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UniProtKB/Swiss-Prot entry Q9BYF1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACE2_HUMAN
Primary accession number Q9BYF1
Secondary accession numbers Q6UWP0 Q86WT0 Q9NRA7 Q9UFZ6
Integrated into Swiss-Prot on August 2, 2005
Sequence was last modified on August 2, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 60)
Name and origin of the protein
Protein name Angiotensin-converting enzyme 2 [Precursor]
Synonyms EC 3.4.17.-
ACE-related carboxypeptidase
Angiotensin-converting enzyme homolog
ACEH
Contains Processed angiotensin-converting enzyme 2
Gene name
Name: ACE2
ORFNames: UNQ868/PRO1885
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION, AND ENZYME REGULATION.
TISSUE=Heart;
PubMed=10969042 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A novel angiotensin-converting enzyme-related carboxypeptidase (ACE2) converts angiotensin I to angiotensin 1-9.";
Circ. Res. 87:E1-E9(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, GLYCOSYLATION, FUNCTION, AND ENZYME REGULATION.
TISSUE=Lymphoma;
DOI=10.1074/jbc.M002615200; PubMed=10924499 [NCBI, ExPASy, EBI, Israel, Japan]
Tipnis S.R., Hooper N.M., Hyde R., Karran E., Christie G., Turner A.J.;
"A human homolog of angiotensin-converting enzyme. Cloning and functional expression as a captopril-insensitive carboxypeptidase.";
J. Biol. Chem. 275:33238-33243(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
TISSUE=Testis;
DOI=10.1210/en.2004-0443; PubMed=15231706 [NCBI, ExPASy, EBI, Israel, Japan]
Douglas G.C., O'Bryan M.K., Hedger M.P., Lee D.K.L., Yarski M.A., Smith A.I., Lew R.A.;
"The novel angiotensin-converting enzyme (ACE) homolog, ACE2, is selectively expressed by adult Leydig cells of the testis.";
Endocrinology 145:4703-4711(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT SER-638.
TISSUE=Lung, and Testis;
DOI=10.1002/ajmg.a.30779; PubMed=15937940 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Am. J. Med. Genet. A 136:52-57(2005).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Suzuki Y., Watanabe M., Sugano S.;
"Cloning, expression analysis and chromosomal localization of a novel ACE like enzyme.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
DOI=10.1101/gr.1293003; PubMed=12975309 [NCBI, ExPASy, EBI, Israel, Japan]
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND VARIANT ARG-26.
SeattleSNPs program for genomic applications;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-805 (ISOFORM 1).
TISSUE=Testis;
The German cDNA consortium;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[10]
PROTEIN SEQUENCE OF 679-689, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH ITGB1.
DOI=10.1016/j.bbadis.2004.05.005; PubMed=15276642 [NCBI, ExPASy, EBI, Israel, Japan]
Lin Q., Keller R.S., Weaver B., Zisman L.S.;
"Interaction of ACE2 and integrin beta1 in failing human heart.";
Biochim. Biophys. Acta 1689:175-178(2004).
[11]
TISSUE SPECIFICITY.
DOI=10.1016/S0014-5793(02)03640-2; PubMed=12459472 [NCBI, ExPASy, EBI, Israel, Japan]
Harmer D., Gilbert M., Borman R., Clark K.L.;
"Quantitative mRNA expression profiling of ACE 2, a novel homologue of angiotensin converting enzyme.";
FEBS Lett. 532:107-110(2002).
[12]
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND COFACTOR.
DOI=10.1074/jbc.M200581200; PubMed=11815627 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Hydrolysis of biological peptides by human angiotensin-converting enzyme-related carboxypeptidase.";
J. Biol. Chem. 277:14838-14843(2002).
[13]
FUNCTION, INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
DOI=10.1038/nature02145; PubMed=14647384 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus.";
Nature 426:450-454(2003).
[14]
INDUCTION.
DOI=10.1186/1741-7015-2-19; PubMed=15151696 [NCBI, ExPASy, EBI, Israel, Japan]
Goulter A.B., Goddard M.J., Allen J.C., Clark K.L.;
"ACE2 gene expression is up-regulated in the human failing heart.";
BMC Med. 2:19-19(2004).
[15]
TISSUE SPECIFICITY.
DOI=10.1002/path.1570; PubMed=15141377 [NCBI, ExPASy, EBI, Israel, Japan]
Hamming I., Timens W., Bulthuis M.L.C., Lely A.T., Navis G.J., van Goor H.;
"Tissue distribution of ACE2 protein, the functional receptor for SARS coronavirus. A first step in understanding SARS pathogenesis.";
J. Pathol. 203:631-637(2004).
[16]
INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN.
DOI=10.1128/JVI.78.20.11429-11433.2004; PubMed=15452268 [NCBI, ExPASy, EBI, Israel, Japan]
Li W., Greenough T.C., Moore M.J., Vasilieva N., Somasundaran M., Sullivan J.L., Farzan M., Choe H.;
"Efficient replication of severe acute respiratory syndrome coronavirus in mouse cells is limited by murine angiotensin-converting enzyme 2.";
J. Virol. 78:11429-11433(2004).
[17]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-90, AND MASS SPECTROMETRY.
TISSUE=Bile;
DOI=10.1074/mcp.M400015-MCP200; PubMed=15084671 [NCBI, ExPASy, EBI, Israel, Japan]
Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H., Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.;
"A proteomic analysis of human bile.";
Mol. Cell. Proteomics 3:715-728(2004).
[18]
TISSUE SPECIFICITY, AND INDUCTION.
DOI=10.1093/eurheartj/ehi114; PubMed=15671045 [NCBI, ExPASy, EBI, Israel, Japan]
Burrell L.M., Risvanis J., Kubota E., Dean R.G., MacDonald P.S., Lu S., Tikellis C., Grant S.L., Lew R.A., Smith A.I., Cooper M.E., Johnston C.I.;
"Myocardial infarction increases ACE2 expression in rat and humans.";
Eur. Heart J. 26:369-375(2005).
[19]
INTERACTION WITH SARS-COV SPIKE GLYCOPROTEIN, AND MUTAGENESIS.
DOI=10.1038/sj.emboj.7600640; PubMed=15791205 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Receptor and viral determinants of SARS-coronavirus adaptation to human ACE2.";
EMBO J. 24:1634-1643(2005).
[20]
PROTEOLYTIC CLEAVAGE.
DOI=10.1074/jbc.M505111200; PubMed=15983030 [NCBI, ExPASy, EBI, Israel, Japan]
Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., Hooper N.M., Turner A.J.;
"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).";
J. Biol. Chem. 280:30113-30119(2005).
[21]
INTERACTION WITH HCOV-NL63 SPIKE GLYCOPROTEIN.
DOI=10.1073/pnas.0409465102; PubMed=15897467 [NCBI, ExPASy, EBI, Israel, Japan]
Hofmann H., Pyrc K., van der Hoek L., Geier M., Berkhout B., Poehlmann S.;
"Human coronavirus NL63 employs the severe acute respiratory syndrome coronavirus receptor for cellular entry.";
Proc. Natl. Acad. Sci. U.S.A. 102:7988-7993(2005).
[22]
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, AND GLYCOSYLATION AT ASN-53; ASN-90; ASN-103; ASN-322; ASN-432 AND ASN-546.
DOI=10.1074/jbc.M311191200; PubMed=14754895 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ACE2 X-ray structures reveal a large hinge-bending motion important for inhibitor binding and catalysis.";
J. Biol. Chem. 279:17996-18007(2004).
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. In case of human coronaviruses SARS and HCoV-NL63 infections, serve as functional receptor for the spike glycoprotein of both coronaviruses.
  • COFACTOR: Binds 1 zinc ion per subunit.
  • COFACTOR: Binds 1 chloride ion per subunit.
  • ENZYME REGULATION: 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.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=6.9 µM for angiotensin I;
    KM=2 µM for angiotensin II;
    KM=6.8 µM for apelin-13;
    KM=5.5 µM for dynorphin-13;
    pH dependence:   Optimum pH is 6.5 in the presence of 1 M NaCl. Active from pH 6 to 9;
  • SUBUNIT: Interacts with ITGB1. Interacts with SARS-CoV and HCoV-NL63 spike glycoprotein.
  • SUBCELLULAR LOCATION: Processed angiotensin-converting enzyme 2: Secreted.
  • SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDQ9BYF1-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDQ9BYF1-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_014901, VSP_014902.
  • TISSUE SPECIFICITY: 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.
  • INDUCTION: Up-regulated in failing heart.
  • PTM: N-glycosylation on Asn-90 may limit SARS infectivity.
  • SIMILARITY: Belongs to the peptidase M2 family [view classification].
  • WEB RESOURCE: Name=SeattleSNPs; URL="http://pga.gs.washington.edu/data/ace2/";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF291820; AAF99721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF241254; AAF78220.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY623811; AAT45083.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB193259; BAD99266.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB193260; BAD99267.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB046569; BAB40370.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY358714; AAQ89076.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY217547; AAO25651.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039902; AAH39902.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC048094; AAH48094.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL110224; CAB53682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T14762; T14762.
RefSeq NP_068576.1; -.
UniGene Hs.178098
3D structure databases
PDB
1R42; X-ray; 2.20 A; A=1-615.[ExPASy / RCSB / EBI]
1R4L; X-ray; 3.00 A; A=1-615.[ExPASy / RCSB / EBI]
1XJP; Model; -; B=19-615.[ExPASy / RCSB / EBI]
2AJF; X-ray; 2.90 A; A/B=19-615.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1R42; -.
1R4L; -.
1XJP; -.
2AJF; -.
ModBase Q9BYF1.
Protein family/group databases
MEROPS M02.006; -.
PTM databases
PhosphoSite Q9BYF1; -.
Organism-specific databases
H-InvDB HIX0016670; -.
HGNC HGNC:13557; ACE2.
GenAtlas ACE2.
HPA HPA000288; -.
MIM 300335; gene. [NCBI / EBI]
PharmGKB PA425; -.
GeneCards Q9BYF1.
Gene expression databases
ArrayExpress Q9BYF1; -.
CleanEx HS_ACE2; -.
GermOnline ENSG00000130234; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005615; Cellular component: extracellular space (inferred from direct assay from UniProtKB).
GO:0045121; Cellular component: membrane raft (traceable author statement from UniProtKB).
GO:0004180; Molecular function: carboxypeptidase activity (inferred from direct assay from UniProtKB).
GO:0001948; Molecular function: glycoprotein binding (inferred from physical interaction from UniProtKB).
GO:0001618; Molecular function: viral receptor activity (inferred from direct assay from UniProtKB).
GO:0008270; Molecular function: zinc ion binding (traceable author statement from UniProtKB).
GO:0002005; Biological process: angiotensin catabolic process in blood (inferred by curator from UniProtKB).
GO:0003051; Biological process: angiotensin-mediated drinking behavior (inferred from mutant phenotype from UniProtKB).
GO:0006800; Biological process: oxygen and reactive oxygen species metabolic process (inferred by curator from UniProtKB).
GO:0032800; Biological process: receptor biosynthetic process (inferred from mutant phenotype from UniProtKB).
GO:0042127; Biological process: regulation of cell proliferation (traceable author statement from UniProtKB).
GO:0001817; Biological process: regulation of cytokine production (inferred by curator from UniProtKB).
GO:0050727; Biological process: regulation of inflammatory response (inferred by curator from UniProtKB).
GO:0019229; Biological process: regulation of vasoconstriction (inferred by curator from UniProtKB).
GO:0042312; Biological process: regulation of vasodilation (inferred by curator from UniProtKB).
GO:0046813; Biological process: virion attachment, binding of host cell surface receptor (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR006025; Pept_M_Zn_BS.
IPR001548; Peptidase_M2.
Graphical view of domain structure.
PANTHER PTHR10514; Peptidase_M2; 1.
Pfam PF01401; Peptidase_M2; 1.
Pfam graphical view of domain structure.
PRINTS PR00791; PEPDIPTASEA.
ProDom PD004184; Peptidase_M2; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00142; ZINC_PROTEASE; 1.
BLOCKS Q9BYF1.
Genome annotation databases
Ensembl ENSG00000130234; Homo sapiens. [Contig view]
GeneID 59272; -.
KEGG hsa:59272; -.
Phylogenomic databases
HOGENOM Q9BYF1; -.
HOVERGEN Q9BYF1; -.
Other
DrugBank DB00691; Moexipril.
SOURCE ACE2; Homo sapiens.
ProtoNet Q9BYF1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane; Chloride; Direct protein sequencing; Glycoprotein; Host-virus interaction; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Secreted; Signal; Transmembrane; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    17  17     Potential. 
CHAIN   18   805  788     Angiotensin-converting enzyme 2. PRO_0000028570
CHAIN   18     ?        Processed angiotensin-converting enzyme 2. PRO_0000292268
TOPO_DOM   18   740  723     Extracellular (Potential). 
TRANSMEM   741   761  21     Potential. 
TOPO_DOM   762   805  44     Cytoplasmic (Potential). 
REGION   30    41  12     Interaction with SARS-CoV spike glycoprotein. 
REGION   82    84  3     Interaction with SARS-CoV spike glycoprotein. 
REGION   353   357  5     Interaction with SARS-CoV spike glycoprotein. 
ACT_SITE   375   375         
ACT_SITE   505   505         
METAL   374   374        Zinc; catalytic. 
METAL   378   378        Zinc; catalytic. 
METAL   402   402        Zinc; catalytic. 
BINDING   169   169        Chloride. 
BINDING   273   273        Substrate. 
BINDING   345   345        Substrate. 
BINDING   346   346        Substrate; via carbonyl oxygen. 
BINDING   371   371        Substrate. 
BINDING   477   477        Chloride. 
BINDING   481   481        Chloride. 
BINDING   515   515        Substrate. 
CARBOHYD   53    53        N-linked (GlcNAc...) (Probable). 
CARBOHYD   90    90        N-linked (GlcNAc...). 
CARBOHYD   103   103        N-linked (GlcNAc...). 
CARBOHYD   322   322        N-linked (GlcNAc...) (Probable). 
CARBOHYD   432   432        N-linked (GlcNAc...). 
CARBOHYD   546   546        N-linked (GlcNAc...). 
CARBOHYD   690   690        N-linked (GlcNAc...) (Potential). 
DISULFID   133   141         
DISULFID   344   361         
DISULFID   530   542         
VAR_SEQ   555   555        F -> L (in isoform 2). VSP_014901
VAR_SEQ   556   805        Missing (in isoform 2). VSP_014902
VARIANT   26    26  1     K -> R (in dbSNP:rs4646116 [NCBI]). VAR_023082 [3D]
VARIANT   638   638  1     N -> S. VAR_023083 
MUTAGEN   24    26        QAK->KAE: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   31    31        K->D: Abolishes interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   37    37        E->A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   38    38        D->A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   41    41        Y->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   68    68        K->D: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   82    84        MYP->NFS: Inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   110   110        E->P: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   135   136        PD->SM: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   160   160        E->R: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   192   192        R->D: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   219   219        R->D: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   239   239        H->Q: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   309   309        K->D: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   312   312        E->A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   324   324        T->A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   338   340        NVQ->DDR: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   350   350        D->A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   353   353        K->H,A,D: Abolishes interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   355   355        D->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   357   357        R->A: Strongly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   359   359        L->K,A: No effect on interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   383   383        M->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   389   389        P->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein. 
MUTAGEN   393   393        R->A: Slightly inhibits interaction with SARS-CoV spike glycoprotein.