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Protein

Angiotensin-converting enzyme 2

Gene

Ace2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. May be an important regulator of heart function.1 Publication

Miscellaneous

In contrast to its human and palm-civet orthologs, does not interact with SARS-CoV spike glycoprotein.

Catalytic activityi

Angiotensin II + H2O = angiotensin-1-7 + L-phenylalanine.

Cofactori

Protein has several cofactor binding sites:
  • Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity
  • chlorideBy similarityNote: Binds 1 Cl- ion per subunit.By similarity

Activity regulationi

Activated by chloride and fluoride, but not bromide. Inhibited by MLN-4760, cFP_Leu, and EDTA, but not by the ACE inhibitors linosipril, captopril, enalaprilat.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei169ChlorideBy similarity1
Binding sitei273SubstrateBy similarity1
Binding sitei345SubstrateBy similarity1
Binding sitei346Substrate; via carbonyl oxygenBy similarity1
Binding sitei371SubstrateBy similarity1
Metal bindingi374Zinc; catalyticPROSITE-ProRule annotation1
Active sitei375PROSITE-ProRule annotation1
Metal bindingi378Zinc; catalyticPROSITE-ProRule annotation1
Metal bindingi402Zinc; catalyticPROSITE-ProRule annotation1
Binding sitei477ChlorideBy similarity1
Binding sitei481ChlorideBy similarity1
Active sitei505PROSITE-ProRule annotation1
Binding sitei515SubstrateBy similarity1

GO - Molecular functioni

  • carboxypeptidase activity Source: CACAO
  • exopeptidase activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • metallopeptidase activity Source: UniProtKB-KW
  • peptidyl-dipeptidase activity Source: InterPro
  • virus receptor activity Source: UniProtKB

GO - Biological processi

Keywordsi

Molecular functionCarboxypeptidase, Hydrolase, Metalloprotease, Protease
LigandChloride, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.17.23 5301

Protein family/group databases

MEROPSiM02.006

Names & Taxonomyi

Protein namesi
Recommended name:
Angiotensin-converting enzyme 2 (EC:3.4.17.23)
Alternative name(s):
ACE-related carboxypeptidase
Cleaved into the following chain:
Gene namesi
Name:Ace2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi728890 Ace2

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini18 – 740ExtracellularSequence analysisAdd BLAST723
Transmembranei741 – 761HelicalSequence analysisAdd BLAST21
Topological domaini762 – 805CytoplasmicSequence analysisAdd BLAST44

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2311

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000002857418 – 805Angiotensin-converting enzyme 2Add BLAST788
ChainiPRO_000029227218 – 708Processed angiotensin-converting enzyme 2Add BLAST691

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi82N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi90N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi133 ↔ 141By similarity
Glycosylationi299N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi344 ↔ 361By similarity
Glycosylationi432N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi530 ↔ 542By similarity
Glycosylationi546N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi601N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi660N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi690N-linked (GlcNAc...) asparagineSequence analysis1

Post-translational modificationi

Glycosylated.1 Publication
Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1 (By similarity).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ5EGZ1
PRIDEiQ5EGZ1

PTM databases

SwissPalmiQ5EGZ1

Expressioni

Tissue specificityi

Expressed in heart, kidney and forebrain. In testis, expression is restricted to Leydig cells. In heart, expressed in endothelial cells from small and large arteries, arterial smooth muscle cells, and myocytes (at protein level). Ubiquitously expressed, with highest levels in ileum, bladder and lung.3 Publications

Inductioni

Down-regulated in hypertensive animals. Up-regulated after myocardial infarction.2 Publications

Interactioni

Subunit structurei

Interacts with ITGB1 and the catalytically active form of TMPRSS2.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047913

Chemistry databases

BindingDBiQ5EGZ1

Structurei

3D structure databases

ProteinModelPortaliQ5EGZ1
SMRiQ5EGZ1
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni652 – 659Essential for cleavage by ADAM17By similarity8
Regioni697 – 716Essential for cleavage by TMPRSS11D and TMPRSS2By similarityAdd BLAST20

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3690 Eukaryota
ENOG410XPJ3 LUCA
HOVERGENiHBG000265
InParanoidiQ5EGZ1
KOiK09708
PhylomeDBiQ5EGZ1

Family and domain databases

CDDicd06461 M2_ACE, 1 hit
InterProiView protein in InterPro
IPR031588 Collectrin_dom
IPR001548 Peptidase_M2
PANTHERiPTHR10514 PTHR10514, 1 hit
PfamiView protein in Pfam
PF16959 Collectrin, 1 hit
PF01401 Peptidase_M2, 1 hit
PRINTSiPR00791 PEPDIPTASEA
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 1 hit
PS00142 ZINC_PROTEASE, 1 hit

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

Q5EGZ1-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSSSCWLLLS LVAVATAQSL IEEKAESFLN KFNQEAEDLS YQSSLASWNY
60 70 80 90 100
NTNITEENAQ KMNEAAAKWS AFYEEQSKIA QNFSLQEIQN ATIKRQLKAL
110 120 130 140 150
QQSGSSALSP DKNKQLNTIL NTMSTIYSTG KVCNSMNPQE CFLLEPGLDE
160 170 180 190 200
IMATSTDYNR RLWAWEGWRA EVGKQLRPLY EEYVVLKNEM ARANNYEDYG
210 220 230 240 250
DYWRGDYEAE GVEGYNYNRN QLIEDVENTF KEIKPLYEQL HAYVRTKLME
260 270 280 290 300
VYPSYISPTG CLPAHLLGDM WGRFWTNLYP LTTPFLQKPN IDVTDAMVNQ
310 320 330 340 350
SWDAERIFKE AEKFFVSVGL PQMTPGFWTN SMLTEPGDDR KVVCHPTAWD
360 370 380 390 400
LGHGDFRIKM CTKVTMDNFL TAHHEMGHIQ YDMAYAKQPF LLRNGANEGF
410 420 430 440 450
HEAVGEIMSL SAATPKHLKS IGLLPSNFQE DNETEINFLL KQALTIVGTL
460 470 480 490 500
PFTYMLEKWR WMVFQDKIPR EQWTKKWWEM KREIVGVVEP LPHDETYCDP
510 520 530 540 550
ASLFHVSNDY SFIRYYTRTI YQFQFQEALC QAAKHDGPLH KCDISNSTEA
560 570 580 590 600
GQKLLNMLSL GNSGPWTLAL ENVVGSRNMD VKPLLNYFQP LFVWLKEQNR
610 620 630 640 650
NSTVGWSTDW SPYADQSIKV RISLKSALGK NAYEWTDNEM YLFRSSVAYA
660 670 680 690 700
MREYFSREKN QTVPFGEADV WVSDLKPRVS FNFFVTSPKN VSDIIPRSEV
710 720 730 740 750
EEAIRMSRGR INDIFGLNDN SLEFLGIYPT LKPPYEPPVT IWLIIFGVVM
760 770 780 790 800
GTVVVGIVIL IVTGIKGRKK KNETKREENP YDSMDIGKGE SNAGFQNSDD

AQTSF
Length:805
Mass (Da):92,491
Last modified:March 15, 2005 - v1
Checksum:iA4079F2407960D28
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
D3ZYK4D3ZYK4_RAT
Angiotensin-converting enzyme
Ace2
766Annotation score:
A0A0G2JXU8A0A0G2JXU8_RAT
Angiotensin-converting enzyme
Ace2
744Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY881244 mRNA Translation: AAW78017.1
RefSeqiNP_001012006.1, NM_001012006.1
UniGeneiRn.230337

Genome annotation databases

GeneIDi302668
KEGGirno:302668
UCSCiRGD:728890 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY881244 mRNA Translation: AAW78017.1
RefSeqiNP_001012006.1, NM_001012006.1
UniGeneiRn.230337

3D structure databases

ProteinModelPortaliQ5EGZ1
SMRiQ5EGZ1
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000047913

Chemistry databases

BindingDBiQ5EGZ1
ChEMBLiCHEMBL2311

Protein family/group databases

MEROPSiM02.006

PTM databases

SwissPalmiQ5EGZ1

Proteomic databases

PaxDbiQ5EGZ1
PRIDEiQ5EGZ1

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi302668
KEGGirno:302668
UCSCiRGD:728890 rat

Organism-specific databases

CTDi59272
RGDi728890 Ace2

Phylogenomic databases

eggNOGiKOG3690 Eukaryota
ENOG410XPJ3 LUCA
HOVERGENiHBG000265
InParanoidiQ5EGZ1
KOiK09708
PhylomeDBiQ5EGZ1

Enzyme and pathway databases

BRENDAi3.4.17.23 5301

Miscellaneous databases

PROiPR:Q5EGZ1

Family and domain databases

CDDicd06461 M2_ACE, 1 hit
InterProiView protein in InterPro
IPR031588 Collectrin_dom
IPR001548 Peptidase_M2
PANTHERiPTHR10514 PTHR10514, 1 hit
PfamiView protein in Pfam
PF16959 Collectrin, 1 hit
PF01401 Peptidase_M2, 1 hit
PRINTSiPR00791 PEPDIPTASEA
PROSITEiView protein in PROSITE
PS00678 WD_REPEATS_1, 1 hit
PS00142 ZINC_PROTEASE, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiACE2_RAT
AccessioniPrimary (citable) accession number: Q5EGZ1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 15, 2005
Last modified: November 7, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Peptidase families
    Classification of peptidase families and list of entries
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Main funding by: National Institutes of Health

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