ID GC_HHV11 Reviewed; 511 AA. AC P10228; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 21-SEP-2011, entry version 67. DE RecName: Full=Glycoprotein C; DE Short=gC; DE Flags: Precursor; GN Name=GC; Synonyms=UL44; OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus OS 1). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Alphaherpesvirinae; Simplexvirus. OX NCBI_TaxID=10299; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=88274327; PubMed=2839594; RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., RA McNab D., Perry L.J., Scott J.E., Taylor P.; RT "The complete DNA sequence of the long unique region in the genome of RT herpes simplex virus type 1."; RL J. Gen. Virol. 69:1531-1574(1988). RN [2] RP INTERACTION WITH HOST C3. RX PubMed=2849025; DOI=10.1016/0882-4010(87)90012-X; RA Eisenberg R.J., Ponce de Leon M., Friedman H.M., Fries L.F., RA Frank M.M., Hastings J.C., Cohen G.H.; RT "Complement component C3b binds directly to purified glycoprotein C of RT herpes simplex virus types 1 and 2."; RL Microb. Pathog. 3:423-435(1987). RN [3] RP DISULFIDE BONDS. RX PubMed=8764057; RA Rux A.H., Moore W.T., Lambris J.D., Abrams W.R., Peng C., RA Friedman H.M., Cohen G.H., Eisenberg R.J.; RT "Disulfide bond structure determination and biochemical analysis of RT glycoprotein C from herpes simplex virus."; RL J. Virol. 70:5455-5465(1996). CC -!- FUNCTION: Major attachment protein that mediates binding of the CC virus to cell surface heparan sulfate or chondroitin sulfate. CC Plays also several roles in host immune evasion by inhibiting the CC host complement cascade activation, and by providing a shield CC against neutralizing antibodies that interfere with gB-gD, gB- CC gH/gL or gD-gH/gL interactions (By similarity). CC -!- SUBUNIT: Interacts with host complement component C3b; this CC interaction inhibits host immune response by disregulating CC complement cascade. CC -!- SUBCELLULAR LOCATION: Virion membrane; Single-pass membrane CC protein (Potential). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing, Alternative initiation; Named isoforms=2; CC Name=gC; CC IsoId=P10228-1; Sequence=Displayed; CC Note=Membrane-bound gC; CC Name=gCsec; CC IsoId=P10228-2; Sequence=VSP_040892; CC Note=Secreted; CC -!- MISCELLANEOUS: There are seven external glycoproteins in HSV-1 and CC 2: gH, gB, gC, gG, gD, gI, and gE. CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein C family. CC -!- SIMILARITY: Contains 1 Ig-like (immunoglobulin-like) domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X14112; CAA32294.1; -; Genomic_DNA. DR PIR; H30088; VGBEF4. DR RefSeq; NP_044646.1; NC_001806.1. DR ProteinModelPortal; P10228; -. DR GeneID; 2703410; -. DR ProtClustDB; PHA3270; -. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030683; P:evasion by virus of host immune response; IEA:UniProtKB-KW. DR InterPro; IPR001038; GA_GC. DR InterPro; IPR007110; Ig-like. DR InterPro; IPR013783; Ig-like_fold. DR Gene3D; G3DSA:2.60.40.10; Ig-like_fold; 1. DR Pfam; PF02124; Marek_A; 1. DR PRINTS; PR00668; GLYCPROTEINC. DR PROSITE; PS50835; IG_LIKE; 1. PE 1: Evidence at protein level; KW Alternative initiation; Alternative splicing; Complete proteome; KW Disulfide bond; Glycoprotein; Host-virus interaction; KW Immunoglobulin domain; Inhibition of host complement factors by virus; KW Initiation of viral infection; Membrane; Reference proteome; Signal; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral immunoevasion; Virion. FT SIGNAL 1 24 Potential. FT CHAIN 25 511 Glycoprotein C. FT /FTId=PRO_0000038197. FT TRANSMEM 481 497 Helical; (Potential). FT DOMAIN 267 359 Ig-like. FT REGION 137 151 Heparin-binding domain (By similarity). FT CARBOHYD 42 42 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 70 70 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 74 74 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 108 108 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 148 148 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 181 181 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 197 197 N-linked (GlcNAc...); by host FT (Potential). FT CARBOHYD 362 362 N-linked (GlcNAc...); by host FT (Potential). FT DISULFID 127 144 FT DISULFID 286 347 FT DISULFID 386 442 FT DISULFID 390 419 FT VAR_SEQ 472 511 VIEAIEWVGIGIGVLAAGVLVVTAIVYVVRTSQSRQRHRR FT -> VILGRSRTTHGVEQNASP (in isoform gCsec). FT /FTId=VSP_040892. SQ SEQUENCE 511 AA; 54998 MW; 874BE474DC7D71C5 CRC64; MAPGRVGLAV VLWSLLWLGA GVSGGSETAS TGPTITAGAV TNASEAPTSG SPGSAASPEV TPTSTPNPNN VTQNKTTPTE PASPPTTPKP TSTPKSPPTS TPDPKPKNNT TPAKSGRPTK PPGPVWCDRR DPLARYGSRV QIRCRFRNST RMEFRLQIWR YSMGPSPPIA PAPDLEEVLT NITAPPGGLL VYDSAPNLTD PHVLWAEGAG PGADPPLYSV TGPLPTQRLI IGEVTPATQG MYYLAWGRMD SPHEYGTWVR VRMFRPPSLT LQPHAVMEGQ PFKATCTAAA YYPRNPVEFV WFEDDHQVFN PGQIDTQTHE HPDGFTTVST VTSEAVGGQV PPRTFTCQMT WHRDSVTFSR RNATGLALVL PRPTITMEFG VRIVVCTAGC VPEGVTFAWF LGDDPSPAAK SAVTAQESCD HPGLATVRST LPISYDYSEY ICRLTGYPAG IPVLEHHGSH QPPPRDPTER QVIEAIEWVG IGIGVLAAGV LVVTAIVYVV RTSQSRQRHR R //