[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], AND VARIANT ARG-26. SeattleSNPs variation discovery resource; 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; DOI=10.1186/1471-2164-8-399; PubMed=17974005 [NCBI, ExPASy, EBI, Israel, Japan] Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I.; "The full-ORF clone resource of the German cDNA consortium."; BMC Genomics 8:399-399(2007).
[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]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-546, AND MASS SPECTROMETRY. TISSUE=Liver; DOI=10.1021/pr8008012; PubMed=19159218 [NCBI, ExPASy, EBI, Israel, Japan] Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."; J. Proteome Res. 8:651-661(2009).
[23]	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:	K_M=6.9 µM for angiotensin I;
	K_M=2 µM for angiotensin II;
	K_M=6.8 µM for apelin-13;
	K_M=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.

Name	1
Isoform ID	Q9BYF1-1
This is the isoform sequence displayed in this entry.

Name	2
Isoform ID	Q9BYF1-2
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]

IPI

IPI00465187; -.
IPI00619939; -.

T14762; T14762.

NP_068576.1; -.

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]
3D0G; X-ray; 2.80 A; A/B=19-615.	[ExPASy / RCSB / EBI]
3D0H; X-ray; 3.10 A; A/B=19-615.	[ExPASy / RCSB / EBI]
3D0I; X-ray; 2.90 A; A/B=19-615.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1R42; -.
1R4L; -.
1XJP; -.
2AJF; -.
3D0G; -.
3D0H; -.
3D0I; -.

ModBase

Q9BYF1.

Protein family/group databases

MEROPS

M02.006; -.

PTM databases

PhosphoSite

Q9BYF1; -.

Organism-specific databases

GC0XM015489; -.

HIX0016670; -.

HGNC:13557; ACE2.

HPA000288; -.

300335; gene. [NCBI / EBI]

PharmGKB

PA425; -.

Gene expression databases

Q9BYF1; -.

Q9BYF1; -.

HS_ACE2; -.

ENSG00000130234; Homo sapiens.

Ontologies

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:0016021;	Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0045121;	Cellular component: membrane raft (traceable author statement from UniProtKB).
GO:0005634;	Cellular component: nucleus (inferred from direct assay from HPA).
GO:0005886;	Cellular component: plasma membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004180;	Molecular function: carboxypeptidase activity (inferred from direct assay from UniProtKB).
GO:0031404;	Molecular function: chloride ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0001948;	Molecular function: glycoprotein binding (inferred from physical interaction from UniProtKB).
GO:0008237;	Molecular function: metallopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0008241;	Molecular function: peptidyl-dipeptidase activity (inferred from electronic annotation from InterPro).
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:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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.

Proteomic databases

PRIDE

Q9BYF1; -.

Genome annotation databases

Ensembl

ENSG00000130234; Homo sapiens. [Contig view]

GeneID

59272; -.

KEGG

hsa:59272; -.

Phylogenomic databases

HOGENOM

Q9BYF1; -.

HOVERGEN

Q9BYF1; -.

OMA

Q9BYF1; IYQFQFQ.

Other

DB00691; Moexipril.

65154; -.

Q9BYF1; -.

ACE2; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Carboxypeptidase; Cell membrane; Chloride; Direct protein sequencing; Disulfide bond; Glycoprotein; Host-virus interaction; Hydrolase; Membrane; Metal-binding; Metalloprotease; Polymorphism; Protease; Secreted; Signal; Transmembrane; Zinc.

Features

Feature table viewer

Feature aligner

`Key`	`From 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.`
`MUTAGEN`	`425 427`		`SPD->PSN: Slightly inhibits interaction with SARS-CoV spike glycoprotein.`
`MUTAGEN`	`465 467`		`KGE->QDK: No effect on interaction with SARS-CoV spike glycoprotein.`
`MUTAGEN`	`559 559`		`R->S: Slightly inhibits interaction with SARS-CoV spike glycoprotein.`
`MUTAGEN`	`603 603`		`F->T: No effect on interaction with SARS-CoV spike glycoprotein.`
`CONFLICT`	`18 18`		`Q -> H (in Ref. 9; CAB53682).`
`CONFLICT`	`508 508`		`N -> D (in Ref. 6; AAQ89076).`
`CONFLICT`	`631 631`		`K -> R (in Ref. 5; BAB40370).`
`HELIX`	`23 52`	`30`
`HELIX`	`56 77`	`22`
`TURN`	`78 82`	`5`
`HELIX`	`91 100`	`10`
`HELIX`	`104 107`	`4`
`HELIX`	`110 129`	`20`
`STRAND`	`131 134`	`4`
`STRAND`	`137 143`	`7`
`TURN`	`144 146`	`3`
`HELIX`	`148 154`	`7`
`HELIX`	`158 171`	`14`
`HELIX`	`173 193`	`21`
`HELIX`	`199 204`	`6`
`TURN`	`205 207`	`3`
`TURN`	`213 215`	`3`
`HELIX`	`220 251`	`32`
`TURN`	`253 255`	`3`
`HELIX`	`264 266`	`3`
`STRAND`	`267 271`	`5`
`HELIX`	`276 278`	`3`
`HELIX`	`279 282`	`4`
`TURN`	`284 287`	`4`
`TURN`	`294 297`	`4`
`HELIX`	`298 300`	`3`
`HELIX`	`304 316`	`13`
`TURN`	`317 319`	`3`
`HELIX`	`327 330`	`4`
`STRAND`	`347 352`	`6`
`STRAND`	`355 359`	`5`
`HELIX`	`366 384`	`19`
`TURN`	`385 387`	`3`
`HELIX`	`390 392`	`3`
`HELIX`	`400 413`	`14`
`HELIX`	`415 420`	`6`
`HELIX`	`432 446`	`15`
`HELIX`	`449 465`	`17`
`HELIX`	`470 472`	`3`
`HELIX`	`473 483`	`11`
`HELIX`	`499 502`	`4`
`HELIX`	`504 507`	`4`
`HELIX`	`514 531`	`18`
`TURN`	`532 534`	`3`
`HELIX`	`539 541`	`3`
`HELIX`	`548 558`	`11`
`TURN`	`559 562`	`4`
`HELIX`	`566 574`	`9`
`STRAND`	`575 578`	`4`
`HELIX`	`582 598`	`17`
`STRAND`	`600 602`	`3`
`STRAND`	`607 609`	`3`

Sequence information

Length: 805 AA [This is the length of the unprocessed precursor]

Molecular weight: 92463 Da [This is the MW of the unprocessed precursor]

CRC64: 8EE6EB0A931550E8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSSSSWLLLS LVAVTAAQST IEEQAKTFLD KFNHEAEDLF YQSSLASWNY NTNITEENVQ 

        70         80         90        100        110        120 
NMNNAGDKWS AFLKEQSTLA QMYPLQEIQN LTVKLQLQAL QQNGSSVLSE DKSKRLNTIL 

       130        140        150        160        170        180 
NTMSTIYSTG KVCNPDNPQE CLLLEPGLNE IMANSLDYNE RLWAWESWRS EVGKQLRPLY 

       190        200        210        220        230        240 
EEYVVLKNEM ARANHYEDYG DYWRGDYEVN GVDGYDYSRG QLIEDVEHTF EEIKPLYEHL 

       250        260        270        280        290        300 
HAYVRAKLMN AYPSYISPIG CLPAHLLGDM WGRFWTNLYS LTVPFGQKPN IDVTDAMVDQ 

       310        320        330        340        350        360 
AWDAQRIFKE AEKFFVSVGL PNMTQGFWEN SMLTDPGNVQ KAVCHPTAWD LGKGDFRILM 

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

       430        440        450        460        470        480 
IGLLSPDFQE DNETEINFLL KQALTIVGTL PFTYMLEKWR WMVFKGEIPK DQWMKKWWEM 

       490        500        510        520        530        540 
KREIVGVVEP VPHDETYCDP ASLFHVSNDY SFIRYYTRTL YQFQFQEALC QAAKHEGPLH 

       550        560        570        580        590        600 
KCDISNSTEA GQKLFNMLRL GKSEPWTLAL ENVVGAKNMN VRPLLNYFEP LFTWLKDQNK 

       610        620        630        640        650        660 
NSFVGWSTDW SPYADQSIKV RISLKSALGD KAYEWNDNEM YLFRSSVAYA MRQYFLKVKN 

       670        680        690        700        710        720 
QMILFGEEDV RVANLKPRIS FNFFVTAPKN VSDIIPRTEV EKAIRMSRSR INDAFRLNDN 

       730        740        750        760        770        780 
SLEFLGIQPT LGPPNQPPVS IWLIVFGVVM GVIVVGIVIL IFTGIRDRKK KNKARSGENP 

       790        800 
YASIDISKGE NNPGFQNTDD VQTSF

Q9BYF1 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools