SubmitCancel

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, UNQ868/PRO1885
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

Binds 1 zinc ion per subunit.1 Publication
Binds 1 chloride ion per subunit.1 Publication

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 II
  3. KM=6.8 µM for apelin-13
  4. KM=5.5 µM for dynorphin-13

pH dependencei

Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9.

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. protein binding Source: UniProtKB
  6. virus receptor activity Source: UniProtKB
  7. 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

Chain Processed angiotensin-converting enzyme 2 : Secreted 3 Publications
Cell membrane; Single-pass type I membrane protein 3 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini18 – 740723Extracellular Reviewed predictionAdd
BLAST
Transmembranei741 – 76121Helical; Reviewed predictionAdd
BLAST
Topological domaini762 – 80544Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

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

Organism-specific databases

PharmGKBiPA425.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717 Reviewed predictionAdd
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...) Inferred
Glycosylationi90 – 901N-linked (GlcNAc...)2 Publications
Glycosylationi103 – 1031N-linked (GlcNAc...)1 Publication
Disulfide bondi133 ↔ 1411 Publication
Glycosylationi322 – 3221N-linked (GlcNAc...) Inferred
Disulfide bondi344 ↔ 3611 Publication
Glycosylationi432 – 4321N-linked (GlcNAc...)1 Publication
Disulfide bondi530 ↔ 5421 Publication
Glycosylationi546 – 5461N-linked (GlcNAc...)2 Publications
Glycosylationi690 – 6901N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

N-glycosylation on Asn-90 may limit SARS infectivity.
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.6 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 TMPRSS2.6 Publications

Protein-protein interaction databases

BioGridi121864. 3 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 – 5230
Helixi56 – 7722
Turni78 – 825
Helixi85 – 873
Helixi91 – 10010
Helixi104 – 1074
Helixi110 – 12920
Beta strandi131 – 1344
Beta strandi137 – 1437
Turni144 – 1463
Helixi148 – 1547
Helixi158 – 17114
Helixi173 – 19321
Beta strandi196 – 1983
Helixi199 – 2046
Turni205 – 2073
Turni213 – 2153
Helixi220 – 25132
Turni253 – 2553
Beta strandi258 – 2603
Helixi264 – 2663
Beta strandi267 – 2715
Helixi276 – 2783
Helixi279 – 2824
Turni284 – 2874
Turni294 – 2974
Helixi298 – 3003
Helixi304 – 31613
Turni317 – 3193
Helixi327 – 3304
Beta strandi338 – 3403
Beta strandi347 – 3526
Beta strandi355 – 3595
Helixi366 – 38419
Turni385 – 3873
Helixi390 – 3923
Helixi400 – 41314
Helixi415 – 4206
Turni422 – 4265
Helixi432 – 44615
Helixi449 – 46517
Beta strandi466 – 4683
Helixi470 – 4723
Helixi473 – 48311
Beta strandi486 – 4883
Helixi499 – 5024
Helixi504 – 5074
Helixi514 – 53118
Turni532 – 5343
Helixi539 – 5413
Helixi548 – 55811
Turni559 – 5624
Helixi566 – 5749
Beta strandi575 – 5784
Helixi582 – 59817
Beta strandi600 – 6023
Beta strandi607 – 6093

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.

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.

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG71044.
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

MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY    50
NTNITEENVQ NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL 100
QQNGSSVLSE DKSKRLNTIL NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE 150
IMANSLDYNE RLWAWESWRS EVGKQLRPLY EEYVVLKNEM ARANHYEDYG 200
DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL HAYVRAKLMN 250
AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 300
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD 350
LGKGDFRILM CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF 400
HEAVGEIMSL SAATPKHLKS IGLLSPDFQE DNETEINFLL KQALTIVGTL 450
PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM KREIVGVVEP VPHDETYCDP 500
ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH KCDISNSTEA 550
GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK 600
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA 650
MRQYFLKVKN QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV 700
EKAIRMSRSR INDAFRLNDN SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM 750
GVIVVGIVIL IFTGIRDRKK KNKARSGENP YASIDISKGE NNPGFQNTDD 800
VQTSF 805
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

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. VSP_014901
Alternative sequencei556 – 805250Missing in isoform 2. VSP_014902Add
BLAST

Sequence conflict

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
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. 3 interactions.
DIPi DIP-44689N.
IntActi Q9BYF1. 1 interaction.
MINTi MINT-4538816.
STRINGi 9606.ENSP00000252519.

Chemistry

BindingDBi Q9BYF1.
ChEMBLi CHEMBL2096989.
DrugBanki 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 GC0XM015489.
HGNCi HGNC:13557. ACE2.
HPAi CAB026174.
HPA000288.
MIMi 300335. gene.
neXtProti NX_Q9BYF1.
PharmGKBi PA425.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG71044.
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: September 3, 2014
This is version 130 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

Similar proteinsi