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P47820 (ACE_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme

Short name=ACE
EC=3.2.1.-
EC=3.4.15.1
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen=CD143

Cleaved into the following chain:

  1. Angiotensin-converting enzyme, soluble form
Gene names
Name:Ace
Synonyms:Dcp1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length1313 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI-anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety. This GPIase activity seems to be crucial for the egg-binding ability of the sperm By similarity.

Catalytic activity

Release of a C-terminal dipeptide, oligopeptide-|-Xaa-Yaa, when Xaa is not Pro, and Yaa is neither Asp nor Glu. Thus, conversion of angiotensin I to angiotensin II, with increase in vasoconstrictor activity, but no action on angiotensin II.

Cofactor

Binds 2 zinc ions per subunit. Isoform Testis-specific only binds 1 zinc ion per subunit By similarity.

Binds 3 chloride ions per subunit By similarity.

Subcellular location

Angiotensin-converting enzyme, soluble form: Secreted By similarity.

Cell membrane; Single-pass type I membrane protein By similarity.

Tissue specificity

Testis-specific isoform isexpressed in spermatocytes, adult testis. Also expressed in brain, kidney, lung, skeletal muscle and heart. Ref.3

Induction

Up-regulated after myocardial infarction. Ref.6

Post-translational modification

Phosphorylated by CK2 on Ser-1306; which allows membrane retention By similarity.

Sequence similarities

Belongs to the peptidase M2 family.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Signal
Transmembrane
Transmembrane helix
   LigandMetal-binding
Zinc
   Molecular functionCarboxypeptidase
Hydrolase
Metalloprotease
Protease
   PTMGlycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaging

Inferred from expression pattern PubMed 22100841. Source: RGD

angiogenesis involved in coronary vascular morphogenesis

Inferred from mutant phenotype PubMed 22123369. Source: RGD

bradykinin catabolic process

Inferred from direct assay PubMed 2172462. Source: RGD

brain development

Inferred from expression pattern PubMed 3021286. Source: RGD

cellular response to glucose stimulus

Inferred from expression pattern PubMed 17626897. Source: RGD

eating behavior

Inferred from mutant phenotype PubMed 19361967. Source: RGD

female pregnancy

Inferred from expression pattern PubMed 17977916. Source: RGD

kidney development

Inferred from expression pattern PubMed 7977726. Source: RGD

lung alveolus development

Inferred from mutant phenotype PubMed 22587910. Source: RGD

lung development

Inferred from expression pattern PubMed 7977726. Source: RGD

male gonad development

Inferred from expression pattern PubMed 7977726. Source: RGD

negative regulation of calcium ion import

Inferred from mutant phenotype PubMed 10506486. Source: RGD

organ regeneration

Inferred from mutant phenotype PubMed 22441330. Source: RGD

peptide catabolic process

Inferred from direct assay PubMed 16148611. Source: RGD

peptide metabolic process

Inferred from mutant phenotype PubMed 10642323. Source: RGD

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 19301230. Source: RGD

positive regulation of inflammatory response

Inferred from mutant phenotype PubMed 20304959. Source: RGD

positive regulation of neurogenesis

Inferred from mutant phenotype PubMed 20122169. Source: RGD

positive regulation of systemic arterial blood pressure

Inferred from mutant phenotype PubMed 10506486. Source: RGD

proteolysis

Inferred from direct assay PubMed 16203874PubMed 16908757. Source: RGD

regulation of blood pressure

Inferred from direct assay PubMed 1750504. Source: BHF-UCL

regulation of smooth muscle cell migration

Inferred from direct assay PubMed 1750504. Source: BHF-UCL

response to dexamethasone

Inferred from expression pattern PubMed 1659346. Source: RGD

response to drug

Inferred from expression pattern PubMed 9495881. Source: RGD

response to hypoxia

Inferred from expression pattern PubMed 14527966. Source: RGD

response to laminar fluid shear stress

Inferred from expression pattern PubMed 9048650. Source: RGD

response to lipopolysaccharide

Inferred from mutant phenotype PubMed 19114890. Source: RGD

response to nutrient levels

Inferred from expression pattern PubMed 18389998. Source: RGD

response to thyroid hormone

Inferred from expression pattern PubMed 1659346. Source: RGD

sensory perception of pain

Inferred from mutant phenotype PubMed 18555989. Source: RGD

vasoconstriction

Inferred from mutant phenotype PubMed 20204775. Source: RGD

   Cellular_componentbasal plasma membrane

Inferred from direct assay PubMed 2841539. Source: RGD

brush border membrane

Inferred from direct assay PubMed 2827504. Source: RGD

extracellular space

Inferred from direct assay PubMed 19307186. Source: RGD

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from direct assay PubMed 3031366. Source: RGD

vesicle

Inferred from direct assay PubMed 2841539. Source: RGD

   Molecular_functioncarboxypeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

drug binding

Inferred from physical interaction PubMed 7620708. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from direct assay PubMed 16203874. Source: RGD

peptide binding

Inferred from direct assay PubMed 16203874. Source: RGD

peptidyl-dipeptidase activity

Inferred from direct assay Ref.1. Source: RGD

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Somatic (identifier: P47820-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform Testis-specific (identifier: P47820-2)

Also known as: ACE-T;

The sequence of this isoform differs from the canonical sequence as follows:
     1-581: Missing.
     582-646: GCSRPWQEVL...PLPDNYPEGI → MGQGWATPGL...ACLFSSSPPT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 By similarity
Chain36 – 13131278Angiotensin-converting enzyme
PRO_0000028557
Chain36 – 12381203Angiotensin-converting enzyme, soluble form
PRO_0000028558
Propeptide1239 – 131375Removed in secreted form By similarity
PRO_0000028559

Regions

Topological domain36 – 12651230Extracellular Potential
Transmembrane1266 – 128217Helical; Potential
Topological domain1283 – 131331Cytoplasmic Potential
Region36 – 636601Peptidase M2 1
Region637 – 1238602Peptidase M2 2

Sites

Active site39711 By similarity
Active site99512 By similarity
Metal binding3961Zinc 1; catalytic By similarity
Metal binding4001Zinc 1; catalytic By similarity
Metal binding4241Zinc 1; catalytic By similarity
Metal binding9941Zinc 2; catalytic By similarity
Metal binding9981Zinc 2; catalytic By similarity
Metal binding10221Zinc 2; catalytic By similarity
Binding site2371Chloride 1 By similarity
Binding site5351Chloride 1 By similarity
Binding site7971Chloride 2 By similarity
Binding site8351Chloride 3 By similarity
Binding site10961Chloride 2 By similarity
Binding site11001Chloride 2 By similarity
Binding site11331Chloride 3 By similarity

Amino acid modifications

Modified residue13061Phosphoserine By similarity
Glycosylation441N-linked (GlcNAc...) Potential
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1521N-linked (GlcNAc...) Potential
Glycosylation1661N-linked (GlcNAc...) Potential
Glycosylation3241N-linked (GlcNAc...) Potential
Glycosylation5151N-linked (GlcNAc...) Potential
Glycosylation6831N-linked (GlcNAc...) Potential
Glycosylation7011N-linked (GlcNAc...) Potential
Glycosylation7201N-linked (GlcNAc...) Potential
Glycosylation7661N-linked (GlcNAc...) Potential
Glycosylation9481N-linked (GlcNAc...) Potential
Glycosylation11971N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence1 – 581581Missing in isoform Testis-specific.
VSP_037642
Alternative sequence582 – 64665GCSRP…YPEGI → MGQGWATPGLPRFLFLLLCC GHLLPVLSQVAADHVTANQG ITNQATTRSQTTHQSTISQT IQTSNGTPGRGQGHEGARSQ GPAGGNSNKTTPCGKEGEAC LFSSSPPT in isoform Testis-specific.
VSP_037643
Natural variant2071R → K. Ref.1 Ref.5

Experimental info

Sequence conflict3411L → F in AAG35596. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform Somatic [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 8CB5D0015F129591

FASTA1,313150,908
        10         20         30         40         50         60 
MGAASGQRGR WPLSPPLLML SLLLLLLLPP SPAPALDPGL QPGNFSADEA GAQLFADSYN 

        70         80         90        100        110        120 
SSAEVVMFQS TAASWAHDTN ITEENARLQE EAALINQEFA EVWGKKAKEL YESIWQNFTD 

       130        140        150        160        170        180 
QKLRRIIGSV QTLGPANLPL TQRLQYNSLL SNMSRIYSTG KVCFPNKTAT CWSLDPELTN 

       190        200        210        220        230        240 
ILASSRNYAK VLFAWEGWHD AVGIPLRPLY QDFTALSNEA YRQDGFSDTG AYWRSWYESP 

       250        260        270        280        290        300 
SFEESLEHLY HQVEPLYLNL HAFVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWENIY 

       310        320        330        340        350        360 
DMVVPFPDKP NLDVTSTMVQ KGWNATHMFR VAEEFFTSLG LSPMPPEFWA ESMLEKPADG 

       370        380        390        400        410        420 
REVVCHASAW DFYNRKDFRI KQCTRVTMDQ LSTVHHEMGH VQYYLQYKDL HVSLRRGANP 

       430        440        450        460        470        480 
GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA NDIESDINYL LKMALEKIAF LPFGYLVDQW 

       490        500        510        520        530        540 
RWGVFSGRTP PSRYNYDWWY LRTKYQGICP PVARNETHFD AGAKFHIPSV TPYIRYFVSF 

       550        560        570        580        590        600 
VLQFQFHQAL CKEAGHQGPL HQCDIYQSTK AGAKLQQVLQ AGCSRPWQEV LKDLVGSDAL 

       610        620        630        640        650        660 
DASALMEYFQ PVSQWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLET DEAKANRFVE 

       670        680        690        700        710        720 
EYDRTAKVLW NEYAEANWHY NTNITIEGSK ILLQKNKEVS NHTLKYGTWA KTFDVSNFQN 

       730        740        750        760        770        780 
STIKRIIKKV QNVDRAVLPP NELEEYNQIL LDMETTYSVA NVCYTNGTCL SLEPDLTNIM 

       790        800        810        820        830        840 
ATSRKYEELL WVWKSWRDKV GRAILPFFPK YVDFSNKIAK LNGYSDAGDS WRSSYESDDL 

       850        860        870        880        890        900 
EQDLEKLYQE LQPLYLNLHA YVRRSLHRHY GSEYINLDGP IPAHLLGNMW AQTWSNIYDL 

       910        920        930        940        950        960 
VAPFPSAPSI DATEAMIKQG WTPRRIFKEA DNFFTSLGLL PVPPEFWNKS MLEKPTDGRE 

       970        980        990       1000       1010       1020 
VVCHASAWDF YNGKDFRIKQ CTSVNMEELV IAHHEMGHIQ YFMQYKDLPV TFREGANPGF 

      1030       1040       1050       1060       1070       1080 
HEAIGDVLAL SVSTPKHLHS LNLLSSEGSG YEHDINFLMK MALDKIAFIP FSYLIDQWRW 

      1090       1100       1110       1120       1130       1140 
RVFDGSITKE NYNQEWWSLR LKYQGLCPPV PRSQGDFDPG SKFHVPANVP YIRYFISFII 

      1150       1160       1170       1180       1190       1200 
QFQFHEALCR AAGHTGPLYK CDIYQSKEAG KLLADAMKLG YSKQWPEAMK IITGQPNMSA 

      1210       1220       1230       1240       1250       1260 
SAIMNYFKPL TEWLVTENRR HGETLGWPEY TWTPNTARAE GSLPESSRVN FLGMYLEPQQ 

      1270       1280       1290       1300       1310 
ARVGQWVLLF LGVALLVATV GLAHRLYNIH NHHSLRRPHR GPQFGSEVEL RHS 

« Hide

Isoform Testis-specific (ACE-T) [UniParc] [UniParc].

Checksum: 5967406D21CAD52A
Show »

FASTA77588,170

References

« Hide 'large scale' references
[1]"Angiotensin converting enzyme and genetic hypertension: cloning of rat cDNAs and characterization of the enzyme."
Koike G., Krieger J.E., Jacob H.J., Mukoyama M., Pratt R.E., Dzau V.J.
Biochem. Biophys. Res. Commun. 198:380-386(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC), VARIANT LYS-207.
Tissue: Lung.
[2]"Characterization of a missense mutation in the angiotensin I-converting enzyme cDNA in exudative inflammation resistant F344/N rats."
Jafarian-Tehrani M., Listwak S., Barrientos R.M., Michaud A., Corvol P., Sternberg E.M.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SOMATIC).
Strain: Fischer 344/N and Lewis/N.
Tissue: Lung.
[3]"Species-specific splicing and expression of angiotensin converting enzyme."
Tian X.-L., Paul M.
Biochem. Pharmacol. 66:1037-1044(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM TESTIS-SPECIFIC), TISSUE SPECIFICITY.
Strain: Sprague-Dawley.
Tissue: Testis.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SOMATIC).
Tissue: Lung.
[5]"Analysis of the angiotensin converting enzyme (Ace) cDNA sequence and mRNA level of expression in WAG and ISIAH rats."
Tsetsarkin K.A., Dymshits G.M., Markel A.L., Redina O.E.
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 12-1313 (ISOFORM SOMATIC), VARIANT LYS-207.
Tissue: Kidney.
[6]"Myocardial infarction increases ACE2 expression in rat and humans."
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I.
Eur. Heart J. 26:369-375(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03708 mRNA. Translation: AAA82110.1.
U03734 mRNA. Translation: AAA82111.1.
AF201331 mRNA. Translation: AAG35596.1.
AF201332 mRNA. Translation: AAG35597.1.
AF539425 mRNA. Translation: AAN17280.1.
BC085760 mRNA. Translation: AAH85760.1.
AF532783 mRNA. Translation: AAP80808.1.
AF532784 mRNA. Translation: AAP80809.1.
PIRJC2038.
RefSeqNP_036676.1. NM_012544.1.
UniGeneRn.10149.

3D structure databases

ProteinModelPortalP47820.
SMRP47820. Positions 36-647, 651-1234.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-204637.

Chemistry

BindingDBP47820.
ChEMBLCHEMBL2625.

Protein family/group databases

MEROPSM02.001.

PTM databases

PhosphoSiteP47820.

Proteomic databases

PRIDEP47820.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID24310.
KEGGrno:24310.
UCSCRGD:2493. rat. [P47820-1]

Organism-specific databases

CTD1636.
RGD2493. Ace.

Phylogenomic databases

eggNOGNOG71044.
HOGENOMHOG000007838.
HOVERGENHBG000264.
InParanoidP47820.
KOK01283.
PhylomeDBP47820.
TreeFamTF312861.

Gene expression databases

GenevestigatorP47820.

Family and domain databases

InterProIPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
PROSITEPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio602945.
PROP47820.

Entry information

Entry nameACE_RAT
AccessionPrimary (citable) accession number: P47820
Secondary accession number(s): Q7TMC6, Q8CFN1, Q9EQM9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: June 11, 2014
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries