LOCUS NP_036676 1313 aa linear ROD 27-APR-2025
DEFINITION angiotensin-converting enzyme precursor [Rattus norvegicus].
ACCESSION NP_036676
VERSION NP_036676.1
DBSOURCE REFSEQ: accession NM_012544.1
KEYWORDS RefSeq; RefSeq Select.
SOURCE Rattus norvegicus (Norway rat)
ORGANISM Rattus norvegicus
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
REFERENCE 1 (residues 1 to 1313)
AUTHORS Ferreira-Duarte,M., Oliveira,L.C.G., Quintas,C.,
Esteves-Monteiro,M., Duarte-Araujo,M., Sousa,T., Casarini,D.E. and
Morato,M.
TITLE ACE and ACE2 catalytic activity in the fecal content along the gut
JOURNAL Neurogastroenterol Motil 35 (9), e14598 (2023)
PUBMED 37052403
REMARK GeneRIF: ACE and ACE2 catalytic activity in the fecal content along
the gut.
REFERENCE 2 (residues 1 to 1313)
AUTHORS Lin,Y., Li,Y.Q., Wang,H., Wu,H.J., Bai,B.L., Ma,L.J., Zou,J.Z.,
Zhang,Q. and Shi,L.
TITLE Increasing angiotensin-converting enzyme 1 regulated by histone 3
lysine 27 hyperacetylation in high-fat diet-induced hypertensive
rat kidney
JOURNAL J Hypertens 40 (10), 1969-1978 (2022)
PUBMED 35969203
REMARK GeneRIF: Increasing angiotensin-converting enzyme 1 regulated by
histone 3 lysine 27 hyperacetylation in high-fat diet-induced
hypertensive rat kidney.
REFERENCE 3 (residues 1 to 1313)
AUTHORS Saadat,M.
TITLE No significant correlation between ACE Ins/Del genetic polymorphism
and COVID-19 infection
JOURNAL Clin Chem Lab Med 58 (7), 1127-1128 (2020)
PUBMED 32386188
REFERENCE 4 (residues 1 to 1313)
AUTHORS Delanghe,J.R., Speeckaert,M.M. and De Buyzere,M.L.
TITLE COVID-19 infections are also affected by human ACE1 D/I
polymorphism
JOURNAL Clin Chem Lab Med 58 (7), 1125-1126 (2020)
PUBMED 32286246
REFERENCE 5 (residues 1 to 1313)
AUTHORS Shu,Y., Cao,X.Y. and Chen,J.
TITLE Preparation and antagonistic effect of ACE inhibitory peptide from
cashew
JOURNAL J Sci Food Agric 99 (15), 6822-6832 (2019)
PUBMED 31385307
REFERENCE 6 (residues 1 to 1313)
AUTHORS Weinreb,R.N., O'Donnell,J.J., Sandman,R., Char,D.H. and Kimura,S.J.
TITLE Angiotensin-converting enzyme in sarcoid uveitis
JOURNAL Invest Ophthalmol Vis Sci 18 (12), 1285-1287 (1979)
PUBMED 229083
REFERENCE 7 (residues 1 to 1313)
AUTHORS Sedov,V.A.
TITLE [To sanitize liv stock raising of helminthiases]
JOURNAL Veterinariia (12), 10-12 (1978)
PUBMED 734899
REFERENCE 8 (residues 1 to 1313)
AUTHORS Zderkiewicz,E.
TITLE [Autoregulation of cerebral blood flow]
JOURNAL Pol Tyg Lek 33 (29), 1157-1159 (1978)
PUBMED 704419
REFERENCE 9 (residues 1 to 1313)
AUTHORS Sancho,J., Re,R., Burton,J., Barger,A.C. and Haber,E.
TITLE The role of the renin-angiotensin-aldosterone system in
cardiovascular homeostasis in normal human subjects
JOURNAL Circulation 53 (3), 400-405 (1976)
PUBMED 174834
REFERENCE 10 (residues 1 to 1313)
AUTHORS Silverstein,E., Friedland,J., Lyons,H.A. and Gourin,A.
TITLE Elevation of angiotensin-converting enzyme in granulomatous lymph
nodes and serum in sarcoidosis: clinical and possible pathogenic
significance
JOURNAL Ann N Y Acad Sci 278, 498-513 (1976)
PUBMED 183595
COMMENT PROVISIONAL REFSEQ: This record has not yet been subject to final
NCBI review. The reference sequence was derived from U03734.1.
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 :: U03734.1, BC085760.1 [ECO:0000332]
RNAseq introns :: single sample supports all introns
SAMD00132261, SAMD00132262
[ECO:0000348]
##Evidence-Data-END##
##RefSeq-Attributes-START##
RefSeq Select criteria :: based on single protein-coding transcript
##RefSeq-Attributes-END##
FEATURES Location/Qualifiers
source 1..1313
/organism="Rattus norvegicus"
/db_xref="taxon:10116"
/chromosome="10"
/map="10q32.1"
Protein 1..1313
/product="angiotensin-converting enzyme precursor"
/EC_number="3.4.15.1"
/note="kininase II; angiotensin-converting enzyme;
dipeptidyl carboxypeptidase I; angiotensin 1 converting
enzyme 1; Dipeptidyl carboxypeptidase 1 (Angiotensin
I-converting enzyme); angiotensin I-converting enzyme
(Dipeptidyl carboxypeptidase 1); angiotensin I converting
enzyme 1; angiotensin I converting enzyme
(peptidyl-dipeptidase A) 1; angiotensin-converting
enzyme-like"
/calculated_mol_wt=147263
sig_peptide 1..35
/inference="COORDINATES: ab initio prediction:SignalP:6.0"
/calculated_mol_wt=3635
mat_peptide 36..1313
/product="Angiotensin-converting enzyme.
/id=PRO_0000028557"
/note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
/calculated_mol_wt=147263
Site 44
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Region 46..629
/region_name="Peptidase_M2"
/note="Angiotensin-converting enzyme; pfam01401"
/db_xref="CDD:460196"
Site 60
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 80
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 117
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 152
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 166
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 324
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 515
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Region 650..1227
/region_name="Peptidase_M2"
/note="Angiotensin-converting enzyme; pfam01401"
/db_xref="CDD:460196"
Site 683
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 701
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 720
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 766
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 948
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Site 1197
/site_type="glycosylation"
/note="N-linked (GlcNAc...) asparagine.
/evidence=ECO:0000255; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
Region 1221..1262
/region_name="Juxtamembrane stalk.
/evidence=ECO:0000250|UniProtKB:P12821"
/note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
Site 1266..1282
/site_type="transmembrane region"
/note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
Site 1306
/site_type="phosphorylation"
/note="Phosphoserine.
/evidence=ECO:0007744|PubMed:22673903; propagated from
UniProtKB/Swiss-Prot (P47820.1)"
CDS 1..1313
/gene="Ace"
/gene_synonym="CD143; Dcp1; StsRR92"
/coded_by="NM_012544.1:24..3965"
/db_xref="GeneID:24310"
/db_xref="RGD:2493"
ORIGIN
1 mgaasgqrgr wplsppllml slllllllpp spapaldpgl qpgnfsadea gaqlfadsyn
61 ssaevvmfqs taaswahdtn iteenarlqe eaalinqefa evwgkkakel yesiwqnftd
121 qklrriigsv qtlgpanlpl tqrlqynsll snmsriystg kvcfpnktat cwsldpeltn
181 ilassrnyak vlfawegwhd avgiplkply qdftalsnea yrqdgfsdtg aywrswyesp
241 sfeeslehly hqveplylnl hafvrralhr rygdkyinlr gpipahllgd mwaqsweniy
301 dmvvpfpdkp nldvtstmvq kgwnathmfr vaeefftslg lspmppefwa esmlekpadg
361 revvchasaw dfynrkdfri kqctrvtmdq lstvhhemgh vqyylqykdl hvslrrganp
421 gfheaigdvl alsvstpahl hkiglldrva ndiesdinyl lkmalekiaf lpfgylvdqw
481 rwgvfsgrtp psrynydwwy lrtkyqgicp pvarnethfd agakfhipsv tpyiryfvsf
541 vlqfqfhqal ckeaghqgpl hqcdiyqstk agaklqqvlq agcsrpwqev lkdlvgsdal
601 dasalmeyfq pvsqwlqeqn qrngevlgwp eyqwrpplpd nypegidlet deakanrfve
661 eydrtakvlw neyaeanwhy ntnitiegsk illqknkevs nhtlkygtwa ktfdvsnfqn
721 stikriikkv qnvdravlpp neleeynqil ldmettysva nvcytngtcl slepdltnim
781 atsrkyeell wvwkswrdkv grailpffpk yvdfsnkiak lngysdagds wrssyesddl
841 eqdleklyqe lqplylnlha yvrrslhrhy gseyinldgp ipahllgnmw aqtwsniydl
901 vapfpsapsi dateamikqg wtprrifkea dnfftslgll pvppefwnks mlekptdgre
961 vvchasawdf yngkdfrikq ctsvnmeelv iahhemghiq yfmqykdlpv tfreganpgf
1021 heaigdvlal svstpkhlhs lnllssegsg yehdinflmk maldkiafip fsylidqwrw
1081 rvfdgsitke nynqewwslr lkyqglcppv prsqgdfdpg skfhvpanvp yiryfisfii
1141 qfqfhealcr aaghtgplyk cdiyqskeag klladamklg yskqwpeamk iitgqpnmsa
1201 saimnyfkpl tewlvtenrr hgetlgwpey twtpntarae gslpessrvn flgmylepqq
1261 arvgqwvllf lgvallvatv glahrlynih nhhslrrphr gpqfgsevel rhs
//
