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Q56NL1 (ACE2_PAGLA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 31, 2012. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Angiotensin-converting enzyme 2
EC=3.4.17.23
Alternative name(s):
ACE-related carboxypeptidase

Cleaved into the following chain:

  1. Processed angiotensin-converting enzyme 2
Gene names
Name:ACE2
OrganismPaguma larvata (Masked palm civet)
Taxonomic identifier9675 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Carnivora › Feliformia › Viverridae › Paradoxurinae › Paguma

Protein attributes

Sequence length805 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity. Functional receptor for human coronavirus SARS.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit.

Binds 1 chloride ion per subunit.

Subunit structure

Interacts with SARS-CoV S protein. Ref.1

Subcellular location

Processed angiotensin-converting enzyme 2: Secreted By similarity.

Cell membrane; Single-pass type I membrane protein By similarity.

Post-translational modification

Proteolytic cleavage by ADAM17 generates a secreted form By similarity.

Sequence similarities

Belongs to the peptidase M2 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 805788Angiotensin-converting enzyme 2
PRO_0000028572
Chain18 – 708691Processed angiotensin-converting enzyme 2
PRO_0000292270

Regions

Topological domain18 – 740723Extracellular Potential
Transmembrane741 – 76121Helical; Potential
Topological domain762 – 80544Cytoplasmic Potential
Region30 – 4112Interaction with SARS S protein
Region82 – 843Interaction with SARS S protein By similarity
Region90 – 934Interaction with SARS S protein
Region353 – 3575Interaction with SARS S protein By similarity

Sites

Active site3751 By similarity
Active site5051 By similarity
Metal binding3741Zinc; catalytic
Metal binding3781Zinc; catalytic
Metal binding4021Zinc; catalytic
Binding site1691Chloride By similarity
Binding site2731Substrate By similarity
Binding site3451Substrate By similarity
Binding site3461Substrate; via carbonyl oxygen By similarity
Binding site3711Substrate By similarity
Binding site4771Chloride By similarity
Binding site4811Chloride By similarity
Binding site5151Substrate By similarity

Amino acid modifications

Glycosylation531N-linked (GlcNAc...) Potential
Glycosylation2161N-linked (GlcNAc...) Potential
Glycosylation3221N-linked (GlcNAc...) Potential
Glycosylation5461N-linked (GlcNAc...) Potential
Glycosylation6601N-linked (GlcNAc...) Potential
Glycosylation6901N-linked (GlcNAc...) Potential
Disulfide bond133 ↔ 141 Ref.2
Disulfide bond344 ↔ 361 Ref.2
Disulfide bond530 ↔ 542 Ref.2

Secondary structure

1 .............................................................................................. 805
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q56NL1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: CF6406851F73E378

FASTA80592,611
        10         20         30         40         50         60 
MSGSFWLLLS FAALTAAQST TEELAKTFLE TFNYEAQELS YQSSVASWNY NTNITDENAK 

        70         80         90        100        110        120 
NMNEAGAKWS AYYEEQSKLA QTYPLAEIQD AKIKRQLQAL QQSGSSVLSA DKSQRLNTIL 

       130        140        150        160        170        180 
NAMSTIYSTG KACNPNNPQE CLLLEPGLDN IMENSKDYNE RLWAWEGWRA EVGKQLRPLY 

       190        200        210        220        230        240 
EEYVALKNEM ARANNYEDYG DYWRGDYEEE WTGGYNYSRN QLIQDVEDTF EQIKPLYQHL 

       250        260        270        280        290        300 
HAYVRAKLMD TYPSRISRTG CLPAHLLGDM WGRFWTNLYP LTVPFGQKPN IDVTDAMVNQ 

       310        320        330        340        350        360 
NWDARRIFKE AEKFFVSVGL PNMTQGFWEN SMLTEPGDGR KVVCHPTAWD LGKGDFRIKM 

       370        380        390        400        410        420 
CTKVTMDDFL TAHHEMGHIQ YDMAYAAQPF LLRNGANEGF HEAVGEIMSL SAATPNHLKT 

       430        440        450        460        470        480 
IGLLSPAFSE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGAIPK EQWMQKWWEM 

       490        500        510        520        530        540 
KRNIVGVVEP VPHDETYCDP ASLFHVANDY SFIRYYTRTI YQFQFQEALC QIAKHEGPLH 

       550        560        570        580        590        600 
KCDISNSTEA GKKLLEMLSL GRSEPWTLAL ERVVGAKNMN VTPLLNYFEP LFTWLKEQNR 

       610        620        630        640        650        660 
NSFVGWDTDW RPYSDQSIKV RISLKSALGE KAYEWNDNEM YLFRSSIAYA MREYFSKVKN 

       670        680        690        700        710        720 
QTIPFVEDNV WVSDLKPRIS FNFFVTFSNN VSDVIPRSEV EDAIRMSRSR INDAFRLDDN 

       730        740        750        760        770        780 
SLEFLGIEPT LSPPYRPPVT IWLIVFGVVM GAIVVGIVLL IVSGIRNRRK NDQAGSEENP 

       790        800 
YASVDLNKGE NNPGFQHADD VQTSF

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References

[1]"Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2."
Li W., Zhang C., Sui J., Kuhn J.H., Moore M.J., Luo S., Wong S.-K., Huang I.-C., Xu K., Vasilieva N., Murakami A., He Y., Marasco W.A., Guan Y., Choe H., Farzan M.
EMBO J. 24:1634-1643(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SARS-COV S PROTEIN.
[2]"Mechanisms of host receptor adaptation by severe acute respiratory syndrome coronavirus."
Wu K., Peng G., Wilken M., Geraghty R.J., Li F.
J. Biol. Chem. 287:8904-8911(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 19-613, ZINC-BINDING SITES, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY881174 mRNA. Translation: AAX63775.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3D0GX-ray2.80A/B19-55[»]
3D0HX-ray3.10A/B19-55[»]
3D0IX-ray2.90A/B19-55[»]
3SCKX-ray3.00A/B19-613[»]
3SCLX-ray3.00A/B19-613[»]
ProteinModelPortalQ56NL1.
SMRQ56NL1. Positions 19-615.
ModBaseSearch...

Protein family/group databases

MEROPSM02.006.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000265.

Family and domain databases

InterProIPR001548. Peptidase_M2.
[Graphical view]
PANTHERPTHR10514. PTHR10514. 1 hit.
PfamPF01401. Peptidase_M2. 1 hit.
[Graphical view]
PRINTSPR00791. PEPDIPTASEA.
PROSITEPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ56NL1.

Entry information

Entry nameACE2_PAGLA
AccessionPrimary (citable) accession number: Q56NL1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: May 10, 2005
Last modified: October 31, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents