P03316

SS
Gene name
Protein name
Structural polyprotein
Names
p130 [Cleaved into: Capsid protein , EC 3.4.21.90 , Coat protein , C; Precursor of protein E3/E2 , p62 , pE2; Assembly protein E3; Spike glycoprotein E2 , E2 envelope glycoprotein; 6K protein; Spike glycoprotein E1 , E1 envelope glycoprotein]
Species
Sindbis virus (SINV)
KEGG Pathway
vg:1502155
EC number
3.4.21.90: Serine endopeptidases
Protein Class

Descriptions

This structural polyprotein forms an icosahedral capsid that binds to the viral RNA genome at a site adjacent to a ribosome binding site for viral genome translation following genome release. Autoinhibition of the suicidal capsid protease (CP) involves the C-terminal tryptophan localizing to the active pocket, effectively deactivating the enzyme. This results in the lack of enzymatic activity, crucial for halting the viral replication cycle as the virus cannot produce infectious progeny.

Autoinhibitory domains (AIDs)

263-264 (C-terminal residues of capsid protease) SS

Target domain

114-264 (Peptidase S3)

Relief mechanism

Partner binding

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

14 structures for P03316

Entry ID Method Resolution Chain Position Source
1KXA X-ray 310 A A 106-264 PDB
1KXB X-ray 290 A A 106-264 PDB
1KXC X-ray 310 A A 106-264 PDB
1KXD X-ray 300 A A 106-264 PDB
1KXE X-ray 320 A A 106-264 PDB
1KXF X-ray 238 A A 106-264 PDB
1LD4 EM 1140 A PDB
1SVP X-ray 200 A A/B 106-266 PDB
1Z8Y EM 900 A PDB
2SNV X-ray 280 A A 114-264 PDB
2SNW X-ray 270 A A/B 107-264 PDB
3J0F EM - PDB
3MUU X-ray 329 A PDB
3MUW EM - PDB

9 variants for P03316

Variant ID(s) Position Change Description Diseaes Association Provenance
329 S>RVT strain: AR339 [UniProt] No
333 D>G strain: HRLP [UniProt] No
351 V>E strain: AR339 and HRLP [UniProt] No
398 K>E strain: AR339 [UniProt] No
442 S>R causes attenuation of the virus [UniProt] No
447 N>KNGSF strain: ov-100 [UniProt] No
500 R>G strain: AR339 [UniProt] No
719 K>L strain: TE12 [UniProt] No
919 D>V strain: HRLP [UniProt] No

No associated diseases with P03316

3 regional properties for P03316

Type Name Position InterPro Accession
domain Toll/interleukin-1 receptor homology (TIR) domain 560 - 703 IPR000157
domain Sterile alpha motif domain 409 - 476 IPR001660-1
domain Sterile alpha motif domain 479 - 548 IPR001660-2

Functions

Description
EC Number 3.4.21.90 Serine endopeptidases
Subcellular Localization
  • [Capsid protein]: Virion
  • Host cytoplasm
  • Host cell membrane
  • Host nucleus
  • Shuttles between the cytoplasm and the nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

8 GO annotations of cellular component

Name Definition
host cell cytoplasm The cytoplasm of a host cell.
host cell nucleus A membrane-bounded organelle as it is found in the host cell in which chromosomes are housed and replicated. The host is defined as the larger of the organisms involved in a symbiotic interaction.
host cell plasma membrane The plasma membrane surrounding a host cell.
icosahedral viral capsid, spike A short structure attached to an icosahedral virion capsid, and used for attachment to the host cell.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.
T=4 icosahedral viral capsid The protein coat that surrounds the infective nucleic acid in some virus particles where the subunits (capsomeres) are arranged to form an icosahedron with T=4 symmetry. The T=4 capsid is composed of 12 pentameric and 30 hexameric capsomeres.
viral envelope The lipid bilayer of a virion that surrounds the protein capsid. May also contain glycoproteins.
virion membrane The lipid bilayer surrounding a virion.

4 GO annotations of molecular function

Name Definition
RNA binding Binding to an RNA molecule or a portion thereof.
serine-type endopeptidase activity Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a catalytic mechanism that involves a catalytic triad consisting of a serine nucleophile that is activated by a proton relay involving an acidic residue (e.g. aspartate or glutamate) and a basic residue (usually histidine).
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex.
ubiquitin-like protein ligase binding Binding to a ubiquitin-like protein ligase, such as ubiquitin-ligase.

6 GO annotations of biological process

Name Definition
clathrin-dependent endocytosis of virus by host cell Any clathrin-mediated endocytosis that is involved in the uptake of a virus into a host cell. Begins by invagination of a specific region of the host cell plasma membrane around the bound virus to form a clathrin-coated pit, which then pinches off to form a clathrin-coated endocytic vesicle containing the virus.
fusion of virus membrane with host endosome membrane Fusion of a virus membrane with a host endosome membrane. Occurs after internalization of the virus through the endosomal pathway, and results in release of the virus contents into the cell.
membrane fusion The membrane organization process that joins two lipid bilayers to form a single membrane.
proteolysis The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds.
suppression by virus of host toll-like receptor signaling pathway Any process in which a virus stops, prevents, or reduces the frequency, rate or extent of toll-like receptor (TLR) signaling in the host organism.
virion attachment to host cell The process by which a virion protein binds to molecules on the host cellular surface or host cell surface projection.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MNRGFFNMLG RRPFPAPTAM WRPRRRRQAA PMPARNGLAS QIQQLTTAVS ALVIGQATRP
70 80 90 100 110 120
QPPRPRPPPR QKKQAPKQPP KPKKPKTQEK KKKQPAKPKP GKRQRMALKL EADRLFDVKN
130 140 150 160 170 180
EDGDVIGHAL AMEGKVMKPL HVKGTIDHPV LSKLKFTKSS AYDMEFAQLP VNMRSEAFTY
190 200 210 220 230 240
TSEHPEGFYN WHHGAVQYSG GRFTIPRGVG GRGDSGRPIM DNSGRVVAIV LGGADEGTRT
250 260 270 280 290 300
ALSVVTWNSK GKTIKTTPEG TEEWSAAPLV TAMCLLGNVS FPCDRPPTCY TREPSRALDI
310 320 330 340 350 360
LEENVNHEAY DTLLNAILRC GSSGRSKRSV IDDFTLTSPY LGTCSYCHHT VPCFSPVKIE
370 380 390 400 410 420
QVWDEADDNT IRIQTSAQFG YDQSGAASAN KYRYMSLKQD HTVKEGTMDD IKISTSGPCR
430 440 450 460 470 480
RLSYKGYFLL AKCPPGDSVT VSIVSSNSAT SCTLARKIKP KFVGREKYDL PPVHGKKIPC
490 500 510 520 530 540
TVYDRLKETT AGYITMHRPR PHAYTSYLEE SSGKVYAKPP SGKNITYECK CGDYKTGTVS
550 560 570 580 590 600
TRTEITGCTA IKQCVAYKSD QTKWVFNSPD LIRHDDHTAQ GKLHLPFKLI PSTCMVPVAH
610 620 630 640 650 660
APNVIHGFKH ISLQLDTDHL TLLTTRRLGA NPEPTTEWIV GKTVRNFTVD RDGLEYIWGN
670 680 690 700 710 720
HEPVRVYAQE SAPGDPHGWP HEIVQHYYHR HPVYTILAVA SATVAMMIGV TVAVLCACKA
730 740 750 760 770 780
RRECLTPYAL APNAVIPTSL ALLCCVRSAN AETFTETMSY LWSNSQPFFW VQLCIPLAAF
790 800 810 820 830 840
IVLMRCCSCC LPFLVVAGAY LAKVDAYEHA TTVPNVPQIP YKALVERAGY APLNLEITVM
850 860 870 880 890 900
SSEVLPSTNQ EYITCKFTTV VPSPKIKCCG SLECQPAAHA DYTCKVFGGV YPFMWGGAQC
910 920 930 940 950 960
FCDSENSQMS EAYVELSADC ASDHAQAIKV HTAAMKVGLR IVYGNTTSFL DVYVNGVTPG
970 980 990 1000 1010 1020
TSKDLKVIAG PISASFTPFD HKVVIHRGLV YNYDFPEYGA MKPGAFGDIQ ATSLTSKDLI
1030 1040 1050 1060 1070 1080
ASTDIRLLKP SAKNVHVPYT QASSGFEMWK NNSGRPLQET APFGCKIAVN PLRAVDCSYG
1090 1100 1110 1120 1130 1140
NIPISIDIPN AAFIRTSDAP LVSTVKCEVS ECTYSADFGG MATLQYVSDR EGQCPVHSHS
1150 1160 1170 1180 1190 1200
STATLQESTV HVLEKGAVTV HFSTASPQAN FIVSLCGKKT TCNAECKPPA DHIVSTPHKN
1210 1220 1230 1240
DQEFQAAISK TSWSWLFALF GGASSLLIIG LMIFACSMML TSTRR