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P10228

- GC_HHV11

UniProt

P10228 - GC_HHV11

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
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    • History
      Entry version 83 (01 Oct 2014)
      Sequence version 1 (01 Jul 1989)
      Previous versions | rss
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    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

    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]

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. virion membrane Source: UniProtKB-SubCell

    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 annotations
    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 annotations
    Glycosylationi362 – 3621N-linked (GlcNAc...); by hostSequence Analysis
    Disulfide bondi386 ↔ 4421 PublicationPROSITE-ProRule annotations
    Disulfide bondi390 ↔ 4191 PublicationPROSITE-ProRule annotations

    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]
    ProtoNetiSearch...

    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: P10228-1) [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

    MAPGRVGLAV VLWSLLWLGA GVSGGSETAS TGPTITAGAV TNASEAPTSG    50
    SPGSAASPEV TPTSTPNPNN VTQNKTTPTE PASPPTTPKP TSTPKSPPTS 100
    TPDPKPKNNT TPAKSGRPTK PPGPVWCDRR DPLARYGSRV QIRCRFRNST 150
    RMEFRLQIWR YSMGPSPPIA PAPDLEEVLT NITAPPGGLL VYDSAPNLTD 200
    PHVLWAEGAG PGADPPLYSV TGPLPTQRLI IGEVTPATQG MYYLAWGRMD 250
    SPHEYGTWVR VRMFRPPSLT LQPHAVMEGQ PFKATCTAAA YYPRNPVEFV 300
    WFEDDHQVFN PGQIDTQTHE HPDGFTTVST VTSEAVGGQV PPRTFTCQMT 350
    WHRDSVTFSR RNATGLALVL PRPTITMEFG VRIVVCTAGC VPEGVTFAWF 400
    LGDDPSPAAK SAVTAQESCD HPGLATVRST LPISYDYSEY ICRLTGYPAG 450
    IPVLEHHGSH QPPPRDPTER QVIEAIEWVG IGIGVLAAGV LVVTAIVYVV 500
    RTSQSRQRHR R 511

    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 1, 2014
    This is version 83 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

    Similar proteinsi