWQEFA 100
    EVWGKKAKEL FDAIRQNFTD SKLRRVIETI RTLGPANLPL ARRQQYNSLQ 150
    NNMNRIYSTS KVCLPNKTAT CWSLEPELTN ILASSRSYAK LLFAWESWHD 200
    VVGIPLKPLY QDFTALSNEA YKQDGFSDTG AYWRSAYDSP SFEETLEHLY 250
    HQLEPLYLNL HAYVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWDNIY 300
    DMVVPFPNKP NLDVTNTMVQ KGWNVTHMFR VAEEFFTSMG LSPMPPEFWA 350
    ESMLEKPTDG REVVCHASAW DFFNRKDFRI KQCTRITMEQ LSTVHHEMGH 400
    VQYYLQYKDL TVPLRRGANP GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA 450
    NDLESDINYL LKMALEKIAF LPFGYLVDQW RWGVFSGHTP PSRYNFDWWY 500
    FRTKYQGICP PVVRNETHFD AGAKFHIPSG TPYIRYFVSF ILQFQFHQAL 550
    CKEAGHQGPL HQCDIYQSTQ AGAKLQRVLQ AGYSRPWQEV LKEMVGSDTL 600
    DAQALLEYFQ PVIRWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLVT 650
    DETEAERFVE EYDRTARVLW NEYAEANWQY NTNITLEASK ILLQKNKKVA 700
    NHTLKYGTLA KKFDVSNFQN YTIKRIIKKV QNMDRAVLPP KELEEYNQIL 750
    MDMETTYSIA NVCYLNGTCL HLEPDLTNVM ATSRKYEELL WVWKSWRDKV 800
    GRAILPLFPK YVELSNKIAH LNGYADGGDS WRSSYESKSL EQDLEQLYQE 850
    LQPLYLNLHA YVRRSLHRHY GSQHINLDGP IPAHLLGNMW AQTWSNIYDL 900
    VAPFPSAPNL DATEAMIKQG WTPRRIFKEA DDFFTSLGLL PVSEEFWNKS 950
    MLEKPGDGRE VVCHASAWDF YNGKDFRIKQ CTSVNMEDLV IAHHEMGHIQ 1000
    YFMQYKDLPV TFREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGGG 1050
    YEHDINFLMK MALDKIAFIP FSYLIDQWRW RVFDGSITKE NYNQEWWSLR 1100
    LKYQGLCPPV PRSQDDFDPG SKFHVPANVP YIRYFVSFII QFQFHEALCR 1150
    AAGHTGPLHK CDIYQSKEAG KLLADTMKMG YSKPWPEAMK LITGQPNMSA 1200
    SAMMNYFKPL TEWLVTENRR HGETLGWPEY NWTPNTARSE GPFPESGRVN 1250
    FLGMYLEPQQ ARVGQWVLLF LGVSLLVATL GLTHRLFSIR QHGHSLHRPH 1300
    RGPQFGSEVE LRHS 1314
    Length:1,314
    Mass (Da):151,595
    Last modified:June 7, 2005 - v1
    Checksum:i74E29238E87F157E
    GO
    Isoform Testis-specific (identifier: Q50JE5-2)

    Also known as: ACE-T

    Sequence is not available
    Length:
    Mass (Da):

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB212958 mRNA. Translation: BAD98304.1.
    RefSeqiNP_001268510.1. NM_001281581.1. [Q50JE5-1]

    Genome annotation databases

    GeneIDi101824864.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB212958 mRNA. Translation: BAD98304.1 .
    RefSeqi NP_001268510.1. NM_001281581.1. [Q50JE5-1 ]

    3D structure databases

    ProteinModelPortali Q50JE5.
    SMRi Q50JE5. Positions 36-647, 651-1234.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M02.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 101824864.

    Phylogenomic databases

    HOVERGENi HBG000264.

    Enzyme and pathway databases

    BRENDAi 3.4.15.1. 3239.

    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. "cDNA cloning of hamster angiotensin-converting enzyme and mRNA expression."
      Uchide T., Fujimori Y., Fukushima U., Uechi M., Sasaki T., Temma K.
      DNA Seq. 17:319-325(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiACE_MESAU
    AccessioniPrimary (citable) accession number: Q50JE5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: June 7, 2005
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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