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P47820

- ACE_RAT

UniProt

P47820 - ACE_RAT

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Protein

Angiotensin-converting enzyme

Gene

Ace

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

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).By similarity

Catalytic activityi

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.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 2 Zn(2+) ions per subunit. Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 3 chloride ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei237 – 2371Chloride 1By similarity
Metal bindingi396 – 3961Zinc 1; catalyticBy similarity
Active sitei397 – 39711PROSITE-ProRule annotation
Metal bindingi400 – 4001Zinc 1; catalyticBy similarity
Metal bindingi424 – 4241Zinc 1; catalyticBy similarity
Binding sitei535 – 5351Chloride 1By similarity
Binding sitei797 – 7971Chloride 2By similarity
Binding sitei835 – 8351Chloride 3By similarity
Metal bindingi994 – 9941Zinc 2; catalyticBy similarity
Active sitei995 – 99512PROSITE-ProRule annotation
Metal bindingi998 – 9981Zinc 2; catalyticBy similarity
Metal bindingi1022 – 10221Zinc 2; catalyticBy similarity
Binding sitei1096 – 10961Chloride 2By similarity
Binding sitei1100 – 11001Chloride 2By similarity
Binding sitei1133 – 11331Chloride 3By similarity

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB-KW
  2. drug binding Source: RGD
  3. metal ion binding Source: UniProtKB-KW
  4. metallopeptidase activity Source: RGD
  5. peptide binding Source: RGD
  6. peptidyl-dipeptidase activity Source: RGD

GO - Biological processi

  1. aging Source: RGD
  2. angiogenesis involved in coronary vascular morphogenesis Source: RGD
  3. bradykinin catabolic process Source: RGD
  4. brain development Source: RGD
  5. cellular response to glucose stimulus Source: RGD
  6. eating behavior Source: RGD
  7. female pregnancy Source: RGD
  8. kidney development Source: RGD
  9. lung alveolus development Source: RGD
  10. lung development Source: RGD
  11. male gonad development Source: RGD
  12. negative regulation of calcium ion import Source: RGD
  13. organ regeneration Source: RGD
  14. peptide catabolic process Source: RGD
  15. peptide metabolic process Source: RGD
  16. positive regulation of apoptotic process Source: RGD
  17. positive regulation of inflammatory response Source: RGD
  18. positive regulation of neurogenesis Source: RGD
  19. positive regulation of systemic arterial blood pressure Source: RGD
  20. proteolysis Source: RGD
  21. regulation of blood pressure Source: BHF-UCL
  22. regulation of smooth muscle cell migration Source: BHF-UCL
  23. response to dexamethasone Source: RGD
  24. response to drug Source: RGD
  25. response to hypoxia Source: RGD
  26. response to laminar fluid shear stress Source: RGD
  27. response to lipopolysaccharide Source: RGD
  28. response to nutrient levels Source: RGD
  29. response to thyroid hormone Source: RGD
  30. sensory perception of pain Source: RGD
  31. vasoconstriction Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM02.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme (EC:3.2.1.-, EC:3.4.15.1)
Short name:
ACE
Alternative name(s):
Dipeptidyl carboxypeptidase I
Kininase II
CD_antigen: CD143
Cleaved into the following chain:
Gene namesi
Name:Ace
Synonyms:Dcp1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi2493. Ace.

Subcellular locationi

Cell membrane By similarity; Single-pass type I membrane protein By similarity. Cytoplasm By similarity
Note: Detected in both cell membrane and cytoplasm in neurons.By similarity

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 12651230ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1266 – 128217HelicalSequence AnalysisAdd
BLAST
Topological domaini1283 – 131331CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. basal plasma membrane Source: RGD
  2. brush border membrane Source: RGD
  3. cytoplasm Source: UniProtKB-KW
  4. extracellular space Source: RGD
  5. integral component of membrane Source: UniProtKB-KW
  6. plasma membrane Source: RGD
  7. vesicle Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535By similarityAdd
BLAST
Chaini36 – 13131278Angiotensin-converting enzymePRO_0000028557Add
BLAST
Chaini36 – 12381203Angiotensin-converting enzyme, soluble formPRO_0000028558Add
BLAST
Propeptidei1239 – 131375Removed in secreted formBy similarityPRO_0000028559Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi44 – 441N-linked (GlcNAc...)Sequence Analysis
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi117 – 1171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi152 – 1521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi166 – 1661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi324 – 3241N-linked (GlcNAc...)Sequence Analysis
Glycosylationi515 – 5151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi683 – 6831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi701 – 7011N-linked (GlcNAc...)Sequence Analysis
Glycosylationi720 – 7201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi766 – 7661N-linked (GlcNAc...)Sequence Analysis
Glycosylationi948 – 9481N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1197 – 11971N-linked (GlcNAc...)Sequence Analysis
Modified residuei1306 – 13061PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEiP47820.

PTM databases

PhosphoSiteiP47820.

Expressioni

Tissue specificityi

Testis-specific isoform is expressed in spermatocytes, adult testis. Also expressed in brain, kidney, lung, skeletal muscle and heart.1 Publication

Inductioni

Up-regulated after myocardial infarction.1 Publication

Gene expression databases

GenevestigatoriP47820.

Interactioni

Protein-protein interaction databases

MINTiMINT-204637.

Structurei

3D structure databases

ProteinModelPortaliP47820.
SMRiP47820. Positions 36-647, 651-1234.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni36 – 636601Peptidase M2 1Add
BLAST
Regioni637 – 1238602Peptidase M2 2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71044.
HOGENOMiHOG000007838.
HOVERGENiHBG000264.
InParanoidiP47820.
KOiK01283.
PhylomeDBiP47820.
TreeFamiTF312861.

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 2 hits.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Somatic (identifier: P47820-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGAASGQRGR WPLSPPLLML SLLLLLLLPP SPAPALDPGL QPGNFSADEA
60 70 80 90 100
GAQLFADSYN SSAEVVMFQS TAASWAHDTN ITEENARLQE EAALINQEFA
110 120 130 140 150
EVWGKKAKEL YESIWQNFTD QKLRRIIGSV QTLGPANLPL TQRLQYNSLL
160 170 180 190 200
SNMSRIYSTG KVCFPNKTAT CWSLDPELTN ILASSRNYAK VLFAWEGWHD
210 220 230 240 250
AVGIPLRPLY QDFTALSNEA YRQDGFSDTG AYWRSWYESP SFEESLEHLY
260 270 280 290 300
HQVEPLYLNL HAFVRRALHR RYGDKYINLR GPIPAHLLGD MWAQSWENIY
310 320 330 340 350
DMVVPFPDKP NLDVTSTMVQ KGWNATHMFR VAEEFFTSLG LSPMPPEFWA
360 370 380 390 400
ESMLEKPADG REVVCHASAW DFYNRKDFRI KQCTRVTMDQ LSTVHHEMGH
410 420 430 440 450
VQYYLQYKDL HVSLRRGANP GFHEAIGDVL ALSVSTPAHL HKIGLLDRVA
460 470 480 490 500
NDIESDINYL LKMALEKIAF LPFGYLVDQW RWGVFSGRTP PSRYNYDWWY
510 520 530 540 550
LRTKYQGICP PVARNETHFD AGAKFHIPSV TPYIRYFVSF VLQFQFHQAL
560 570 580 590 600
CKEAGHQGPL HQCDIYQSTK AGAKLQQVLQ AGCSRPWQEV LKDLVGSDAL
610 620 630 640 650
DASALMEYFQ PVSQWLQEQN QRNGEVLGWP EYQWRPPLPD NYPEGIDLET
660 670 680 690 700
DEAKANRFVE EYDRTAKVLW NEYAEANWHY NTNITIEGSK ILLQKNKEVS
710 720 730 740 750
NHTLKYGTWA KTFDVSNFQN STIKRIIKKV QNVDRAVLPP NELEEYNQIL
760 770 780 790 800
LDMETTYSVA NVCYTNGTCL SLEPDLTNIM ATSRKYEELL WVWKSWRDKV
810 820 830 840 850
GRAILPFFPK YVDFSNKIAK LNGYSDAGDS WRSSYESDDL EQDLEKLYQE
860 870 880 890 900
LQPLYLNLHA YVRRSLHRHY GSEYINLDGP IPAHLLGNMW AQTWSNIYDL
910 920 930 940 950
VAPFPSAPSI DATEAMIKQG WTPRRIFKEA DNFFTSLGLL PVPPEFWNKS
960 970 980 990 1000
MLEKPTDGRE VVCHASAWDF YNGKDFRIKQ CTSVNMEELV IAHHEMGHIQ
1010 1020 1030 1040 1050
YFMQYKDLPV TFREGANPGF HEAIGDVLAL SVSTPKHLHS LNLLSSEGSG
1060 1070 1080 1090 1100
YEHDINFLMK MALDKIAFIP FSYLIDQWRW RVFDGSITKE NYNQEWWSLR
1110 1120 1130 1140 1150
LKYQGLCPPV PRSQGDFDPG SKFHVPANVP YIRYFISFII QFQFHEALCR
1160 1170 1180 1190 1200
AAGHTGPLYK CDIYQSKEAG KLLADAMKLG YSKQWPEAMK IITGQPNMSA
1210 1220 1230 1240 1250
SAIMNYFKPL TEWLVTENRR HGETLGWPEY TWTPNTARAE GSLPESSRVN
1260 1270 1280 1290 1300
FLGMYLEPQQ ARVGQWVLLF LGVALLVATV GLAHRLYNIH NHHSLRRPHR
1310
GPQFGSEVEL RHS
Length:1,313
Mass (Da):150,908
Last modified:February 1, 1996 - v1
Checksum:i8CB5D0015F129591
GO
Isoform Testis-specific (identifier: P47820-2) [UniParc] [UniParc]FASTAAdd to Basket

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

Show »
Length:775
Mass (Da):88,170
Checksum:i5967406D21CAD52A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti341 – 3411L → F in AAG35596. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti207 – 2071R → K.2 Publications

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 581581Missing in isoform Testis-specific. 1 PublicationVSP_037642Add
BLAST
Alternative sequencei582 – 64665GCSRP…YPEGI → MGQGWATPGLPRFLFLLLCC GHLLPVLSQVAADHVTANQG ITNQATTRSQTTHQSTISQT IQTSNGTPGRGQGHEGARSQ GPAGGNSNKTTPCGKEGEAC LFSSSPPT in isoform Testis-specific. 1 PublicationVSP_037643Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiJC2038.
RefSeqiNP_036676.1. NM_012544.1.
UniGeneiRn.10149.

Genome annotation databases

GeneIDi24310.
KEGGirno:24310.
UCSCiRGD:2493. rat. [P47820-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
PIRi JC2038.
RefSeqi NP_036676.1. NM_012544.1.
UniGenei Rn.10149.

3D structure databases

ProteinModelPortali P47820.
SMRi P47820. Positions 36-647, 651-1234.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-204637.

Chemistry

BindingDBi P47820.
ChEMBLi CHEMBL2625.
GuidetoPHARMACOLOGYi 1613.

Protein family/group databases

MEROPSi M02.001.

PTM databases

PhosphoSitei P47820.

Proteomic databases

PRIDEi P47820.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 24310.
KEGGi rno:24310.
UCSCi RGD:2493. rat. [P47820-1 ]

Organism-specific databases

CTDi 1636.
RGDi 2493. Ace.

Phylogenomic databases

eggNOGi NOG71044.
HOGENOMi HOG000007838.
HOVERGENi HBG000264.
InParanoidi P47820.
KOi K01283.
PhylomeDBi P47820.
TreeFami TF312861.

Miscellaneous databases

NextBioi 602945.
PROi P47820.

Gene expression databases

Genevestigatori P47820.

Family and domain databases

InterProi IPR001548. Peptidase_M2.
[Graphical view ]
PANTHERi PTHR10514. PTHR10514. 1 hit.
Pfami PF01401. Peptidase_M2. 2 hits.
[Graphical view ]
PRINTSi PR00791. PEPDIPTASEA.
PROSITEi PS00142. ZINC_PROTEASE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: INDUCTION.

Entry informationi

Entry nameiACE_RAT
AccessioniPrimary (citable) accession number: P47820
Secondary accession number(s): Q7TMC6, Q8CFN1, Q9EQM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 134 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3