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P10228

- GC_HHV11

UniProt

P10228 - GC_HHV11

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Protein

Envelope glycoprotein C

Gene

gC

Organism
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Biological processi

  1. suppression by virus of host complement activation Source: UniProtKB-KW
  2. viral entry into host cell Source: UniProtKB-KW
  3. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Inhibition of host complement factors by virus, Viral attachment to host adhesion receptor, Viral attachment to host cell, Viral immunoevasion, Virus entry into host cell

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein C
Gene namesi
Name:gC
Synonyms:UL44
OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10299 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]
ProteomesiUP000009294: Genome

Subcellular locationi

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. virion Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 511487Envelope glycoprotein CPRO_0000038197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi42 – 421N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi70 – 701N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi74 – 741N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi108 – 1081N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi127 ↔ 1441 PublicationPROSITE-ProRule annotation
Glycosylationi148 – 1481N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi181 – 1811N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi197 – 1971N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi286 ↔ 3471 PublicationPROSITE-ProRule annotation
Glycosylationi362 – 3621N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi386 ↔ 4421 PublicationPROSITE-ProRule annotation
Disulfide bondi390 ↔ 4191 PublicationPROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

Interacts with host complement component C3b; this interaction inhibits host immune response by disregulating complement cascade.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP10228.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini25 – 480456Virion surfaceSequence AnalysisAdd
BLAST
Topological domaini498 – 51114CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei481 – 49717HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini267 – 35993Ig-likeAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni137 – 15115Heparin-binding domainBy similarityAdd
BLAST

Sequence similaritiesi

Keywords - Domaini

Immunoglobulin domain, Signal, Transmembrane, Transmembrane helix

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
InterProiIPR001038. GA_GC.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
[Graphical view]
PfamiPF02124. Marek_A. 1 hit.
[Graphical view]
PRINTSiPR00668. GLYCPROTEINC.
PROSITEiPS50835. IG_LIKE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing and alternative initiation. Align

Isoform gC (identifier: P10228) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MAPGRVGLAV VLWSLLWLGA GVSGGSETAS TGPTITAGAV TNASEAPTSG
60 70 80 90 100
SPGSAASPEV TPTSTPNPNN VTQNKTTPTE PASPPTTPKP TSTPKSPPTS
110 120 130 140 150
TPDPKPKNNT TPAKSGRPTK PPGPVWCDRR DPLARYGSRV QIRCRFRNST
160 170 180 190 200
RMEFRLQIWR YSMGPSPPIA PAPDLEEVLT NITAPPGGLL VYDSAPNLTD
210 220 230 240 250
PHVLWAEGAG PGADPPLYSV TGPLPTQRLI IGEVTPATQG MYYLAWGRMD
260 270 280 290 300
SPHEYGTWVR VRMFRPPSLT LQPHAVMEGQ PFKATCTAAA YYPRNPVEFV
310 320 330 340 350
WFEDDHQVFN PGQIDTQTHE HPDGFTTVST VTSEAVGGQV PPRTFTCQMT
360 370 380 390 400
WHRDSVTFSR RNATGLALVL PRPTITMEFG VRIVVCTAGC VPEGVTFAWF
410 420 430 440 450
LGDDPSPAAK SAVTAQESCD HPGLATVRST LPISYDYSEY ICRLTGYPAG
460 470 480 490 500
IPVLEHHGSH QPPPRDPTER QVIEAIEWVG IGIGVLAAGV LVVTAIVYVV
510
RTSQSRQRHR R

Note: Membrane-bound gC.

Length:511
Mass (Da):54,998
Last modified:July 1, 1989 - v1
Checksum:i874BE474DC7D71C5
GO
Isoform gCsec (identifier: P10228-2) [UniParc]FASTAAdd to Basket

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

Note: Secreted.

Show »
Length:489
Mass (Da):52,547
Checksum:i9699C16B1B67CB0E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei472 – 51140VIEAI…QRHRR → VILGRSRTTHGVEQNASP in isoform gCsec. CuratedVSP_040892Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32294.1.
PIRiH30088. VGBEF4.
RefSeqiNP_044646.1. NC_001806.1.

Genome annotation databases

GeneIDi2703410.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X14112 Genomic DNA. Translation: CAA32294.1 .
PIRi H30088. VGBEF4.
RefSeqi NP_044646.1. NC_001806.1.

3D structure databases

ProteinModelPortali P10228.
ModBasei Search...
MobiDBi Search...

Chemistry

ChEMBLi CHEMBL2364696.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 2703410.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
InterProi IPR001038. GA_GC.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
[Graphical view ]
Pfami PF02124. Marek_A. 1 hit.
[Graphical view ]
PRINTSi PR00668. GLYCPROTEINC.
PROSITEi PS50835. IG_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGC_HHV11
AccessioniPrimary (citable) accession number: P10228
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: October 29, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3