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Protein

Spike glycoprotein

Gene

S

Organism
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 and CLEC4M/DC-SIGNR receptors and internalization of the virus into the endosomes of the host cell induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.UniRule annotation2 Publications
Spike protein S2: mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model, the protein has at least three conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes.UniRule annotation
Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.UniRule annotation1 Publication

Miscellaneous

Tor2 is the prototype of the virus isolated during the severe SARS outbreak in 2002-2003. GD03 has been isolated from the second mild SARS outbreak in winter 2003-2004. SZ3 has been isolated from palm civet, the presumed animal reservoir. The spike proteins from those three isolates display a strong affinity for palm civet ACE2 receptor, whereas only the Tor2 spike protein efficiently binds human ACE2. This may explain the high pathogenicity of Tor2 virus, whose spike is highly adapted to the human host. Therefore, the lack of severity of disease during the 2003-2004 outbreak could be due to the incomplete adaptation of GD03 virus to bind human ACE2. Mutation Asn-479 and Thr-487 in palm civet coronavirus seems necessary and sufficient for the virus to acquire the ability to efficiently infect humans.

GO - Molecular functioni

  • host cell surface receptor binding Source: BHF-UCL
  • identical protein binding Source: IntAct

GO - Biological processi

Keywordsi

Biological processFusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Viral attachment to host cell, Viral penetration into host cytoplasm, Virulence, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Spike glycoproteinUniRule annotation
Short name:
S glycoproteinUniRule annotation
Alternative name(s):
E2UniRule annotation
Peplomer proteinUniRule annotation
Cleaved into the following 3 chains:
Spike protein S1UniRule annotation
Spike protein S2UniRule annotation
Spike protein S2'UniRule annotation
Gene namesi
Name:SUniRule annotation
ORF Names:2
OrganismiHuman SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
Taxonomic identifieri227859 [NCBI]
Taxonomic lineageiVirusesssRNA virusesssRNA positive-strand viruses, no DNA stageNidoviralesCoronaviridaeCoronavirinaeBetacoronavirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
Paguma larvata (Masked palm civet) [TaxID: 9675]
Proteomesi

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini14 – 1195ExtracellularUniRule annotationAdd BLAST1182
Transmembranei1196 – 1216HelicalUniRule annotationAdd BLAST21
Topological domaini1217 – 1255CytoplasmicUniRule annotationAdd BLAST39

GO - Cellular componenti

Keywords - Cellular componenti

Host cell membrane, Host membrane, Membrane, Viral envelope protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi323C → A: No effect on human ACE2 binding in vitro. 1 Publication1
Mutagenesisi348C → A: Complete loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi452E → A: 90% loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi454D → A: Complete loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi463D → A: Partial loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi467C → A: Complete loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi474C → A: Complete loss of human ACE2 binding in vitro. 1 Publication1
Mutagenesisi480D → A: No effect on human ACE2 binding in vitro. 1 Publication1
Mutagenesisi667R → S: 40% loss of cell-cell fusion. 1 Publication1
Mutagenesisi672K → S: No effect on cell-cell fusion. 1 Publication1
Mutagenesisi797R → N: Complete loss of trypsin-induced membrane fusion. 1 Publication1
Mutagenesisi1251K → A: Decrease in Golgi localization, and complete loss of COPI binding; when associated with A-1253. 1 Publication1
Mutagenesisi1253H → A: Decrease in Golgi localization, and complete loss of COPI binding; when associated with A-1251. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 13UniRule annotationAdd BLAST13
ChainiPRO_000003720814 – 1255Spike glycoproteinAdd BLAST1242
ChainiPRO_000003720914 – 667Spike protein S1UniRule annotationAdd BLAST654
ChainiPRO_0000037210668 – 1255Spike protein S2UniRule annotationAdd BLAST588
ChainiPRO_0000444082798 – 1255Spike protein S2'UniRule annotationAdd BLAST458

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi65N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi73N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi109N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi118N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi119N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi158N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi227N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi269N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi318N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi323 ↔ 348UniRule annotation
Glycosylationi330N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi357N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Disulfide bondi366 ↔ 419UniRule annotation
Disulfide bondi467 ↔ 474
Glycosylationi589N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi602N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi691N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi699N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi783N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1056N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1080N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1116N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1140N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1155N-linked (GlcNAc...) asparagine; by hostUniRule annotation1
Glycosylationi1176N-linked (GlcNAc...) asparagine; by hostUniRule annotation1

Post-translational modificationi

The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested by cathepsin CTSL within endosomes.1 Publication
Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor.UniRule annotation
The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested within host endosomes.UniRule annotation

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei667 – 668CleavageUniRule annotation1 Publication2
Sitei797 – 798CleavageUniRule annotation1 Publication2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP59594

Interactioni

Subunit structurei

Homotrimer; each monomer consists of a S1 and a S2 subunit. The resulting peplomers protrude from the virus surface as spikes (By similarity). Binds to human and palm civet ACE2 and human CLEC4M/DC-SIGNR. Interacts with the accessory proteins 3a and 7a.UniRule annotation6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself9EBI-15582614,EBI-15582614

GO - Molecular functioni

Protein-protein interaction databases

DIPiDIP-29105N
IntActiP59594, 1 interactor

Structurei

Secondary structure

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliP59594
SMRiP59594
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59594

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni306 – 527Receptor-binding domainUniRule annotationAdd BLAST222
Regioni424 – 494Receptor-binding motif; binding to human ACE2Add BLAST71
Regioni770 – 788Fusion peptideUniRule annotationAdd BLAST19
Regioni902 – 952Heptad repeat 1UniRule annotationAdd BLAST51
Regioni1145 – 1184Heptad repeat 2UniRule annotationAdd BLAST40

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili931 – 975UniRule annotationAdd BLAST45
Coiled coili1157 – 1185UniRule annotationAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1251 – 1255KxHxxUniRule annotation5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1217 – 1236Cys-richAdd BLAST20

Domaini

The KxHxx motif seems to function as an ER retrieval and binds COPI in vitro.

Sequence similaritiesi

Belongs to the betacoronaviruses spike protein family.UniRule annotation

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

OrthoDBiVOG0900000Z

Family and domain databases

Gene3Di1.20.5.790, 1 hit
HAMAPiMF_04099 BETA_CORONA_SPIKE, 1 hit
InterProiView protein in InterPro
IPR002552 Corona_S2
IPR027400 S_HR2
IPR032500 Spike_N
IPR018548 Spike_rcpt-bd
IPR036326 Spike_rcpt-bd_sf
PfamiView protein in Pfam
PF01601 Corona_S2, 1 hit
PF16451 Spike_NTD, 1 hit
PF09408 Spike_rec_bind, 1 hit
SUPFAMiSSF143587 SSF143587, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P59594-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFIFLLFLTL TSGSDLDRCT TFDDVQAPNY TQHTSSMRGV YYPDEIFRSD
60 70 80 90 100
TLYLTQDLFL PFYSNVTGFH TINHTFGNPV IPFKDGIYFA ATEKSNVVRG
110 120 130 140 150
WVFGSTMNNK SQSVIIINNS TNVVIRACNF ELCDNPFFAV SKPMGTQTHT
160 170 180 190 200
MIFDNAFNCT FEYISDAFSL DVSEKSGNFK HLREFVFKNK DGFLYVYKGY
210 220 230 240 250
QPIDVVRDLP SGFNTLKPIF KLPLGINITN FRAILTAFSP AQDIWGTSAA
260 270 280 290 300
AYFVGYLKPT TFMLKYDENG TITDAVDCSQ NPLAELKCSV KSFEIDKGIY
310 320 330 340 350
QTSNFRVVPS GDVVRFPNIT NLCPFGEVFN ATKFPSVYAW ERKKISNCVA
360 370 380 390 400
DYSVLYNSTF FSTFKCYGVS ATKLNDLCFS NVYADSFVVK GDDVRQIAPG
410 420 430 440 450
QTGVIADYNY KLPDDFMGCV LAWNTRNIDA TSTGNYNYKY RYLRHGKLRP
460 470 480 490 500
FERDISNVPF SPDGKPCTPP ALNCYWPLND YGFYTTTGIG YQPYRVVVLS
510 520 530 540 550
FELLNAPATV CGPKLSTDLI KNQCVNFNFN GLTGTGVLTP SSKRFQPFQQ
560 570 580 590 600
FGRDVSDFTD SVRDPKTSEI LDISPCSFGG VSVITPGTNA SSEVAVLYQD
610 620 630 640 650
VNCTDVSTAI HADQLTPAWR IYSTGNNVFQ TQAGCLIGAE HVDTSYECDI
660 670 680 690 700
PIGAGICASY HTVSLLRSTS QKSIVAYTMS LGADSSIAYS NNTIAIPTNF
710 720 730 740 750
SISITTEVMP VSMAKTSVDC NMYICGDSTE CANLLLQYGS FCTQLNRALS
760 770 780 790 800
GIAAEQDRNT REVFAQVKQM YKTPTLKYFG GFNFSQILPD PLKPTKRSFI
810 820 830 840 850
EDLLFNKVTL ADAGFMKQYG ECLGDINARD LICAQKFNGL TVLPPLLTDD
860 870 880 890 900
MIAAYTAALV SGTATAGWTF GAGAALQIPF AMQMAYRFNG IGVTQNVLYE
910 920 930 940 950
NQKQIANQFN KAISQIQESL TTTSTALGKL QDVVNQNAQA LNTLVKQLSS
960 970 980 990 1000
NFGAISSVLN DILSRLDKVE AEVQIDRLIT GRLQSLQTYV TQQLIRAAEI
1010 1020 1030 1040 1050
RASANLAATK MSECVLGQSK RVDFCGKGYH LMSFPQAAPH GVVFLHVTYV
1060 1070 1080 1090 1100
PSQERNFTTA PAICHEGKAY FPREGVFVFN GTSWFITQRN FFSPQIITTD
1110 1120 1130 1140 1150
NTFVSGNCDV VIGIINNTVY DPLQPELDSF KEELDKYFKN HTSPDVDLGD
1160 1170 1180 1190 1200
ISGINASVVN IQKEIDRLNE VAKNLNESLI DLQELGKYEQ YIKWPWYVWL
1210 1220 1230 1240 1250
GFIAGLIAIV MVTILLCCMT SCCSCLKGAC SCGSCCKFDE DDSEPVLKGV

KLHYT
Length:1,255
Mass (Da):139,125
Last modified:April 23, 2003 - v1
Checksum:i1C49ACA2CFD38FC0
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti49S → L in strain: Isolate GZ50. 1
Natural varianti77G → D in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate GZ50, Isolate CUHK-W1, Isolate HKU-36871, Isolate GD01, Isolate GD03 and Isolate SZ3. 1
Natural varianti78N → D in strain: Isolate GD03. 1
Natural varianti118N → S in strain: Isolate Shanghai LY. 1
Natural varianti139A → V in strain: Isolate GD03. 1
Natural varianti144M → L in strain: Isolate BJ03. 1
Natural varianti147Q → R in strain: Isolate GD03. 1
Natural varianti193F → S in strain: Isolate Shanghai LY. 1
Natural varianti227N → K in strain: Isolate SZ3. 1
Natural varianti239S → L in strain: Isolate GD01 and Isolate SZ3. 1
Natural varianti244I → T in strain: Isolate BJ01, Isolate BJ02, Isolate BJ03, Isolate BJ04, Isolate GZ50, Isolate CUHK-W1, Isolate HKU-36871, Isolate GD01, Isolate GD03 and Isolate SZ3. 1
Natural varianti261T → K in strain: Isolate SZ3. 1
Natural varianti311G → R in strain: Isolate GD01 and Isolate BJ02. 1
Natural varianti344K → R in strain: Isolate GD01, Isolate GD03 and Isolate SZ3; no effect on affinity with either human or palm civet ACE2. 1 Publication1
Natural varianti360F → S in strain: Isolate GD03 and Isolate SZ3; no effect on affinity with either human or palm civet ACE2. 1 Publication1
Natural varianti426R → G in strain: Isolate Shanghai LY. 1
Natural varianti437N → D in strain: Isolate Shanghai LY. 1
Natural varianti472L → P in strain: Isolate GD03. 1
Natural varianti479N → K in strain: Isolate SZ3; 20fold decrease of affinity with human ACE2; no effect on affinity with palm civet ACE2. 1 Publication1
Natural varianti480D → G in strain: Isolate GD03. 1
Natural varianti487T → S in strain: Isolate GD03 and Isolate SZ3; 20fold decrease of affinity with human ACE2; decrease of affinity with palm civet ACE2. 1 Publication1
Natural varianti501F → Y in strain: Isolate GD01. 1
Natural varianti577S → A in strain: Isolate Tor2 and Isolate Shanghai QXC1. 1
Natural varianti605D → N in strain: Isolate Shanghai QXC1. 1
Natural varianti607S → P in strain: Isolate SZ3. 1
Natural varianti608T → A in strain: Isolate Shanghai QXC1. 1
Natural varianti609A → L in strain: Isolate GD03. 1
Natural varianti613D → E in strain: Isolate GD03. 1
Natural varianti665L → S in strain: Isolate GD03 and Isolate SZ3. 1
Natural varianti701S → L in strain: Isolate SZ3. 1
Natural varianti743T → A in strain: Isolate SZ3. 1
Natural varianti743T → R in strain: Isolate GD03. 1
Natural varianti754A → V in strain: Isolate SZ3. 1
Natural varianti765A → V in strain: Isolate GD03. 1
Natural varianti778Y → D in strain: Isolate GD01, Isolate GZ50, Isolate GD03 and Isolate SZ3. 1
Natural varianti794P → S in strain: Isolate GD01. 1
Natural varianti804L → P in strain: Isolate Shanghai LY. 1
Natural varianti860 – 861VS → LR in strain: Isolate BJ03. 2
Natural varianti894T → A in strain: Isolate SZ3. 1
Natural varianti999E → G in strain: Isolate Shanghai LY. 1
Natural varianti1001R → M in strain: Isolate BJ04. 1
Natural varianti1132E → G in strain: Isolate Shanghai QXC1. 1
Natural varianti1148L → F in strain: Isolate Frankfurt 1 and Isolate FRA. 1
Natural varianti1163K → E in strain: Isolate GD03 and Isolate SZ3. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY278741 Genomic RNA Translation: AAP13441.1
AY274119 Genomic RNA Translation: AAP41037.1
AY282752 Genomic RNA Translation: AAP30713.1
AY278554 Genomic RNA Translation: AAP13567.1
AY278491 Genomic RNA No translation available.
AY304495 Genomic RNA No translation available.
AY304492 Genomic RNA No translation available.
AY278487 Genomic RNA No translation available.
AY278488 Genomic RNA Translation: AAP30030.1
AY278490 Genomic RNA No translation available.
AY279354 Genomic RNA No translation available.
AY278489 Genomic RNA Translation: AAP51227.1
AY283794 Genomic RNA No translation available.
AY283795 Genomic RNA No translation available.
AY283796 Genomic RNA No translation available.
AY283797 Genomic RNA No translation available.
AY283798 Genomic RNA No translation available.
AY291451 Genomic RNA Translation: AAP37017.1
AY310120 Genomic RNA Translation: AAP50485.1
AY291315 Genomic RNA Translation: AAP33697.1
AY304486 Genomic RNA No translation available.
AY321118 Genomic RNA No translation available.
AY323976 mRNA Translation: AAP73417.1
AY322207 Genomic RNA Translation: AAP82968.1
AY338174 Genomic RNA Translation: AAQ01597.1
AY338175 Genomic RNA Translation: AAQ01609.1
AY348314 Genomic RNA Translation: AAP97882.1
AP006557 Genomic RNA Translation: BAC81348.1
AP006558 Genomic RNA Translation: BAC81362.1
AP006559 Genomic RNA Translation: BAC81376.1
AP006560 Genomic RNA Translation: BAC81390.1
AP006561 Genomic RNA Translation: BAC81404.1
AY323977 Genomic RNA Translation: AAP72986.1
AY362698 Genomic RNA No translation available.
AY362699 Genomic RNA No translation available.
AY427439 Genomic RNA Translation: AAQ94060.1
AY463059 Genomic RNA Translation: AAR86788.1
AY525636 Genomic RNA Translation: AAS10463.1

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY278741 Genomic RNA Translation: AAP13441.1
AY274119 Genomic RNA Translation: AAP41037.1
AY282752 Genomic RNA Translation: AAP30713.1
AY278554 Genomic RNA Translation: AAP13567.1
AY278491 Genomic RNA No translation available.
AY304495 Genomic RNA No translation available.
AY304492 Genomic RNA No translation available.
AY278487 Genomic RNA No translation available.
AY278488 Genomic RNA Translation: AAP30030.1
AY278490 Genomic RNA No translation available.
AY279354 Genomic RNA No translation available.
AY278489 Genomic RNA Translation: AAP51227.1
AY283794 Genomic RNA No translation available.
AY283795 Genomic RNA No translation available.
AY283796 Genomic RNA No translation available.
AY283797 Genomic RNA No translation available.
AY283798 Genomic RNA No translation available.
AY291451 Genomic RNA Translation: AAP37017.1
AY310120 Genomic RNA Translation: AAP50485.1
AY291315 Genomic RNA Translation: AAP33697.1
AY304486 Genomic RNA No translation available.
AY321118 Genomic RNA No translation available.
AY323976 mRNA Translation: AAP73417.1
AY322207 Genomic RNA Translation: AAP82968.1
AY338174 Genomic RNA Translation: AAQ01597.1
AY338175 Genomic RNA Translation: AAQ01609.1
AY348314 Genomic RNA Translation: AAP97882.1
AP006557 Genomic RNA Translation: BAC81348.1
AP006558 Genomic RNA Translation: BAC81362.1
AP006559 Genomic RNA Translation: BAC81376.1
AP006560 Genomic RNA Translation: BAC81390.1
AP006561 Genomic RNA Translation: BAC81404.1
AY323977 Genomic RNA Translation: AAP72986.1
AY362698 Genomic RNA No translation available.
AY362699 Genomic RNA No translation available.
AY427439 Genomic RNA Translation: AAQ94060.1
AY463059 Genomic RNA Translation: AAR86788.1
AY525636 Genomic RNA Translation: AAS10463.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Q4Zmodel-A17-680[»]
1T7Gmodel-A/C/E17-680[»]
B/D/F737-1026[»]
1U4Kmodel-D764-1089[»]
1WNCX-ray2.80A/B/C/D/E/F900-948[»]
A/B/C/D/E/F1144-1185[»]
1WYYX-ray2.20A/B885-981[»]
A/B1145-1189[»]
1XJPmodel-A17-680[»]
1ZV7X-ray1.70A/B1150-1193[»]
1ZV8X-ray1.94A/C/E/G/I/K901-950[»]
B/D/F/H/J/L1150-1185[»]
1ZVBX-ray1.70A/B/C940-973[»]
2AJFX-ray2.90E/F323-502[»]
2BEQX-ray1.60A/B/C914-949[»]
D/E/F1148-1193[»]
2BEZX-ray1.60C896-972[»]
F1142-1183[»]
2DD8X-ray2.30S317-518[»]
2FXPNMR-A/B/C1141-1193[»]
2GHVX-ray2.20C/E317-510[»]
2GHWX-ray2.30A/C317-510[»]
2RUMNMR-A770-788[»]
2RUNNMR-A1185-1202[»]
2RUONMR-A873-888[»]
3BGFX-ray3.00A/S318-510[»]
3D0GX-ray2.80E/F324-502[»]
3D0HX-ray3.10E/F324-502[»]
3D0IX-ray2.90E/F324-502[»]
3SCIX-ray2.90E/F306-527[»]
3SCJX-ray3.00E/F323-502[»]
3SCKX-ray3.00E/F324-502[»]
3SCLX-ray3.00E/F324-502[»]
5WRGelectron microscopy4.30A/B/C1-1196[»]
5X4SX-ray2.20A14-292[»]
5X58electron microscopy3.20A/B/C14-1193[»]
5X5Belectron microscopy3.70A/B/C14-1193[»]
5XJKNMR-A758-821[»]
5XLRelectron microscopy3.80A/B/C1-1196[»]
6ACCelectron microscopy3.60A/B/C1-1196[»]
6ACDelectron microscopy3.90A/B/C1-1196[»]
6ACGelectron microscopy5.40A/B/C1-1196[»]
6ACJelectron microscopy4.20A/B/C1-1196[»]
6ACKelectron microscopy4.50A/B/C1-1196[»]
6CRVelectron microscopy3.20A/B/C14-1190[»]
6CRWelectron microscopy3.90A/B/C14-1190[»]
6CRXelectron microscopy3.90A/B/C14-1190[»]
6CRZelectron microscopy3.30A/B/C14-1190[»]
6CS0electron microscopy3.80A/B/C14-1190[»]
6CS1electron microscopy4.60A/B/C14-1190[»]
6CS2electron microscopy4.40A/B/C14-1190[»]
ProteinModelPortaliP59594
SMRiP59594
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29105N
IntActiP59594, 1 interactor

Proteomic databases

PRIDEiP59594

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

OrthoDBiVOG0900000Z

Miscellaneous databases

EvolutionaryTraceiP59594

Family and domain databases

Gene3Di1.20.5.790, 1 hit
HAMAPiMF_04099 BETA_CORONA_SPIKE, 1 hit
InterProiView protein in InterPro
IPR002552 Corona_S2
IPR027400 S_HR2
IPR032500 Spike_N
IPR018548 Spike_rcpt-bd
IPR036326 Spike_rcpt-bd_sf
PfamiView protein in Pfam
PF01601 Corona_S2, 1 hit
PF16451 Spike_NTD, 1 hit
PF09408 Spike_rec_bind, 1 hit
SUPFAMiSSF143587 SSF143587, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiSPIKE_CVHSA
AccessioniPrimary (citable) accession number: P59594
Secondary accession number(s): Q6QU82
, Q7T696, Q7TA19, Q7TFA2, Q7TFB1, Q80BV6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: October 10, 2018
This is version 125 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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