GenomeNet

Database: RefSeq
Entry: NP_997507
LinkDB: NP_997507
Original site: NP_997507 
LOCUS       NP_997507               1312 aa            linear   ROD 23-DEC-2018
DEFINITION  angiotensin-converting enzyme isoform 1 precursor [Mus musculus].
ACCESSION   NP_997507
VERSION     NP_997507.1
DBSOURCE    REFSEQ: accession NM_207624.5
KEYWORDS    RefSeq.
SOURCE      Mus musculus (house mouse)
  ORGANISM  Mus musculus
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
            Muroidea; Muridae; Murinae; Mus; Mus.
REFERENCE   1  (residues 1 to 1312)
  AUTHORS   Moraes OA, Flues K, Scapini KB, Mostarda C, Evangelista FS,
            Rodrigues B, Dartora DR, Fiorino P, Angelis K and Irigoyen MC.
  TITLE     ACE gene dosage determines additional autonomic dysfunction and
            increases renal angiotensin II levels in diabetic mice
  JOURNAL   Clinics (Sao Paulo) 73, e246 (2018)
   PUBMED   30088535
  REMARK    GeneRIF: a small increase in angiotensin-converting enzyme activity
            in diabetic animals leads to greater impairment of autonomic
            function, as demonstrated by increased sympathetic modulation and
            reduced cardiac vagal modulation along with increased renal
            expression of Ang II.
            Publication Status: Online-Only
REFERENCE   2  (residues 1 to 1312)
  AUTHORS   Srivillibhuthur M, Warder BN, Toke NH, Shah PP, Feng Q, Gao N,
            Bonder EM and Verzi MP.
  TITLE     TFAM is required for maturation of the fetal and adult intestinal
            epithelium
  JOURNAL   Dev. Biol. 439 (2), 92-101 (2018)
   PUBMED   29684311
REFERENCE   3  (residues 1 to 1312)
  AUTHORS   Kohlstedt K, Trouvain C, Fromel T, Mudersbach T, Henschler R and
            Fleming I.
  TITLE     Role of the angiotensin-converting enzyme in the G-CSF-induced
            mobilization of progenitor cells
  JOURNAL   Basic Res. Cardiol. 113 (3), 18 (2018)
   PUBMED   29549541
  REMARK    GeneRIF: ACE expression/phosphorylation in the bone-marrow niche
            interface negatively regulates G-CSF-induced signaling and
            hematopoietic progenitor cell mobilization.
            Publication Status: Online-Only
REFERENCE   4  (residues 1 to 1312)
  AUTHORS   Moran CS, Biros E, Krishna SM, Wang Y, Tikellis C, Morton SK, Moxon
            JV, Cooper ME, Norman PE, Burrell LM, Thomas MC and Golledge J.
  TITLE     Resveratrol Inhibits Growth of Experimental Abdominal Aortic
            Aneurysm Associated With Upregulation of Angiotensin-Converting
            Enzyme 2
  JOURNAL   Arterioscler. Thromb. Vasc. Biol. 37 (11), 2195-2203 (2017)
   PUBMED   28935757
  REMARK    GeneRIF: Resveratrol upregulated ACE2 and inhibited abdominal
            aortic aneurysm growth in a mouse model.
REFERENCE   5  (residues 1 to 1312)
  AUTHORS   Song R, Lopez MLSS and Yosypiv IV.
  TITLE     Foxd1 is an upstream regulator of the renin-angiotensin system
            during metanephric kidney development
  JOURNAL   Pediatr. Res. 82 (5), 855-862 (2017)
   PUBMED   28665931
REFERENCE   6  (residues 1 to 1312)
  AUTHORS   Cambien F, Poirier O, Lecerf L, Evans A, Cambou JP, Arveiler D, Luc
            G, Bard JM, Bara L, Ricard S et al.
  TITLE     Deletion polymorphism in the gene for angiotensin-converting enzyme
            is a potent risk factor for myocardial infarction
  JOURNAL   Nature 359 (6396), 641-644 (1992)
   PUBMED   1328889
REFERENCE   7  (residues 1 to 1312)
  AUTHORS   Langford KG, Shai SY, Howard TE, Kovac MJ, Overbeek PA and
            Bernstein KE.
  TITLE     Transgenic mice demonstrate a testis-specific promoter for
            angiotensin-converting enzyme
  JOURNAL   J. Biol. Chem. 266 (24), 15559-15562 (1991)
   PUBMED   1651914
REFERENCE   8  (residues 1 to 1312)
  AUTHORS   Howard TE, Shai SY, Langford KG, Martin BM and Bernstein KE.
  TITLE     Transcription of testicular angiotensin-converting enzyme (ACE) is
            initiated within the 12th intron of the somatic ACE gene
  JOURNAL   Mol. Cell. Biol. 10 (8), 4294-4302 (1990)
   PUBMED   2164636
REFERENCE   9  (residues 1 to 1312)
  AUTHORS   Shai SY, Langford KG, Martin BM and Bernstein KE.
  TITLE     Genomic DNA 5' to the mouse and human angiotensin-converting enzyme
            genes contains two distinct regions of conserved sequence
  JOURNAL   Biochem. Biophys. Res. Commun. 167 (3), 1128-1133 (1990)
   PUBMED   2157425
REFERENCE   10 (residues 1 to 1312)
  AUTHORS   Bernstein KE, Martin BM, Edwards AS and Bernstein EA.
  TITLE     Mouse angiotensin-converting enzyme is a protein composed of two
            homologous domains
  JOURNAL   J. Biol. Chem. 264 (20), 11945-11951 (1989)
   PUBMED   2545691
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            BY210311.1, AK161020.1 and AL731865.9.
            
            Transcript Variant: This variant (1) encodes the longest isoform
            (1).
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            Transcript exon combination :: AK154632.1, AK161020.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMN00849374, SAMN00849375
                                           [ECO:0000348]
            ##Evidence-Data-END##
FEATURES             Location/Qualifiers
     source          1..1312
                     /organism="Mus musculus"
                     /strain="C57BL/6"
                     /db_xref="taxon:10090"
                     /chromosome="11"
                     /map="11 68.84 cM"
     Protein         1..1312
                     /product="angiotensin-converting enzyme isoform 1
                     precursor"
                     /EC_number="3.4.15.1"
                     /note="dipeptidyl peptidase; kininase II; dipeptidyl
                     carboxypeptidase I; angiotensin-converting enzyme"
                     /calculated_mol_wt=147398
     sig_peptide     1..34
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=3539
     mat_peptide     35..1312
                     /product="Angiotensin-converting enzyme"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
                     /calculated_mol_wt=147398
     mat_peptide     35..1237
                     /product="Angiotensin-converting enzyme, soluble form"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
                     /calculated_mol_wt=138974
     Region          35..635
                     /region_name="Peptidase M2 1"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
     Region          45..628
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:279709"
     Site            order(365..367,395..396,399,423,469,523..525,530,532,535)
                     /site_type="active"
                     /db_xref="CDD:188999"
     Site            order(395,399,423)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188999"
     Region          636..1237
                     /region_name="Peptidase M2 2"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
     Region          649..1226
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:279709"
     Site            order(963..965,993..994,997,1021,1067,1121..1123,1128,
                     1130,1133)
                     /site_type="active"
                     /db_xref="CDD:188999"
     Site            order(993,997,1021)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188999"
     Site            1265..1281
                     /site_type="transmembrane region"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
     Site            1305
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|PubMed:21183079};
                     propagated from UniProtKB/Swiss-Prot (P09470.3)"
     CDS             1..1312
                     /gene="Ace"
                     /gene_synonym="AW208573; CD143"
                     /coded_by="NM_207624.5:38..3976"
                     /note="isoform 1 precursor is encoded by transcript
                     variant 1"
                     /db_xref="CCDS:CCDS25543.1"
                     /db_xref="GeneID:11421"
                     /db_xref="MGI:MGI:87874"
ORIGIN      
        1 mgaasgqrgr wplsppllml sllvlllqps papaldpglq pgnfspdeag aqlfaesyns
       61 saevvmfqst vaswahdtni teenarrqee aalvsqefae vwgkkakely esiwqnftds
      121 klrriigsir tlgpanlpla qrqqynslls nmsriystgk vcfpnktatc wsldpeltni
      181 lassrsyakl lfawegwhda vgiplkplyq dftaisneay rqddfsdtga fwrswyesps
      241 feeslehiyh qleplylnlh ayvrralhrr ygdkyvnlrg pipahllgdm waqsweniyd
      301 mvvpfpdkpn ldvtstmvqk gwnathmfrv seefftslgl spmppefwae smlekptdgr
      361 evvchasawd fynrkdfrik qctrvtmeql atvhhemghv qyylqykdlh vslrrganpg
      421 fheaigdvla lsvstpahlh kiglldhvtn diesdinyll kmalekiafl pfgylvdqwr
      481 wgvfsgrtpp srynfdwwyl rtkyqgicpp varnethfda gakfhipnvt pyiryfvsfv
      541 lqfqfhqalc keaghqgplh qcdiyqsaqa gaklkqvlqa gcsrpwqevl kdlvgsdald
      601 akalleyfqp vsqwleeqnq rngevlgwpe nqwrpplpdn ypegidletd eakadrfvee
      661 ydrtaqvlln eyaeanwqyn tnitiegski llekstevsn htlkygtrak tfdvsnfqns
      721 sikriikklq nldravlppk eleeynqill dmettyslsn icytngtcmp lepdltnmma
      781 tsrkyeellw awkswrdkvg railpffpky vefsnkiakl ngytdagdsw rslyesdnle
      841 qdleklyqel qplylnlhay vrrslhrhyg seyinldgpi pahllgnmwa qtwsniydlv
      901 apfpsapnid ateamikqgw tprrifkead nfftslgllp vppefwnksm lekptdgrev
      961 vchpsawdfy ngkdfrikqc tsvnmedlvi ahhemghiqy fmqykdlpvt freganpgfh
     1021 eaigdimals vstpkhlysl nllstegsgy eydinflmkm aldkiafipf sylidqwrwr
     1081 vfdgsitken ynqewwslrl kyqglcppvp rsqgdfdpgs kfhvpanvpy vryfvsfiiq
     1141 fqfhealcra aghtgplhkc diyqskeagk lladamklgy skpwpeamkl itgqpnmsas
     1201 ammnyfkplt ewlvtenrrh getlgwpeyn wapntaraeg staesnrvnf lglylepqqa
     1261 rvgqwvllfl gvallvatvg lahrlynirn hhslrrphrg pqfgsevelr hs
//
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