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P10228 (GC_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein C
Gene names
Name:gC
Synonyms:UL44
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length511 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Major attachment protein that mediates binding of the virus to cell surface heparan sulfate or chondroitin sulfate. Plays also several roles in host immune evasion by inhibiting the host complement cascade activation, and by providing a shield against neutralizing antibodies that interfere with gB-gD, gB-gH/gL or gD-gH/gL interactions By similarity.

Subunit structure

Interacts with host complement component C3b; this interaction inhibits host immune response by disregulating complement cascade. Ref.2

Subcellular location

Virion membrane; Single-pass membrane protein Potential.

Miscellaneous

There are seven external glycoproteins in HSV-1 and 2: gH, gB, gC, gG, gD, gI, and gE.

Sequence similarities

Belongs to the herpesviridae glycoprotein C family.

Contains 1 Ig-like (immunoglobulin-like) domain.

Alternative products

This entry describes 2 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform gC (identifier: P10228-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Membrane-bound gC.
Isoform gCsec (identifier: P10228-2)

The sequence of this isoform differs from the canonical sequence as follows:
     472-511: VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR → VILGRSRTTHGVEQNASP
Note: Secreted.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 511487Envelope glycoprotein C
PRO_0000038197

Regions

Topological domain25 – 480456Virion surface Potential
Transmembrane481 – 49717Helical; Potential
Topological domain498 – 51114Cytoplasmic Potential
Domain267 – 35993Ig-like
Region137 – 15115Heparin-binding domain By similarity

Amino acid modifications

Glycosylation421N-linked (GlcNAc...); by host Potential
Glycosylation701N-linked (GlcNAc...); by host Potential
Glycosylation741N-linked (GlcNAc...); by host Potential
Glycosylation1081N-linked (GlcNAc...); by host Potential
Glycosylation1481N-linked (GlcNAc...); by host Potential
Glycosylation1811N-linked (GlcNAc...); by host Potential
Glycosylation1971N-linked (GlcNAc...); by host Potential
Glycosylation3621N-linked (GlcNAc...); by host Potential
Disulfide bond127 ↔ 144 Ref.3
Disulfide bond286 ↔ 347 Ref.3
Disulfide bond386 ↔ 442 Ref.3
Disulfide bond390 ↔ 419 Ref.3

Natural variations

Alternative sequence472 – 51140VIEAI…QRHRR → VILGRSRTTHGVEQNASP in isoform gCsec.
VSP_040892

Sequences

Sequence LengthMass (Da)Tools
Isoform gC [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: 874BE474DC7D71C5

FASTA51154,998
        10         20         30         40         50         60 
MAPGRVGLAV VLWSLLWLGA GVSGGSETAS TGPTITAGAV TNASEAPTSG SPGSAASPEV 

        70         80         90        100        110        120 
TPTSTPNPNN VTQNKTTPTE PASPPTTPKP TSTPKSPPTS TPDPKPKNNT TPAKSGRPTK 

       130        140        150        160        170        180 
PPGPVWCDRR DPLARYGSRV QIRCRFRNST RMEFRLQIWR YSMGPSPPIA PAPDLEEVLT 

       190        200        210        220        230        240 
NITAPPGGLL VYDSAPNLTD PHVLWAEGAG PGADPPLYSV TGPLPTQRLI IGEVTPATQG 

       250        260        270        280        290        300 
MYYLAWGRMD SPHEYGTWVR VRMFRPPSLT LQPHAVMEGQ PFKATCTAAA YYPRNPVEFV 

       310        320        330        340        350        360 
WFEDDHQVFN PGQIDTQTHE HPDGFTTVST VTSEAVGGQV PPRTFTCQMT WHRDSVTFSR 

       370        380        390        400        410        420 
RNATGLALVL PRPTITMEFG VRIVVCTAGC VPEGVTFAWF LGDDPSPAAK SAVTAQESCD 

       430        440        450        460        470        480 
HPGLATVRST LPISYDYSEY ICRLTGYPAG IPVLEHHGSH QPPPRDPTER QVIEAIEWVG 

       490        500        510 
IGIGVLAAGV LVVTAIVYVV RTSQSRQRHR R 

« Hide

Isoform gCsec [UniParc].

Checksum: 9699C16B1B67CB0E
Show »

FASTA48952,547

References

[1]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complement component C3b binds directly to purified glycoprotein C of herpes simplex virus types 1 and 2."
Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., Frank M.M., Hastings J.C., Cohen G.H.
Microb. Pathog. 3:423-435(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HOST C3.
[3]"Disulfide bond structure determination and biochemical analysis of glycoprotein C from herpes simplex virus."
Rux A.H., Moore W.T., Lambris J.D., Abrams W.R., Peng C., Friedman H.M., Cohen G.H., Eisenberg R.J.
J. Virol. 70:5455-5465(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DISULFIDE BONDS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14112 Genomic DNA. Translation: CAA32294.1.
PIRVGBEF4. H30088.
RefSeqNP_044646.1. NC_001806.1.

3D structure databases

ProteinModelPortalP10228.
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2364696.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703410.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
InterProIPR001038. GA_GC.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamPF02124. Marek_A. 1 hit.
[Graphical view]
PRINTSPR00668. GLYCPROTEINC.
PROSITEPS50835. IG_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGC_HHV11
AccessionPrimary (citable) accession number: P10228
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: July 9, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families