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Protein

Spike glycoprotein

Gene

S

Organism
Human SARS coronavirus (SARS-CoV) (Severe acute respiratory syndrome coronavirus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.
S2 is 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.

GO - Molecular functioni

  • host cell surface receptor binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Fusion 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 glycoprotein
Short name:
S glycoprotein
Alternative name(s):
E2
Peplomer protein
Cleaved into the following 2 chains:
Gene namesi
Name:S
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
  • UP000000354 Componenti: Genome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini14 – 1195ExtracellularSequence analysisAdd BLAST1182
Transmembranei1196 – 1216HelicalSequence analysisAdd BLAST21
Topological domaini1217 – 1255CytoplasmicSequence analysisAdd BLAST39

GO - Cellular componenti

Complete GO annotation...

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
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 – 13Sequence analysisAdd BLAST13
ChainiPRO_000003720814 – 1255Spike glycoproteinAdd BLAST1242
ChainiPRO_000003720914 – 667Spike protein S1Sequence analysisAdd BLAST654
ChainiPRO_0000037210668 – 1255Spike protein S2Sequence analysisAdd BLAST588

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi29N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi65N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi73N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi109N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi118N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi119N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi158N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi227N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi269N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi318N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi323 ↔ 348
Glycosylationi330N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi357N-linked (GlcNAc...); by hostSequence analysis1
Disulfide bondi366 ↔ 419
Disulfide bondi467 ↔ 474
Glycosylationi589N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi602N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi691N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi699N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi783N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1056N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1080N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1116N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1140N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1155N-linked (GlcNAc...); by hostSequence analysis1
Glycosylationi1176N-linked (GlcNAc...); by hostSequence analysis1

Post-translational modificationi

The cytoplasmic Cys-rich domain is palmitoylated. Spike glycoprotein is digested by cathepsin CTSL within endosomes.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei667 – 668CleavageSequence analysis2

Keywords - PTMi

Disulfide bond, Glycoprotein, Lipoprotein, Palmitate

Proteomic databases

PRIDEiP59594.

Interactioni

Subunit structurei

Homotrimer. Binds to human and palm civet ACE2 and human CLEC4M/DC-SIGNR. Interacts with the accessory proteins 3a and 7a.6 Publications

GO - Molecular functioni

  • host cell surface receptor binding Source: BHF-UCL

Protein-protein interaction databases

DIPiDIP-29105N.

Structurei

Secondary structure

11255
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi326 – 329Combined sources4
Helixi337 – 339Combined sources3
Beta strandi341 – 345Combined sources5
Beta strandi347 – 349Combined sources3
Helixi352 – 354Combined sources3
Beta strandi362 – 368Combined sources7
Helixi371 – 378Combined sources8
Beta strandi380 – 390Combined sources11
Helixi391 – 396Combined sources6
Beta strandi397 – 400Combined sources4
Helixi404 – 408Combined sources5
Beta strandi418 – 424Combined sources7
Helixi426 – 429Combined sources4
Beta strandi431 – 433Combined sources3
Beta strandi439 – 441Combined sources3
Beta strandi462 – 464Combined sources3
Beta strandi469 – 471Combined sources3
Beta strandi478 – 480Combined sources3
Beta strandi483 – 487Combined sources5
Helixi489 – 491Combined sources3
Beta strandi492 – 501Combined sources10
Beta strandi509 – 511Combined sources3
Helixi773 – 777Combined sources5
Helixi780 – 783Combined sources4
Turni784 – 786Combined sources3
Helixi879 – 887Combined sources9
Beta strandi898 – 900Combined sources3
Helixi915 – 948Combined sources34
Helixi1148 – 1151Combined sources4
Helixi1162 – 1172Combined sources11
Helixi1173 – 1178Combined sources6
Helixi1182 – 1192Combined sources11

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[»]
ProteinModelPortaliP59594.
SMRiP59594.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59594.

Family & Domainsi

Region

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

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili931 – 975Sequence analysisAdd BLAST45
Coiled coili1157 – 1185Sequence analysisAdd BLAST29

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1251 – 1255KxHxx5

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 coronaviruses spike protein family.Curated

Keywords - Domaini

Coiled coil, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di1.20.5.790. 1 hit.
InterProiIPR002552. Corona_S2.
IPR027400. S_HR2.
IPR032500. Spike_N.
IPR018548. Spike_rcpt-bd.
[Graphical view]
PfamiPF01601. Corona_S2. 1 hit.
PF16451. Spike_NTD. 1 hit.
PF09408. Spike_rec_bind. 1 hit.
[Graphical view]

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.

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[»]
ProteinModelPortaliP59594.
SMRiP59594.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29105N.

Proteomic databases

PRIDEiP59594.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP59594.

Family and domain databases

Gene3Di1.20.5.790. 1 hit.
InterProiIPR002552. Corona_S2.
IPR027400. S_HR2.
IPR032500. Spike_N.
IPR018548. Spike_rcpt-bd.
[Graphical view]
PfamiPF01601. Corona_S2. 1 hit.
PF16451. Spike_NTD. 1 hit.
PF09408. Spike_rec_bind. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSPIKE_CVHSA
AccessioniPrimary (citable) accession number: P59594
Secondary accession number(s): Q6QU82
, Q7T696, Q7TA19, Q7TFA2, Q7TFB1, Q80BV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 23, 2003
Last sequence update: April 23, 2003
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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.

Caution

Cleavage into S1 and S2 remains controversial, since biochemical evidence for this proteolytic cleavage is largely negative.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.