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Protein

Angiotensin-converting enzyme 2

Gene

Ace2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

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

Enzyme 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

GO - Biological processi

  • angiotensin maturation Source: InterPro
  • maternal process involved in female pregnancy Source: RGD
  • negative regulation of ERK1 and ERK2 cascade Source: RGD
  • negative regulation of smooth muscle cell proliferation Source: RGD
  • receptor-mediated virion attachment to host cell Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Chloride, 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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi728890. Ace2.

Subcellular locationi

Topology

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

GO - Cellular componenti

  • cell surface Source: UniProtKB
  • cytoplasm Source: UniProtKB-SubCell
  • extracellular space Source: RGD
  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: RGD
  • plasma membrane Source: UniProtKB
Complete GO annotation...

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...)Sequence analysis1
Glycosylationi82N-linked (GlcNAc...)Sequence analysis1
Glycosylationi90N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi133 ↔ 141By similarity
Glycosylationi299N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi344 ↔ 361By similarity
Glycosylationi432N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi530 ↔ 542By similarity
Glycosylationi546N-linked (GlcNAc...)Sequence analysis1
Glycosylationi601N-linked (GlcNAc...)Sequence analysis1
Glycosylationi660N-linked (GlcNAc...)Sequence analysis1
Glycosylationi690N-linked (GlcNAc...)Sequence 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

Gene expression databases

BgeeiENSRNOG00000031665.

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.
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.
InterProiIPR033591. ACE2.
IPR031588. Collectrin_dom.
IPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 2 hits.
PTHR10514:SF24. PTHR10514:SF24. 2 hits.
PfamiPF16959. Collectrin. 1 hit.
PF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

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.

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.
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

PROiQ5EGZ1.

Gene expression databases

BgeeiENSRNOG00000031665.

Family and domain databases

CDDicd06461. M2_ACE. 1 hit.
InterProiIPR033591. ACE2.
IPR031588. Collectrin_dom.
IPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 2 hits.
PTHR10514:SF24. PTHR10514:SF24. 2 hits.
PfamiPF16959. Collectrin. 1 hit.
PF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACE2_RAT
AccessioniPrimary (citable) accession number: Q5EGZ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: March 15, 2005
Last modified: November 30, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.