LOCUS NP_997507 1312 aa linear ROD 28-NOV-2023
DEFINITION angiotensin-converting enzyme isoform 1 precursor [Mus musculus].
ACCESSION NP_997507
VERSION NP_997507.1
DBSOURCE REFSEQ: accession NM_207624.6
KEYWORDS RefSeq; RefSeq Select.
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 Cao D, Saito S, Xu L, Fan W, Li X, Ahmed F, Jovanovic P, Shibata T,
Che M, Bernstein EA, Gianni J, Divakaruni AS, Okwan-Duodu D, Khan
Z, Riera CE, Chen F and Bernstein KE.
TITLE Myeloid cell ACE shapes cellular metabolism and function in PCSK-9
induced atherosclerosis
JOURNAL Front Immunol 14, 1278383 (2023)
PUBMED 37928535
REMARK Publication Status: Online-Only
REFERENCE 2 (residues 1 to 1312)
AUTHORS Juretzko A, Steinbach A, Witte J, Hannemann A, Miehe B, Siegerist
F, Wolke C, Stracke S and Rettig R.
TITLE Renal angiotensin I-converting enzyme-deficient mice are protected
against aristolochic acid nephropathy
JOURNAL Pflugers Arch 475 (3), 391-403 (2023)
PUBMED 36520238
REMARK GeneRIF: Renal angiotensin I-converting enzyme-deficient mice are
protected against aristolochic acid nephropathy.
REFERENCE 3 (residues 1 to 1312)
AUTHORS Gao Y, Sun Y, Islam S, Nakamura T, Tomita T, Zou K and Michikawa M.
TITLE Presenilin 1 deficiency impairs Abeta42-to-Abeta40- and
angiotensin-converting activities of ACE
JOURNAL Front Aging Neurosci 15, 1098034 (2023)
PUBMED 36875692
REMARK Publication Status: Online-Only
REFERENCE 4 (residues 1 to 1312)
AUTHORS Ahuja N, Hiltabidle MS, Rajasekhar H, Voss S, Lu SZ, Barlow HR,
Cowdin MA, Daniel E, Vaddaraju V, Anandakumar T, Black E, Cleaver O
and Maynard C.
TITLE Endothelial Cyp26b1 restrains murine heart valve growth during
development
JOURNAL Dev Biol 486, 81-95 (2022)
PUBMED 35364055
REFERENCE 5 (residues 1 to 1312)
AUTHORS Trieu BH, Remmers BC, Toddes C, Brandner DD, Lefevre EM, Kocharian
A, Retzlaff CL, Dick RM, Mashal MA, Gauthier EA, Xie W, Zhang Y,
More SS and Rothwell PE.
TITLE Angiotensin-converting enzyme gates brain circuit-specific
plasticity via an endogenous opioid
JOURNAL Science 375 (6585), 1177-1182 (2022)
PUBMED 35201898
REMARK GeneRIF: Angiotensin-converting enzyme gates brain circuit-specific
plasticity via an endogenous opioid.
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
AL596246.10 and AL731865.9.
Sequence Note: The RefSeq transcript and protein were derived from
genomic sequence to make the sequence consistent with the reference
genome assembly. The genomic coordinates used for the transcript
record were based on alignments.
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 :: AK161020.1, AK154632.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMN00849374, SAMN00849375
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on conservation, expression,
longest protein
##RefSeq-Attributes-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;
angiotensin I converting enzyme (peptidyl-dipeptidase A)
1"
/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.
/id=PRO_0000028539"
/note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
/calculated_mol_wt=147398
mat_peptide 35..1237
/product="Angiotensin-converting enzyme, soluble form.
/evidence=ECO:0000250|UniProtKB:P12821.
/id=PRO_0000028540"
/note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
/calculated_mol_wt=138974
Region 45..628
/region_name="Peptidase_M2"
/note="Angiotensin-converting enzyme; pfam01401"
/db_xref="CDD:426243"
Site 59
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 79
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 116
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 151
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000269|PubMed:16944957; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 165
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 323
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site order(365..368,389,395..396,399,403,422..423,427,469,
523..525,530,532,535)
/site_type="active"
/db_xref="CDD:341055"
Site order(395,399,423)
/site_type="other"
/note="Zn binding site [ion binding]"
/db_xref="CDD:341055"
Site 514
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Region 649..1226
/region_name="Peptidase_M2"
/note="Angiotensin-converting enzyme; pfam01401"
/db_xref="CDD:426243"
Site 682
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 700
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (complex) asparagine.
/evidence=ECO:0000250|UniProtKB:P12821; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 719
/site_type="glycosylation"
/note="N-linked (GlcNAc...) (complex) asparagine.
/evidence=ECO:0000250|UniProtKB:P12821; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 765
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site 947
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Site order(963..966,987,993..994,997,1001,1020..1021,1025,1067,
1121..1123,1128,1130,1133)
/site_type="active"
/db_xref="CDD:341055"
Site order(993,997,1021)
/site_type="other"
/note="Zn binding site [ion binding]"
/db_xref="CDD:341055"
Site 1196
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
Region 1220..1261
/region_name="Juxtamembrane stalk.
/evidence=ECO:0000250|UniProtKB:P12821"
/note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
Site 1265..1281
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (P09470.3)"
Site 1305
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:21183079; propagated from
UniProtKB/Swiss-Prot (P09470.3)"
CDS 1..1312
/gene="Ace"
/gene_synonym="CD143"
/coded_by="NM_207624.6:35..3973"
/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
//
