GenomeNet

Database: RefSeq
Entry: NP_036676
LinkDB: NP_036676
Original site: NP_036676 
LOCUS       NP_036676               1313 aa            linear   ROD 11-NOV-2018
DEFINITION  angiotensin-converting enzyme precursor [Rattus norvegicus].
ACCESSION   NP_036676
VERSION     NP_036676.1
DBSOURCE    REFSEQ: accession NM_012544.1
KEYWORDS    RefSeq.
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   Faulk KE, Nedungadi TP and Cunningham JT.
  TITLE     Angiotensin converting enzyme 1 in the median preoptic nucleus
            contributes to chronic intermittent hypoxia hypertension
  JOURNAL   Physiol Rep 5 (10) (2017)
   PUBMED   28536140
  REMARK    GeneRIF: Data suggest that angiotensin converting enzyme 1 within
            median preoptic nucleus plays a critical role in the sustained
            hypertension seen in chronic intermittent hypoxia.
REFERENCE   2  (residues 1 to 1313)
  AUTHORS   Faulk K, Shell B, Nedungadi TP and Cunningham JT.
  TITLE     Role of angiotensin-converting enzyme 1 within the median preoptic
            nucleus following chronic intermittent hypoxia
  JOURNAL   Am. J. Physiol. Regul. Integr. Comp. Physiol. 312 (2), R245-R252
            (2017)
   PUBMED   28003214
  REMARK    GeneRIF: Chromatin immunoprecipitation (ChIP) assays demonstrated
            an increase in FosB/DeltaFosB association with the ACE1 gene within
            the MnPO following CIH. FosB/DeltaFosB may transcriptionally target
            ACE1 within the MnPO following CIH to affect the downstream PVN
            region, which may influence SNA and blood pressure.
REFERENCE   3  (residues 1 to 1313)
  AUTHORS   Sanguesa G, Shaligram S, Akther F, Roglans N, Laguna JC, Rahimian R
            and Alegret M.
  TITLE     Type of supplemented simple sugar, not merely calorie intake,
            determines adverse effects on metabolism and aortic function in
            female rats
  JOURNAL   Am. J. Physiol. Heart Circ. Physiol. 312 (2), H289-H304 (2017)
   PUBMED   27923787
REFERENCE   4  (residues 1 to 1313)
  AUTHORS   Wang J, Yin N, Deng Y, Wei Y, Huang Y, Pu X, Li L, Zheng Y, Guo J,
            Yu J, Li X and Yi P.
  TITLE     Ascorbic Acid Protects against Hypertension through Downregulation
            of ACE1 Gene Expression Mediated by Histone Deacetylation in
            Prenatal Inflammation-Induced Offspring
  JOURNAL   Sci Rep 6, 39469 (2016)
   PUBMED   27995995
  REMARK    GeneRIF: ascorbic acid is able to prevent hypertension in offspring
            from prenatal inflammation exposure through ACE1 downregulation
            Publication Status: Online-Only
REFERENCE   5  (residues 1 to 1313)
  AUTHORS   Dos Santos RL, Dellacqua LO, Delgado NT, Rouver WN, Podratz PL,
            Lima LC, Piccin MP, Meyrelles SS, Mauad H, Graceli JB and Moyses
            MR.
  TITLE     Pomegranate peel extract attenuates oxidative stress by decreasing
            coronary angiotensin-converting enzyme (ACE) activity in
            hypertensive female rats
  JOURNAL   J. Toxicol. Environ. Health Part A 79 (21), 998-1007 (2016)
   PUBMED   27710705
  REMARK    GeneRIF: Pomegranate peel extract consumption conferred protection
            against hypertension in the spontaneously hypertensive rat model.
            This finding was demonstrated by marked reduction in coronary ACE
            activity, oxidative stress, and vascular remodelling.
REFERENCE   6  (residues 1 to 1313)
  AUTHORS   Martinelli I, Mainini E and Mazzi C.
  TITLE     [Effect of 5-hydroxytryptophan on the secretion of PRL, GH, TSH and
            cortisol in obesity]
  JOURNAL   Minerva Endocrinol. 17 (3), 121-126 (1992)
   PUBMED   1298871
REFERENCE   7  (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   8  (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   9  (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   10 (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
COMMENT     PROVISIONAL REFSEQ: This record has not yet been subject to final
            NCBI review. The reference sequence was derived from U03734.1.
            
            Summary: catalyzes the conversion of angiotensin I to angiotensin
            II; plays a role in regulation of blood pressure [RGD, Feb 2006].
            
            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 :: BC085760.1 [ECO:0000332]
            RNAseq introns              :: single sample supports all introns
                                           SAMD00052296, SAMD00052297
                                           [ECO:0000348]
            ##Evidence-Data-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"
                     /calculated_mol_wt=147263
     sig_peptide     1..35
                     /inference="COORDINATES: ab initio prediction:SignalP:4.0"
                     /calculated_mol_wt=3635
     mat_peptide     36..1313
                     /product="Angiotensin-converting enzyme"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
                     /calculated_mol_wt=147263
     Region          36..636
                     /region_name="Peptidase M2 1"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
     Region          46..629
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:279709"
     Site            order(366..368,396..397,400,424,470,524..526,531,533,536)
                     /site_type="active"
                     /db_xref="CDD:188999"
     Site            order(396,400,424)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188999"
     Region          637..1238
                     /region_name="Peptidase M2 2"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
     Region          650..1227
                     /region_name="Peptidase_M2"
                     /note="Angiotensin-converting enzyme; pfam01401"
                     /db_xref="CDD:279709"
     Site            order(964..966,994..995,998,1022,1068,1122..1124,1129,
                     1131,1134)
                     /site_type="active"
                     /db_xref="CDD:188999"
     Site            order(994,998,1022)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188999"
     Site            1266..1282
                     /site_type="transmembrane region"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="propagated from UniProtKB/Swiss-Prot (P47820.1)"
     Site            1306
                     /site_type="other"
                     /experiment="experimental evidence, no additional details
                     recorded"
                     /note="Phosphoserine. {ECO:0000244|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
//
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