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P09470

- ACE_MOUSE

UniProt

P09470 - ACE_MOUSE

Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 3 (30 Aug 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.3 Publications

    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

    Enzyme regulationi

    Peptidase activity is specifically inhibited by lisinopril, captopril and enalaprilat. In contrast, GPIase activity is nearly insensitive to captopril.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei236 – 2361Chloride 1By similarity
    Metal bindingi395 – 3951Zinc 1; catalyticBy similarity
    Active sitei396 – 39611PROSITE-ProRule annotation
    Metal bindingi399 – 3991Zinc 1; catalyticBy similarity
    Metal bindingi423 – 4231Zinc 1; catalyticBy similarity
    Binding sitei534 – 5341Chloride 1By similarity
    Binding sitei796 – 7961Chloride 2By similarity
    Binding sitei834 – 8341Chloride 3By similarity
    Metal bindingi993 – 9931Zinc 2; catalytic
    Active sitei994 – 99412
    Metal bindingi997 – 9971Zinc 2; catalytic
    Metal bindingi1021 – 10211Zinc 2; catalyticBy similarity
    Binding sitei1095 – 10951Chloride 2By similarity
    Binding sitei1099 – 10991Chloride 2By similarity
    Binding sitei1132 – 11321Chloride 3By similarity

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB
    4. peptidase activity Source: MGI
    5. peptidyl-dipeptidase activity Source: UniProtKB
    6. protein binding Source: MGI

    GO - Biological processi

    1. heart contraction Source: MGI
    2. hormone catabolic process Source: BHF-UCL
    3. kidney development Source: MGI
    4. neutrophil mediated immunity Source: MGI
    5. positive regulation of systemic arterial blood pressure Source: MGI
    6. regulation of blood pressure Source: BHF-UCL
    7. spermatogenesis Source: MGI

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_196539. 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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:87874. Ace.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Cytoplasm 1 Publication
    Note: Detected in both cell membrane and cytoplasm in neurons.

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Low blood pressure, elevated serum potassium, anemia, and renal defects. Male mice have reduced fertility.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi993 – 9931H → K: Abolishes peptidase activity but no effect on GPIase activity; when associated to K-997. 1 Publication
    Mutagenesisi994 – 9941E → D: Abolishes peptidase activity but no effect on GPIase activity. 1 Publication
    Mutagenesisi997 – 9971H → K: Abolishes peptidase activity but no effect on GPIase activity; when associated to K-993. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 34341 PublicationAdd
    BLAST
    Chaini35 – 13121278Angiotensin-converting enzymePRO_0000028539Add
    BLAST
    Chaini35 – 12371203Angiotensin-converting enzyme, soluble formPRO_0000028540Add
    BLAST
    Propeptidei1238 – 131275Removed in secreted formBy similarityPRO_0000028541Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi116 – 1161N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi151 – 1511N-linked (GlcNAc...)1 Publication
    Disulfide bondi162 ↔ 170By similarity
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi323 – 3231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi514 – 5141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi682 – 6821N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi700 – 7001N-linked (GlcNAc...) (complex)By similarity
    Glycosylationi719 – 7191N-linked (GlcNAc...) (complex)By similarity
    Disulfide bondi762 ↔ 768By similarity
    Glycosylationi765 – 7651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi947 – 9471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi962 ↔ 980By similarity
    Disulfide bondi1148 ↔ 1160By similarity
    Glycosylationi1196 – 11961N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1305 – 13051PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated by CK2 on Ser-1305; which allows membrane retention.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP09470.
    PaxDbiP09470.
    PRIDEiP09470.

    PTM databases

    PhosphoSiteiP09470.

    Expressioni

    Tissue specificityi

    Testis-specific isoform is expressed in spermatocytes, adult testis.

    Inductioni

    Expression is thought to be subject to hormonal regulation by androgens.

    Gene expression databases

    ArrayExpressiP09470.
    BgeeiP09470.
    GenevestigatoriP09470.

    Interactioni

    Protein-protein interaction databases

    BioGridi197920. 1 interaction.
    IntActiP09470. 3 interactions.
    MINTiMINT-4086662.

    Structurei

    3D structure databases

    ProteinModelPortaliP09470.
    SMRiP09470. Positions 35-646, 650-1235.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini35 – 12641230ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1282 – 131231CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1265 – 128117HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 635601Peptidase M2 1Add
    BLAST
    Regioni636 – 1237602Peptidase M2 2Add
    BLAST

    Sequence similaritiesi

    Belongs to the peptidase M2 family.Curated

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG71044.
    GeneTreeiENSGT00520000055576.
    HOGENOMiHOG000007838.
    HOVERGENiHBG000264.
    InParanoidiP09470.
    KOiK01283.
    OMAiMEQLFTV.
    OrthoDBiEOG76HQ13.
    PhylomeDBiP09470.
    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: P09470-1) [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 SLLVLLLQPS PAPALDPGLQ PGNFSPDEAG     50
    AQLFAESYNS SAEVVMFQST VASWAHDTNI TEENARRQEE AALVSQEFAE 100
    VWGKKAKELY ESIWQNFTDS KLRRIIGSIR TLGPANLPLA QRQQYNSLLS 150
    NMSRIYSTGK VCFPNKTATC WSLDPELTNI LASSRSYAKL LFAWEGWHDA 200
    VGIPLKPLYQ DFTAISNEAY RQDDFSDTGA FWRSWYESPS FEESLEHIYH 250
    QLEPLYLNLH AYVRRALHRR YGDKYVNLRG PIPAHLLGDM WAQSWENIYD 300
    MVVPFPDKPN LDVTSTMVQK GWNATHMFRV SEEFFTSLGL SPMPPEFWAE 350
    SMLEKPTDGR EVVCHASAWD FYNRKDFRIK QCTRVTMEQL ATVHHEMGHV 400
    QYYLQYKDLH VSLRRGANPG FHEAIGDVLA LSVSTPAHLH KIGLLDHVTN 450
    DIESDINYLL KMALEKIAFL PFGYLVDQWR WGVFSGRTPP SRYNFDWWYL 500
    RTKYQGICPP VARNETHFDA GAKFHIPNVT PYIRYFVSFV LQFQFHQALC 550
    KEAGHQGPLH QCDIYQSAQA GAKLKQVLQA GCSRPWQEVL KDLVGSDALD 600
    AKALLEYFQP VSQWLEEQNQ RNGEVLGWPE NQWRPPLPDN YPEGIDLETD 650
    EAKADRFVEE YDRTAQVLLN EYAEANWQYN TNITIEGSKI LLEKSTEVSN 700
    HTLKYGTRAK TFDVSNFQNS SIKRIIKKLQ NLDRAVLPPK ELEEYNQILL 750
    DMETTYSLSN ICYTNGTCMP LEPDLTNMMA TSRKYEELLW AWKSWRDKVG 800
    RAILPFFPKY VEFSNKIAKL NGYTDAGDSW RSLYESDNLE QDLEKLYQEL 850
    QPLYLNLHAY VRRSLHRHYG SEYINLDGPI PAHLLGNMWA QTWSNIYDLV 900
    APFPSAPNID ATEAMIKQGW TPRRIFKEAD NFFTSLGLLP VPPEFWNKSM 950
    LEKPTDGREV VCHPSAWDFY NGKDFRIKQC TSVNMEDLVI AHHEMGHIQY 1000
    FMQYKDLPVT FREGANPGFH EAIGDIMALS VSTPKHLYSL NLLSTEGSGY 1050
    EYDINFLMKM ALDKIAFIPF SYLIDQWRWR VFDGSITKEN YNQEWWSLRL 1100
    KYQGLCPPVP RSQGDFDPGS KFHVPANVPY VRYFVSFIIQ FQFHEALCRA 1150
    AGHTGPLHKC DIYQSKEAGK LLADAMKLGY SKPWPEAMKL ITGQPNMSAS 1200
    AMMNYFKPLT EWLVTENRRH GETLGWPEYN WAPNTARAEG STAESNRVNF 1250
    LGLYLEPQQA RVGQWVLLFL GVALLVATVG LAHRLYNIRN HHSLRRPHRG 1300
    PQFGSEVELR HS 1312
    Length:1,312
    Mass (Da):150,918
    Last modified:August 30, 2005 - v3
    Checksum:i7DF9F5BE91762DFF
    GO
    Isoform Testis-specific (identifier: P09470-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: ACE-T

    The sequence of this isoform differs from the canonical sequence as follows:
         1-580: Missing.
         581-646: GCSRPWQEVL...LPDNYPEGID → MGQGWATPGL...TIDQTTQIPN

    Show »
    Length:732
    Mass (Da):84,047
    Checksum:i16C817E7FBD09BD9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti568 – 5681A → T in AAA37147. (PubMed:2545691)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 580580Missing in isoform Testis-specific. 1 PublicationVSP_037638Add
    BLAST
    Alternative sequencei581 – 64666GCSRP…PEGID → MGQGWATPGLPSFLFLLLCC GHHLLVLSQVATDHVTANQG ITNQATTRSQTTTHQATIDQ TTQIPN in isoform Testis-specific. 1 PublicationVSP_037639Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04946 mRNA. Translation: AAA37147.1.
    J04947 mRNA. Translation: AAA37148.1.
    M55333 mRNA. Translation: AAA37149.1.
    M61094 Genomic DNA. Translation: AAA37150.1.
    BC040404 mRNA. Translation: AAH40404.1.
    J03940 mRNA. Translation: AAA37146.1.
    CCDSiCCDS25543.1. [P09470-1]
    CCDS25544.1. [P09470-2]
    PIRiA34171.
    A35655.
    RefSeqiNP_033728.1. NM_009598.2. [P09470-2]
    NP_997507.1. NM_207624.5. [P09470-1]
    UniGeneiMm.754.

    Genome annotation databases

    EnsembliENSMUST00000001963; ENSMUSP00000001963; ENSMUSG00000020681. [P09470-1]
    ENSMUST00000001964; ENSMUSP00000001964; ENSMUSG00000020681. [P09470-2]
    GeneIDi11421.
    KEGGimmu:11421.
    UCSCiuc007lxu.2. mouse. [P09470-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J04946 mRNA. Translation: AAA37147.1 .
    J04947 mRNA. Translation: AAA37148.1 .
    M55333 mRNA. Translation: AAA37149.1 .
    M61094 Genomic DNA. Translation: AAA37150.1 .
    BC040404 mRNA. Translation: AAH40404.1 .
    J03940 mRNA. Translation: AAA37146.1 .
    CCDSi CCDS25543.1. [P09470-1 ]
    CCDS25544.1. [P09470-2 ]
    PIRi A34171.
    A35655.
    RefSeqi NP_033728.1. NM_009598.2. [P09470-2 ]
    NP_997507.1. NM_207624.5. [P09470-1 ]
    UniGenei Mm.754.

    3D structure databases

    ProteinModelPortali P09470.
    SMRi P09470. Positions 35-646, 650-1235.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197920. 1 interaction.
    IntActi P09470. 3 interactions.
    MINTi MINT-4086662.

    Chemistry

    BindingDBi P09470.
    ChEMBLi CHEMBL2994.

    Protein family/group databases

    MEROPSi M02.001.

    PTM databases

    PhosphoSitei P09470.

    Proteomic databases

    MaxQBi P09470.
    PaxDbi P09470.
    PRIDEi P09470.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000001963 ; ENSMUSP00000001963 ; ENSMUSG00000020681 . [P09470-1 ]
    ENSMUST00000001964 ; ENSMUSP00000001964 ; ENSMUSG00000020681 . [P09470-2 ]
    GeneIDi 11421.
    KEGGi mmu:11421.
    UCSCi uc007lxu.2. mouse. [P09470-1 ]

    Organism-specific databases

    CTDi 1636.
    MGIi MGI:87874. Ace.

    Phylogenomic databases

    eggNOGi NOG71044.
    GeneTreei ENSGT00520000055576.
    HOGENOMi HOG000007838.
    HOVERGENi HBG000264.
    InParanoidi P09470.
    KOi K01283.
    OMAi MEQLFTV.
    OrthoDBi EOG76HQ13.
    PhylomeDBi P09470.
    TreeFami TF312861.

    Enzyme and pathway databases

    Reactomei REACT_196539. Metabolism of Angiotensinogen to Angiotensins.

    Miscellaneous databases

    ChiTaRSi ACE. mouse.
    NextBioi 278668.
    PROi P09470.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09470.
    Bgeei P09470.
    Genevestigatori P09470.

    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. "Mouse angiotensin-converting enzyme is a protein composed of two homologous domains."
      Bernstein K.E., Martin B.M., Edwards A.S., Bernstein E.A.
      J. Biol. Chem. 264:11945-11951(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
    2. "Transcription of testicular angiotensin-converting enzyme (ACE) is initiated within the 12th intron of the somatic ACE gene."
      Howard T.E., Shai S.-Y., Langford K.G., Martin B.M., Bernstein K.E.
      Mol. Cell. Biol. 10:4294-4302(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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).
      Strain: FVB/N.
      Tissue: Mammary gland.
    4. "The isolation of angiotensin-converting enzyme cDNA."
      Bernstein K.E., Martin B.M., Bernstein E.A., Linton J., Striker L., Striker G.
      J. Biol. Chem. 263:11021-11024(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-332 (ISOFORM SOMATIC), PARTIAL PROTEIN SEQUENCE.
    5. "Partial protein sequence of mouse and bovine kidney angiotensin converting enzyme."
      Bernstein K.E., Martin B.M., Striker L., Striker G.
      Kidney Int. 33:652-655(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 35-54.
      Tissue: Kidney.
    6. "Male-female differences in fertility and blood pressure in ACE-deficient mice."
      Krege J.H., John S.W., Langenbach L.L., Hodgin J.B., Hagaman J.R., Bachman E.S., Jennette J.C., O'Brien D.A., Smithies O.
      Nature 375:146-148(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Mice lacking angiotensin-converting enzyme have low blood pressure, renal pathology, and reduced male fertility."
      Esther C.R. Jr., Howard T.E., Marino E.M., Goddard J.M., Capecchi M.R., Bernstein K.E.
      Lab. Invest. 74:953-965(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    8. "Angiotensin-converting enzyme is a GPI-anchored protein releasing factor crucial for fertilization."
      Kondoh G., Tojo H., Nakatani Y., Komazawa N., Murata C., Yamagata K., Maeda Y., Kinoshita T., Okabe M., Taguchi R., Takeda J.
      Nat. Med. 11:160-166(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, MUTAGENESIS OF HIS-993; GLU-994 AND HIS-997.
    9. "Proteome-wide characterization of N-glycosylation events by diagonal chromatography."
      Ghesquiere B., Van Damme J., Martens L., Vandekerckhove J., Gevaert K.
      J. Proteome Res. 5:2438-2447(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-151.
      Strain: C57BL/6.
      Tissue: Plasma.
    10. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    11. "Angiotensin II regulates ACE and ACE2 in neurons through p38 mitogen-activated protein kinase and extracellular signal-regulated kinase 1/2 signaling."
      Xiao L., Haack K.K., Zucker I.H.
      Am. J. Physiol. 304:C1073-C1079(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiACE_MOUSE
    AccessioniPrimary (citable) accession number: P09470
    Secondary accession number(s): P22967, Q6GTS2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: August 30, 2005
    Last modified: October 1, 2014
    This is version 145 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    3. Peptidase families
      Classification of peptidase families and list of entries
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3