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Database: UniProt/SWISS-PROT
Entry: ACE_RAT
LinkDB: ACE_RAT
Original site: ACE_RAT 
ID   ACE_RAT                 Reviewed;        1313 AA.
AC   P47820; Q7TMC6; Q8CFN1; Q9EQM9;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-OCT-2017, entry version 153.
DE   RecName: Full=Angiotensin-converting enzyme;
DE            Short=ACE;
DE            EC=3.2.1.-;
DE            EC=3.4.15.1;
DE   AltName: Full=Dipeptidyl carboxypeptidase I;
DE   AltName: Full=Kininase II;
DE   AltName: CD_antigen=CD143;
DE   Contains:
DE     RecName: Full=Angiotensin-converting enzyme, soluble form;
DE   Flags: Precursor;
GN   Name=Ace; Synonyms=Dcp1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC), AND VARIANT LYS-207.
RC   TISSUE=Lung;
RX   PubMed=8292044; DOI=10.1006/bbrc.1994.1053;
RA   Koike G., Krieger J.E., Jacob H.J., Mukoyama M., Pratt R.E.,
RA   Dzau V.J.;
RT   "Angiotensin converting enzyme and genetic hypertension: cloning of
RT   rat cDNAs and characterization of the enzyme.";
RL   Biochem. Biophys. Res. Commun. 198:380-386(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
RC   STRAIN=Fischer 344/N, and Lewis/N; TISSUE=Lung;
RA   Jafarian-Tehrani M., Listwak S., Barrientos R.M., Michaud A.,
RA   Corvol P., Sternberg E.M.;
RT   "Characterization of a missense mutation in the angiotensin I-
RT   converting enzyme cDNA in exudative inflammation resistant F344/N
RT   rats.";
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), AND TISSUE
RP   SPECIFICITY.
RC   STRAIN=Sprague-Dawley; TISSUE=Testis;
RX   PubMed=12963491; DOI=10.1016/S0006-2952(03)00457-X;
RA   Tian X.-L., Paul M.;
RT   "Species-specific splicing and expression of angiotensin converting
RT   enzyme.";
RL   Biochem. Pharmacol. 66:1037-1044(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
RC   TISSUE=Lung;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 12-1313 (ISOFORM SOMATIC), AND VARIANT
RP   LYS-207.
RC   TISSUE=Kidney;
RA   Tsetsarkin K.A., Dymshits G.M., Markel A.L., Redina O.E.;
RT   "Analysis of the angiotensin converting enzyme (Ace) cDNA sequence and
RT   mRNA level of expression in WAG and ISIAH rats.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   INDUCTION.
RX   PubMed=15671045; DOI=10.1093/eurheartj/ehi114;
RA   Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S.,
RA   Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E.,
RA   Johnston C.I.;
RT   "Myocardial infarction increases ACE2 expression in rat and humans.";
RL   Eur. Heart J. 26:369-375(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1306, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA   Lundby C., Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14
RT   different rat organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
CC   -!- FUNCTION: Converts angiotensin I to angiotensin II by release of
CC       the terminal His-Leu, this results in an increase of the
CC       vasoconstrictor activity of angiotensin. Also able to inactivate
CC       bradykinin, a potent vasodilator. Has also a glycosidase activity
CC       which releases GPI-anchored proteins from the membrane by cleaving
CC       the mannose linkage in the GPI moiety. This GPIase activity seems
CC       to be crucial for the egg-binding ability of the sperm (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Release of a C-terminal dipeptide,
CC       oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither
CC       Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II,
CC       with increase in vasoconstrictor activity, but no action on
CC       angiotensin II.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only
CC       binds 1 Zn(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996; Evidence={ECO:0000250};
CC       Note=Binds 3 chloride ions per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Angiotensin-converting enzyme, soluble form:
CC       Secreted {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
CC       type I membrane protein {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Note=Detected in both cell membrane and cytoplasm in neurons.
CC       {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Somatic;
CC         IsoId=P47820-1; Sequence=Displayed;
CC       Name=Testis-specific; Synonyms=ACE-T;
CC         IsoId=P47820-2, Q8CFN1-1;
CC         Sequence=VSP_037642, VSP_037643;
CC   -!- TISSUE SPECIFICITY: Testis-specific isoform is expressed in
CC       spermatocytes, adult testis. Also expressed in brain, kidney,
CC       lung, skeletal muscle and heart. {ECO:0000269|PubMed:12963491}.
CC   -!- INDUCTION: Up-regulated after myocardial infarction.
CC       {ECO:0000269|PubMed:15671045}.
CC   -!- PTM: Phosphorylated by CK2 on Ser-1306; which allows membrane
CC       retention. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the peptidase M2 family. {ECO:0000305}.
DR   EMBL; U03708; AAA82110.1; -; mRNA.
DR   EMBL; U03734; AAA82111.1; -; mRNA.
DR   EMBL; AF201331; AAG35596.1; -; mRNA.
DR   EMBL; AF201332; AAG35597.1; -; mRNA.
DR   EMBL; AF539425; AAN17280.1; -; mRNA.
DR   EMBL; BC085760; AAH85760.1; -; mRNA.
DR   EMBL; AF532783; AAP80808.1; -; mRNA.
DR   EMBL; AF532784; AAP80809.1; -; mRNA.
DR   PIR; JC2038; JC2038.
DR   RefSeq; NP_036676.1; NM_012544.1.
DR   UniGene; Rn.10149; -.
DR   ProteinModelPortal; P47820; -.
DR   SMR; P47820; -.
DR   MINT; MINT-204637; -.
DR   STRING; 10116.ENSRNOP00000010627; -.
DR   BindingDB; P47820; -.
DR   ChEMBL; CHEMBL2625; -.
DR   GuidetoPHARMACOLOGY; 1613; -.
DR   MEROPS; M02.001; -.
DR   iPTMnet; P47820; -.
DR   PhosphoSitePlus; P47820; -.
DR   UniCarbKB; P47820; -.
DR   PaxDb; P47820; -.
DR   PRIDE; P47820; -.
DR   GeneID; 24310; -.
DR   KEGG; rno:24310; -.
DR   UCSC; RGD:2493; rat. [P47820-1]
DR   CTD; 1636; -.
DR   RGD; 2493; Ace.
DR   eggNOG; KOG3690; Eukaryota.
DR   eggNOG; ENOG410XPJ3; LUCA.
DR   HOGENOM; HOG000007838; -.
DR   HOVERGEN; HBG000264; -.
DR   InParanoid; P47820; -.
DR   KO; K01283; -.
DR   PhylomeDB; P47820; -.
DR   TreeFam; TF312861; -.
DR   BRENDA; 3.4.15.1; 5301.
DR   PRO; PR:P47820; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0009925; C:basal plasma membrane; IDA:RGD.
DR   GO; GO:0031526; C:brush border membrane; IDA:RGD.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IDA:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR   GO; GO:0097225; C:sperm midpiece; IDA:RGD.
DR   GO; GO:0031982; C:vesicle; IDA:RGD.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008144; F:drug binding; IPI:RGD.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IMP:RGD.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IDA:RGD.
DR   GO; GO:0007568; P:aging; IEP:RGD.
DR   GO; GO:0060978; P:angiogenesis involved in coronary vascular morphogenesis; IMP:RGD.
DR   GO; GO:0031100; P:animal organ regeneration; IMP:RGD.
DR   GO; GO:0010815; P:bradykinin catabolic process; IDA:RGD.
DR   GO; GO:0007420; P:brain development; IEP:RGD.
DR   GO; GO:1904045; P:cellular response to aldosterone; IEP:RGD.
DR   GO; GO:0071333; P:cellular response to glucose stimulus; IEP:RGD.
DR   GO; GO:0042755; P:eating behavior; IMP:RGD.
DR   GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:RGD.
DR   GO; GO:0007565; P:female pregnancy; IEP:RGD.
DR   GO; GO:0001822; P:kidney development; IEP:RGD.
DR   GO; GO:0048286; P:lung alveolus development; IMP:RGD.
DR   GO; GO:0030324; P:lung development; IEP:RGD.
DR   GO; GO:0008584; P:male gonad development; IEP:RGD.
DR   GO; GO:0097756; P:negative regulation of blood vessel diameter; IMP:RGD.
DR   GO; GO:0090281; P:negative regulation of calcium ion import; IMP:RGD.
DR   GO; GO:0046325; P:negative regulation of glucose import; IMP:RGD.
DR   GO; GO:0035814; P:negative regulation of renal sodium excretion; IMP:RGD.
DR   GO; GO:0043171; P:peptide catabolic process; IDA:RGD.
DR   GO; GO:0006518; P:peptide metabolic process; IMP:RGD.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0045777; P:positive regulation of blood pressure; IMP:RGD.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
DR   GO; GO:0050769; P:positive regulation of neurogenesis; IMP:RGD.
DR   GO; GO:0003084; P:positive regulation of systemic arterial blood pressure; IMP:RGD.
DR   GO; GO:0008217; P:regulation of blood pressure; IDA:BHF-UCL.
DR   GO; GO:0014910; P:regulation of smooth muscle cell migration; IDA:BHF-UCL.
DR   GO; GO:0071548; P:response to dexamethasone; IEP:RGD.
DR   GO; GO:0042493; P:response to drug; IEP:RGD.
DR   GO; GO:0001666; P:response to hypoxia; IEP:RGD.
DR   GO; GO:0034616; P:response to laminar fluid shear stress; IEP:RGD.
DR   GO; GO:0032496; P:response to lipopolysaccharide; IMP:RGD.
DR   GO; GO:0031667; P:response to nutrient levels; IEP:RGD.
DR   GO; GO:0097066; P:response to thyroid hormone; IEP:RGD.
DR   GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
DR   GO; GO:0042310; P:vasoconstriction; IMP:RGD.
DR   CDD; cd06461; M2_ACE; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; PTHR10514; 2.
DR   Pfam; PF01401; Peptidase_M2; 2.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   PROSITE; PS00142; ZINC_PROTEASE; 2.
PE   1: Evidence at protein level;
KW   Alternative splicing; Carboxypeptidase; Cell membrane;
KW   Complete proteome; Cytoplasm; Glycoprotein; Hydrolase; Membrane;
KW   Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
KW   Protease; Reference proteome; Repeat; Secreted; Signal; Transmembrane;
KW   Transmembrane helix; Zinc.
FT   SIGNAL        1     35       {ECO:0000250}.
FT   CHAIN        36   1313       Angiotensin-converting enzyme.
FT                                /FTId=PRO_0000028557.
FT   CHAIN        36   1238       Angiotensin-converting enzyme, soluble
FT                                form.
FT                                /FTId=PRO_0000028558.
FT   PROPEP     1239   1313       Removed in secreted form. {ECO:0000250}.
FT                                /FTId=PRO_0000028559.
FT   TOPO_DOM     36   1265       Extracellular. {ECO:0000255}.
FT   TRANSMEM   1266   1282       Helical. {ECO:0000255}.
FT   TOPO_DOM   1283   1313       Cytoplasmic. {ECO:0000255}.
FT   REGION       36    636       Peptidase M2 1.
FT   REGION      637   1238       Peptidase M2 2.
FT   ACT_SITE    397    397       1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   ACT_SITE    995    995       2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU10095}.
FT   METAL       396    396       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       400    400       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       424    424       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL       994    994       Zinc 2; catalytic. {ECO:0000250}.
FT   METAL       998    998       Zinc 2; catalytic. {ECO:0000250}.
FT   METAL      1022   1022       Zinc 2; catalytic. {ECO:0000250}.
FT   BINDING     237    237       Chloride 1. {ECO:0000250}.
FT   BINDING     535    535       Chloride 1. {ECO:0000250}.
FT   BINDING     797    797       Chloride 2. {ECO:0000250}.
FT   BINDING     835    835       Chloride 3. {ECO:0000250}.
FT   BINDING    1096   1096       Chloride 2. {ECO:0000250}.
FT   BINDING    1100   1100       Chloride 2. {ECO:0000250}.
FT   BINDING    1133   1133       Chloride 3. {ECO:0000250}.
FT   MOD_RES    1306   1306       Phosphoserine.
FT                                {ECO:0000244|PubMed:22673903}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     60     60       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     80     80       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    117    117       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    152    152       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    166    166       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    324    324       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    515    515       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    683    683       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    701    701       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    720    720       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    766    766       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    948    948       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD   1197   1197       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VAR_SEQ       1    581       Missing (in isoform Testis-specific).
FT                                {ECO:0000303|PubMed:12963491}.
FT                                /FTId=VSP_037642.
FT   VAR_SEQ     582    646       GCSRPWQEVLKDLVGSDALDASALMEYFQPVSQWLQEQNQR
FT                                NGEVLGWPEYQWRPPLPDNYPEGI -> MGQGWATPGLPRF
FT                                LFLLLCCGHLLPVLSQVAADHVTANQGITNQATTRSQTTHQ
FT                                STISQTIQTSNGTPGRGQGHEGARSQGPAGGNSNKTTPCGK
FT                                EGEACLFSSSPPT (in isoform Testis-
FT                                specific). {ECO:0000303|PubMed:12963491}.
FT                                /FTId=VSP_037643.
FT   VARIANT     207    207       R -> K. {ECO:0000269|PubMed:8292044,
FT                                ECO:0000269|Ref.5}.
FT   CONFLICT    341    341       L -> F (in Ref. 2; AAG35596).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1313 AA;  150908 MW;  8CB5D0015F129591 CRC64;
     MGAASGQRGR WPLSPPLLML SLLLLLLLPP SPAPALDPGL QPGNFSADEA GAQLFADSYN
     SSAEVVMFQS TAASWAHDTN ITEENARLQE EAALINQEFA EVWGKKAKEL YESIWQNFTD
     QKLRRIIGSV QTLGPANLPL TQRLQYNSLL SNMSRIYSTG KVCFPNKTAT CWSLDPELTN
     ILASSRNYAK VLFAWEGWHD AVGIPLRPLY QDFTALSNEA YRQDGFSDTG AYWRSWYESP
     SFEESLEHLY HQVEPLYLNL HAFVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWENIY
     DMVVPFPDKP NLDVTSTMVQ KGWNATHMFR VAEEFFTSLG LSPMPPEFWA ESMLEKPADG
     REVVCHASAW DFYNRKDFRI KQCTRVTMDQ LSTVHHEMGH VQYYLQYKDL HVSLRRGANP
     GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDIESDINYL LKMALEKIAF LPFGYLVDQW
     RWGVFSGRTP PSRYNYDWWY LRTKYQGICP PVARNETHFD AGAKFHIPSV TPYIRYFVSF
     VLQFQFHQAL CKEAGHQGPL HQCDIYQSTK AGAKLQQVLQ AGCSRPWQEV LKDLVGSDAL
     DASALMEYFQ PVSQWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLET DEAKANRFVE
     EYDRTAKVLW NEYAEANWHY NTNITIEGSK ILLQKNKEVS NHTLKYGTWA KTFDVSNFQN
     STIKRIIKKV QNVDRAVLPP NELEEYNQIL LDMETTYSVA NVCYTNGTCL SLEPDLTNIM
     ATSRKYEELL WVWKSWRDKV GRAILPFFPK YVDFSNKIAK LNGYSDAGDS WRSSYESDDL
     EQDLEKLYQE LQPLYLNLHA YVRRSLHRHY GSEYINLDGP IPAHLLGNMW AQTWSNIYDL
     VAPFPSAPSI DATEAMIKQG WTPRRIFKEA DNFFTSLGLL PVPPEFWNKS MLEKPTDGRE
     VVCHASAWDF YNGKDFRIKQ CTSVNMEELV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF
     HEAIGDVLAL SVSTPKHLHS LNLLSSEGSG YEHDINFLMK MALDKIAFIP FSYLIDQWRW
     RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQGDFDPG SKFHVPANVP YIRYFISFII
     QFQFHEALCR AAGHTGPLYK CDIYQSKEAG KLLADAMKLG YSKQWPEAMK IITGQPNMSA
     SAIMNYFKPL TEWLVTENRR HGETLGWPEY TWTPNTARAE GSLPESSRVN FLGMYLEPQQ
     ARVGQWVLLF LGVALLVATV GLAHRLYNIH NHHSLRRPHR GPQFGSEVEL RHS
//
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