Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9BYF1

- ACE2_HUMAN

UniProt

Q9BYF1 - ACE2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Angiotensin-converting enzyme 2

Gene

ACE2

Organism
Homo sapiens (Human)
Status
Reviewed - 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. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.4 Publications

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:

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 and enalaprilat.4 Publications

Kineticsi

  1. KM=6.9 µM for angiotensin I1 Publication
  2. KM=2 µM for angiotensin II1 Publication
  3. KM=6.8 µM for apelin-131 Publication
  4. KM=5.5 µM for dynorphin-131 Publication

pH dependencei

Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei169 – 1691Chloride
Binding sitei273 – 2731Substrate
Binding sitei345 – 3451Substrate
Binding sitei346 – 3461Substrate; via carbonyl oxygen
Binding sitei371 – 3711Substrate
Metal bindingi374 – 3741Zinc; catalytic
Active sitei375 – 3751
Metal bindingi378 – 3781Zinc; catalytic
Metal bindingi402 – 4021Zinc; catalytic
Binding sitei477 – 4771Chloride
Binding sitei481 – 4811Chloride
Active sitei505 – 5051
Binding sitei515 – 5151Substrate

GO - Molecular functioni

  1. carboxypeptidase activity Source: UniProtKB
  2. endopeptidase activity Source: UniProtKB
  3. glycoprotein binding Source: BHF-UCL
  4. peptide hormone binding Source: Ensembl
  5. virus receptor activity Source: UniProtKB
  6. zinc ion binding Source: BHF-UCL

GO - Biological processi

  1. angiotensin catabolic process in blood Source: BHF-UCL
  2. angiotensin maturation Source: Reactome
  3. angiotensin-mediated drinking behavior Source: BHF-UCL
  4. cellular protein metabolic process Source: Reactome
  5. positive regulation of reactive oxygen species metabolic process Source: BHF-UCL
  6. receptor biosynthetic process Source: BHF-UCL
  7. receptor-mediated virion attachment to host cell Source: BHF-UCL
  8. regulation of cell proliferation Source: BHF-UCL
  9. regulation of cytokine production Source: BHF-UCL
  10. regulation of inflammatory response Source: BHF-UCL
  11. regulation of systemic arterial blood pressure by renin-angiotensin Source: BHF-UCL
  12. regulation of vasoconstriction Source: BHF-UCL
  13. regulation of vasodilation Source: BHF-UCL
  14. response to virus Source: GOC
  15. viral entry into host cell Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

Host-virus interaction

Keywords - Ligandi

Chloride, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.15.1. 2681.
ReactomeiREACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RKQ9BYF1.

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
Angiotensin-converting enzyme homolog
Short name:
ACEH
Metalloprotease MPROT15
Cleaved into the following chain:
Gene namesi
Name:ACE2
ORF Names:UNQ868/PRO1885
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:13557. ACE2.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 740723ExtracellularSequence AnalysisAdd
BLAST
Transmembranei741 – 76121HelicalSequence AnalysisAdd
BLAST
Topological domaini762 – 80544CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. cell surface Source: UniProtKB
  2. cytoplasm Source: UniProtKB-KW
  3. extracellular region Source: UniProtKB
  4. extracellular space Source: BHF-UCL
  5. extracellular vesicular exosome Source: UniProtKB
  6. integral component of membrane Source: UniProtKB-KW
  7. membrane raft Source: BHF-UCL
  8. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi24 – 263QAK → KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi31 – 311K → D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi37 – 371E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi38 – 381D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi41 – 411Y → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi68 – 681K → D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi82 – 843MYP → NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi110 – 1101E → P: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi135 – 1362PD → SM: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi160 – 1601E → R: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi192 – 1921R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi219 – 2191R → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi239 – 2391H → Q: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi309 – 3091K → D: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi312 – 3121E → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi324 – 3241T → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi338 – 3403NVQ → DDR: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi350 – 3501D → A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi353 – 3531K → H, A or D: Abolishes interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi355 – 3551D → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi357 – 3571R → A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi359 – 3591L → K or A: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi383 – 3831M → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi389 – 3891P → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi393 – 3931R → A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi425 – 4273SPD → PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi465 – 4673KGE → QDK: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi559 – 5591R → S: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 1 Publication
Mutagenesisi603 – 6031F → T: No effect on interaction with SARS-CoV spike glycoprotein. 1 Publication

Organism-specific databases

PharmGKBiPA425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 805788Angiotensin-converting enzyme 2PRO_0000028570Add
BLAST
Chaini18 – 708691Processed angiotensin-converting enzyme 2PRO_0000292268Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi53 – 531N-linked (GlcNAc...)1 Publication
Glycosylationi90 – 901N-linked (GlcNAc...)2 Publications
Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
Disulfide bondi133 ↔ 1411 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...)1 Publication
Disulfide bondi344 ↔ 3611 Publication
Glycosylationi432 – 4321N-linked (GlcNAc...)1 Publication
Disulfide bondi530 ↔ 5421 Publication
Glycosylationi546 – 5461N-linked (GlcNAc...)2 Publications
Glycosylationi690 – 6901N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylation on Asn-90 may limit SARS infectivity.5 Publications
Proteolytic cleavage by ADAM17 generates a secreted form. Also cleaved by serine proteases: TMPRSS2, TMPRSS11D and HPN/TMPRSS1.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ9BYF1.
PRIDEiQ9BYF1.

PTM databases

PhosphoSiteiQ9BYF1.

Miscellaneous databases

PMAP-CutDBQ9BYF1.

Expressioni

Tissue specificityi

Expressed in endothelial cells from small and large arteries, and in arterial smooth muscle cells. Expressed in lung alveolar epithelial cells, enterocytes of the small intestine, Leydig cells and Sertoli cells (at protein level). Expressed in heart, kidney, testis, and gastrointestinal system.6 Publications

Inductioni

Up-regulated in failing heart.2 Publications

Gene expression databases

BgeeiQ9BYF1.
CleanExiHS_ACE2.
GenevestigatoriQ9BYF1.

Organism-specific databases

HPAiCAB026174.
HPA000288.

Interactioni

Subunit structurei

Interacts with ITGB1. Interacts with SARS-CoV and HCoV-NL63 spike glycoprotein. Interacts with the catalytically active form of TMPRSS2.7 Publications

Protein-protein interaction databases

BioGridi121864. 4 interactions.
DIPiDIP-44689N.
IntActiQ9BYF1. 1 interaction.
MINTiMINT-4538816.
STRINGi9606.ENSP00000252519.

Structurei

Secondary structure

1
805
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 5230Combined sources
Helixi56 – 7722Combined sources
Turni78 – 825Combined sources
Helixi85 – 873Combined sources
Helixi91 – 10010Combined sources
Helixi104 – 1074Combined sources
Helixi110 – 12920Combined sources
Beta strandi131 – 1344Combined sources
Beta strandi137 – 1437Combined sources
Turni144 – 1463Combined sources
Helixi148 – 1547Combined sources
Helixi158 – 17114Combined sources
Helixi173 – 19321Combined sources
Beta strandi196 – 1983Combined sources
Helixi199 – 2046Combined sources
Turni205 – 2073Combined sources
Turni213 – 2153Combined sources
Helixi220 – 25132Combined sources
Turni253 – 2553Combined sources
Beta strandi258 – 2603Combined sources
Helixi264 – 2663Combined sources
Beta strandi267 – 2715Combined sources
Helixi276 – 2783Combined sources
Helixi279 – 2824Combined sources
Turni284 – 2874Combined sources
Turni294 – 2974Combined sources
Helixi298 – 3003Combined sources
Helixi304 – 31613Combined sources
Turni317 – 3193Combined sources
Helixi327 – 3304Combined sources
Beta strandi338 – 3403Combined sources
Beta strandi347 – 3526Combined sources
Beta strandi355 – 3595Combined sources
Helixi366 – 38419Combined sources
Turni385 – 3873Combined sources
Helixi390 – 3923Combined sources
Helixi400 – 41314Combined sources
Helixi415 – 4206Combined sources
Turni422 – 4265Combined sources
Helixi432 – 44615Combined sources
Helixi449 – 46517Combined sources
Beta strandi466 – 4683Combined sources
Helixi470 – 4723Combined sources
Helixi473 – 48311Combined sources
Beta strandi486 – 4883Combined sources
Helixi499 – 5024Combined sources
Helixi504 – 5074Combined sources
Helixi514 – 53118Combined sources
Turni532 – 5343Combined sources
Helixi539 – 5413Combined sources
Helixi548 – 55811Combined sources
Turni559 – 5624Combined sources
Helixi566 – 5749Combined sources
Beta strandi575 – 5784Combined sources
Helixi582 – 59817Combined sources
Beta strandi600 – 6023Combined sources
Beta strandi607 – 6093Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1R42X-ray2.20A1-615[»]
1R4LX-ray3.00A1-615[»]
1XJPmodel-B19-615[»]
2AJFX-ray2.90A/B19-615[»]
3D0GX-ray2.80A/B56-615[»]
3D0HX-ray3.10A/B56-615[»]
3D0IX-ray2.90A/B56-615[»]
3KBHX-ray3.31A/B/C/D19-615[»]
3SCIX-ray2.90A/B19-615[»]
3SCJX-ray3.00A/B19-615[»]
3SCKX-ray3.00A/B83-615[»]
3SCLX-ray3.00A/B83-615[»]
ProteinModelPortaliQ9BYF1.
SMRiQ9BYF1. Positions 19-615.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BYF1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni30 – 4112Interaction with SARS-CoV spike glycoproteinAdd
BLAST
Regioni82 – 843Interaction with SARS-CoV spike glycoprotein
Regioni353 – 3575Interaction with SARS-CoV spike glycoprotein
Regioni652 – 6598Essential for cleavage by ADAM17
Regioni697 – 71620Essential for cleavage by TMPRSS11D and TMPRSS2Add
BLAST

Sequence similaritiesi

Belongs to the peptidase M2 family.Curated

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71044.
GeneTreeiENSGT00520000055576.
HOGENOMiHOG000292210.
HOVERGENiHBG000265.
InParanoidiQ9BYF1.
KOiK09708.
OMAiRDGANEG.
OrthoDBiEOG76HQ13.
PhylomeDBiQ9BYF1.
TreeFamiTF312861.

Family and domain databases

InterProiIPR001548. Peptidase_M2.
[Graphical view]
PANTHERiPTHR10514. PTHR10514. 1 hit.
PfamiPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSiPR00791. PEPDIPTASEA.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[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 1 (identifier: Q9BYF1-1) [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
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY
60 70 80 90 100
NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL
110 120 130 140 150
QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE
160 170 180 190 200
IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG
210 220 230 240 250
DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN
260 270 280 290 300
AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ
310 320 330 340 350
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD
360 370 380 390 400
LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF
410 420 430 440 450
HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL
460 470 480 490 500
PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP
510 520 530 540 550
ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA
560 570 580 590 600
GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK
610 620 630 640 650
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA
660 670 680 690 700
MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV
710 720 730 740 750
EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM
760 770 780 790 800
GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD

VQTSF
Length:805
Mass (Da):92,463
Last modified:August 2, 2005 - v2
Checksum:i8EE6EB0A931550E8
GO
Isoform 2 (identifier: Q9BYF1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     555-555: F → L
     556-805: Missing.

Note: No experimental confirmation available.

Show »
Length:555
Mass (Da):63,912
Checksum:i3A3842AB792E2DBC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti18 – 181Q → H in CAB53682. (PubMed:17974005)Curated
Sequence conflicti508 – 5081N → D in AAQ89076. (PubMed:12975309)Curated
Sequence conflicti631 – 6311K → R in BAB40370. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti26 – 261K → R.1 Publication
Corresponds to variant rs4646116 [ dbSNP | Ensembl ].
VAR_023082
Natural varianti638 – 6381N → S.1 Publication
Corresponds to variant rs183135788 [ dbSNP | Ensembl ].
VAR_023083

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei555 – 5551F → L in isoform 2. 1 PublicationVSP_014901
Alternative sequencei556 – 805250Missing in isoform 2. 1 PublicationVSP_014902Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291820 mRNA. Translation: AAF99721.1.
AF241254 mRNA. Translation: AAF78220.1.
AY623811 mRNA. Translation: AAT45083.1.
AB193259 mRNA. Translation: BAD99266.1.
AB193260 mRNA. Translation: BAD99267.1.
AB046569 mRNA. Translation: BAB40370.1.
E39033 mRNA. No translation available.
GQ262784 mRNA. Translation: ACT66268.1.
AY358714 mRNA. Translation: AAQ89076.1.
AY217547 Genomic DNA. Translation: AAO25651.1.
CH471074 Genomic DNA. Translation: EAW98892.1.
BC039902 mRNA. Translation: AAH39902.1.
BC048094 mRNA. Translation: AAH48094.2.
AL110224 mRNA. Translation: CAB53682.1.
CCDSiCCDS14169.1. [Q9BYF1-1]
PIRiT14762.
RefSeqiNP_068576.1. NM_021804.2. [Q9BYF1-1]
UniGeneiHs.178098.

Genome annotation databases

EnsembliENST00000252519; ENSP00000252519; ENSG00000130234. [Q9BYF1-1]
ENST00000427411; ENSP00000389326; ENSG00000130234. [Q9BYF1-1]
GeneIDi59272.
KEGGihsa:59272.
UCSCiuc004cxa.1. human. [Q9BYF1-1]

Polymorphism databases

DMDMi71658783.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

SeattleSNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF291820 mRNA. Translation: AAF99721.1 .
AF241254 mRNA. Translation: AAF78220.1 .
AY623811 mRNA. Translation: AAT45083.1 .
AB193259 mRNA. Translation: BAD99266.1 .
AB193260 mRNA. Translation: BAD99267.1 .
AB046569 mRNA. Translation: BAB40370.1 .
E39033 mRNA. No translation available.
GQ262784 mRNA. Translation: ACT66268.1 .
AY358714 mRNA. Translation: AAQ89076.1 .
AY217547 Genomic DNA. Translation: AAO25651.1 .
CH471074 Genomic DNA. Translation: EAW98892.1 .
BC039902 mRNA. Translation: AAH39902.1 .
BC048094 mRNA. Translation: AAH48094.2 .
AL110224 mRNA. Translation: CAB53682.1 .
CCDSi CCDS14169.1. [Q9BYF1-1 ]
PIRi T14762.
RefSeqi NP_068576.1. NM_021804.2. [Q9BYF1-1 ]
UniGenei Hs.178098.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1R42 X-ray 2.20 A 1-615 [» ]
1R4L X-ray 3.00 A 1-615 [» ]
1XJP model - B 19-615 [» ]
2AJF X-ray 2.90 A/B 19-615 [» ]
3D0G X-ray 2.80 A/B 56-615 [» ]
3D0H X-ray 3.10 A/B 56-615 [» ]
3D0I X-ray 2.90 A/B 56-615 [» ]
3KBH X-ray 3.31 A/B/C/D 19-615 [» ]
3SCI X-ray 2.90 A/B 19-615 [» ]
3SCJ X-ray 3.00 A/B 19-615 [» ]
3SCK X-ray 3.00 A/B 83-615 [» ]
3SCL X-ray 3.00 A/B 83-615 [» ]
ProteinModelPortali Q9BYF1.
SMRi Q9BYF1. Positions 19-615.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121864. 4 interactions.
DIPi DIP-44689N.
IntActi Q9BYF1. 1 interaction.
MINTi MINT-4538816.
STRINGi 9606.ENSP00000252519.

Chemistry

BindingDBi Q9BYF1.
ChEMBLi CHEMBL2096989.
DrugBanki DB00722. Lisinopril.
DB00691. Moexipril.
GuidetoPHARMACOLOGYi 1614.

Protein family/group databases

MEROPSi M02.006.

PTM databases

PhosphoSitei Q9BYF1.

Polymorphism databases

DMDMi 71658783.

Proteomic databases

PaxDbi Q9BYF1.
PRIDEi Q9BYF1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252519 ; ENSP00000252519 ; ENSG00000130234 . [Q9BYF1-1 ]
ENST00000427411 ; ENSP00000389326 ; ENSG00000130234 . [Q9BYF1-1 ]
GeneIDi 59272.
KEGGi hsa:59272.
UCSCi uc004cxa.1. human. [Q9BYF1-1 ]

Organism-specific databases

CTDi 59272.
GeneCardsi GC0XM015579.
HGNCi HGNC:13557. ACE2.
HPAi CAB026174.
HPA000288.
MIMi 300335. gene.
neXtProti NX_Q9BYF1.
PharmGKBi PA425.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71044.
GeneTreei ENSGT00520000055576.
HOGENOMi HOG000292210.
HOVERGENi HBG000265.
InParanoidi Q9BYF1.
KOi K09708.
OMAi RDGANEG.
OrthoDBi EOG76HQ13.
PhylomeDBi Q9BYF1.
TreeFami TF312861.

Enzyme and pathway databases

BRENDAi 3.4.15.1. 2681.
Reactomei REACT_147707. Metabolism of Angiotensinogen to Angiotensins.
SABIO-RK Q9BYF1.

Miscellaneous databases

ChiTaRSi ACE2. human.
EvolutionaryTracei Q9BYF1.
GeneWikii Angiotensin-converting_enzyme_2.
GenomeRNAii 59272.
NextBioi 65154.
PMAP-CutDB Q9BYF1.
PROi Q9BYF1.
SOURCEi Search...

Gene expression databases

Bgeei Q9BYF1.
CleanExi HS_ACE2.
Genevestigatori Q9BYF1.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9."
    Donoghue M., Hsieh F., Baronas E., Godbout K., Gosselin M., Stagliano N., Donovan M., Woolf B., Robison K., Jeyaseelan R., Breitbart R.E., Acton S.
    Circ. Res. 87:E1-E9(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, ENZYME REGULATION.
    Tissue: Heart.
  2. "A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase."
    Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.
    J. Biol. Chem. 275:33238-33243(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, ENZYME REGULATION.
    Tissue: Lymphoma.
  3. "The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis."
    Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., Smith A.I., Lew R.A.
    Endocrinology 145:4703-4711(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Tissue: Testis.
  4. "Identification of an alternative 5'-untranslated exon and new polymorphisms of angiotensin-converting enzyme 2 gene: lack of association with SARS in the Vietnamese population."
    Itoyama S., Keicho N., Hijikata M., Quy T., Phi N.C., Long H.T., Ha L.D., Ban V.V., Matsushita I., Yanai H., Kirikae F., Kirikae T., Kuratsuji T., Sasazuki T.
    Am. J. Med. Genet. A 136:52-57(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-638.
    Tissue: Lung and Testis.
  5. "Cloning, expression analysis and chromosomal localization of a novel ACE like enzyme."
    Suzuki Y., Watanabe M., Sugano S.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  6. "MPROT15 polypeptide and MPROT15 polynucleotide."
    Southan C., Burgess N.
    Patent number JP11318472, 24-NOV-1999
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  7. "Comparative susceptibility to SARS-CoV mediated by ACE2 protein of 15 different species."
    Li K.K.B., Yip C.W., Hon C.C., Lam C.Y., Leung F.C.C.
    Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  9. SeattleSNPs variation discovery resource
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-26.
  10. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  11. "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 1).
    Tissue: Brain and Testis.
  12. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1).
    Tissue: Testis.
  13. "Interaction of ACE2 and integrin beta1 in failing human heart."
    Lin Q., Keller R.S., Weaver B., Zisman L.S.
    Biochim. Biophys. Acta 1689:175-178(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ITGB1.
  14. "Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme."
    Harmer D., Gilbert M., Borman R., Clark K.L.
    FEBS Lett. 532:107-110(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  15. "Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase."
    Vickers C., Hales P., Kaushik V., Dick L., Gavin J., Tang J., Godbout K., Parsons T., Baronas E., Hsieh F., Acton S., Patane M.A., Nichols A., Tummino P.
    J. Biol. Chem. 277:14838-14843(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, COFACTOR.
  16. "Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus."
    Li W., Moore M.J., Vasilieva N., Sui J., Wong S.-K., Berne M.A., Somasundaran M., Sullivan J.L., Luzuriaga K., Greenough T.C., Choe H., Farzan M.
    Nature 426:450-454(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, GLYCOSYLATION, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "ACE2 gene expression is up-regulated in the human failing heart."
    Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.
    BMC Med. 2:19-19(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  18. "Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis."
    Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J., van Goor H.
    J. Pathol. 203:631-637(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  19. "Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2."
    Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., Sullivan J.L., Farzan M., Choe H.
    J. Virol. 78:11429-11433(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN.
  20. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90.
    Tissue: Bile.
  21. Cited for: TISSUE SPECIFICITY, INDUCTION.
  22. Cited for: INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, MUTAGENESIS.
  23. "Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)."
    Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., Hooper N.M., Turner A.J.
    J. Biol. Chem. 280:30113-30119(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE.
  24. "Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry."
    Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.
    Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN.
  25. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546.
    Tissue: Liver.
  26. "Angiotensin-converting enzyme 2 ectodomain shedding cleavage-site identification: determinants and constraints."
    Lai Z.W., Hanchapola I., Steer D.L., Smith A.I.
    Biochemistry 50:5182-5194(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC CLEAVAGE.
  27. "A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry."
    Shulla A., Heald-Sargent T., Subramanya G., Zhao J., Perlman S., Gallagher T.
    J. Virol. 85:873-882(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, INTERACTION WITH TMPRSS2.
  28. "TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein."
    Heurich A., Hofmann-Winkler H., Gierer S., Liepold T., Jahn O., Poehlmann S.
    J. Virol. 88:1293-1307(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE.
  29. "ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis."
    Towler P., Staker B., Prasad S.G., Menon S., Tang J., Parsons T., Ryan D., Fisher M., Williams D., Dales N.A., Patane M.A., Pantoliano M.W.
    J. Biol. Chem. 279:17996-18007(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 19-615, X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-615 IN COMPLEX WITH MLN-4760, DISULFIDE BONDS, GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546.

Entry informationi

Entry nameiACE2_HUMAN
AccessioniPrimary (citable) accession number: Q9BYF1
Secondary accession number(s): C7ECU1
, Q6UWP0, Q86WT0, Q9NRA7, Q9UFZ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2005
Last sequence update: August 2, 2005
Last modified: November 26, 2014
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3