GP_CCHFI
ID GP_CCHFI Reviewed; 1684 AA.
AC Q8JSZ3;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Mucin-like variable region;
DE Contains:
DE RecName: Full=GP38 {ECO:0000305|PubMed:17898072};
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000305|PubMed:17898072};
DE Short=Gn;
DE AltName: Full=Glycoprotein G2;
DE Contains:
DE RecName: Full=Non-Structural protein M {ECO:0000305|PubMed:17898072};
DE Short=NSm;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000305|PubMed:17898072};
DE Short=Gc;
DE AltName: Full=Glycoprotein G1;
DE Flags: Precursor;
GN Name=GP;
OS Crimean-Congo hemorrhagic fever virus (strain Nigeria/IbAr10200/1970)
OS (CCHFV).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Nairoviridae; Orthonairovirus.
OX NCBI_TaxID=652961;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9925; Capra hircus (Goat).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=34625; Hyalomma.
OH NCBI_TaxID=9940; Ovis aries (Sheep).
OH NCBI_TaxID=6941; Rhipicephalus microplus (Cattle tick) (Boophilus microplus).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=12072526; DOI=10.1128/jvi.76.14.7263-7275.2002;
RA Sanchez A.J., Vincent M.J., Nichol S.T.;
RT "Characterization of the glycoproteins of Crimean-Congo hemorrhagic fever
RT virus.";
RL J. Virol. 76:7263-7275(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RA Sanchez A.J., Vincent M.J., Deyde V.M., Khristova M.L., Nichol S.T.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PTM.
RX PubMed=17898072; DOI=10.1128/jvi.01647-07;
RA Bergeron E., Vincent M.J., Nichol S.T.;
RT "Crimean-Congo hemorrhagic fever virus glycoprotein processing by the
RT endoprotease SKI-1/S1P is critical for virus infectivity.";
RL J. Virol. 81:13271-13276(2007).
RN [4]
RP FUNCTION.
RX PubMed=19088291; DOI=10.1099/vir.0.006387-0;
RA Simon M., Johansson C., Mirazimi A.;
RT "Crimean-Congo hemorrhagic fever virus entry and replication is clathrin-,
RT pH- and cholesterol-dependent.";
RL J. Gen. Virol. 90:210-215(2009).
CC -!- FUNCTION: Glycoprotein C and glycoprotein N interact with each other
CC and are present at the surface of the virion. They are able to attach
CC the virion to host cell receptors. This attachment induces virion
CC internalization predominantly through clathrin-dependent endocytosis.
CC Also promotes fusion of viral membrane with host endosomal membrane
CC after endocytosis of the virion (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:19088291}.
CC -!- SUBUNIT: Glycoprotein C and Glycoprotein N interact with each other.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Host endoplasmic reticulum membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Note=Interaction
CC between Glycoprotein C and Glycoprotein N is essential for proper
CC targeting of Glycoprotein C to the Golgi complex, where virion budding
CC occurs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000305}. Host Golgi apparatus
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC -!- PTM: Specific enzymatic cleavages in vivo yield mature proteins
CC including glycoprotein C and glycoprotein N.
CC {ECO:0000269|PubMed:17898072}.
CC -!- SIMILARITY: Belongs to the nairovirus envelope glycoprotein family.
CC {ECO:0000305}.
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DR EMBL; AF467768; AAM48106.1; -; Genomic_RNA.
DR PDB; 6VKF; X-ray; 2.52 A; A/B=248-515.
DR PDB; 7A59; X-ray; 2.20 A; A/B/C=1041-1561.
DR PDB; 7A5A; X-ray; 2.99 A; A/B/C/D/E/F=1041-1572.
DR PDB; 7FGF; EM; 2.80 A; A/B/C=1049-1569.
DR PDB; 7L7R; X-ray; 2.10 A; G=1041-1579.
DR PDBsum; 6VKF; -.
DR PDBsum; 7A59; -.
DR PDBsum; 7A5A; -.
DR PDBsum; 7FGF; -.
DR PDBsum; 7L7R; -.
DR BMRB; Q8JSZ3; -.
DR SMR; Q8JSZ3; -.
DR PRIDE; Q8JSZ3; -.
DR Proteomes; UP000008767; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0075512; P:clathrin-dependent endocytosis of virus by host cell; IEA:UniProtKB-KW.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0046760; P:viral budding from Golgi membrane; IDA:UniProtKB.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR002532; Hanta_Gc.
DR InterPro; IPR012487; Nairovirus_M.
DR Pfam; PF01561; Hanta_G2; 1.
DR Pfam; PF07948; Nairovirus_M; 1.
DR PIRSF; PIRSF003962; M_poly_NairoV; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Clathrin-mediated endocytosis of virus by host;
KW Fusion of virus membrane with host endosomal membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host endoplasmic reticulum; Host Golgi apparatus; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..1684
FT /note="Envelopment polyprotein"
FT /evidence="ECO:0000250"
FT /id="PRO_0000406564"
FT CHAIN 19..247
FT /note="Mucin-like variable region"
FT /evidence="ECO:0000250"
FT /id="PRO_0000406565"
FT CHAIN 248..519
FT /note="GP38"
FT /evidence="ECO:0000305|PubMed:17898072"
FT /id="PRO_0000434910"
FT CHAIN 520..842
FT /note="Glycoprotein N"
FT /evidence="ECO:0000305|PubMed:17898072"
FT /id="PRO_0000406566"
FT CHAIN 843..1040
FT /note="Non-Structural protein M"
FT /evidence="ECO:0000305|PubMed:17898072"
FT /id="PRO_0000434911"
FT CHAIN 1041..1684
FT /note="Glycoprotein C"
FT /evidence="ECO:0000305|PubMed:17898072"
FT /id="PRO_0000406567"
FT TRANSMEM 699..719
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 822..842
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 860..880
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 973..993
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 1595..1615
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 22..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 247..248
FT /note="Cleavage; by host furin-like protease"
FT /evidence="ECO:0000305|PubMed:17898072"
FT SITE 516..517
FT /note="Cleavage; by host"
FT /evidence="ECO:0000250"
FT SITE 519..520
FT /note="Cleavage; by host HHAT protease"
FT /evidence="ECO:0000305|PubMed:17898072"
FT SITE 842..843
FT /note="Cleavage; by host protease"
FT /evidence="ECO:0000305|PubMed:17898072"
FT SITE 1037..1038
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT SITE 1040..1041
FT /note="Cleavage; by host protease"
FT /evidence="ECO:0000305|PubMed:17898072"
FT CARBOHYD 25
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 196
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 200
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 426
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 557
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 755
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1054
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1345
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1563
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT HELIX 257..271
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 346..355
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 360..364
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 401..408
FT /evidence="ECO:0007829|PDB:6VKF"
FT TURN 409..412
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 425..429
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 432..435
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 437..443
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 454..463
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 465..473
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 474..476
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 480..491
FT /evidence="ECO:0007829|PDB:6VKF"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:6VKF"
FT STRAND 497..507
FT /evidence="ECO:0007829|PDB:6VKF"
FT HELIX 1061..1065
FT /evidence="ECO:0007829|PDB:7A59"
FT HELIX 1067..1069
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1080..1082
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1090..1096
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1099..1111
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1116..1122
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1131..1153
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1156..1167
FT /evidence="ECO:0007829|PDB:7L7R"
FT HELIX 1171..1174
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1177..1179
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1181..1186
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1193..1195
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1204..1215
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1220..1239
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1245..1248
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1253..1257
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1260..1264
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1276..1281
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1284..1286
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1289..1294
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1297..1300
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1317..1321
FT /evidence="ECO:0007829|PDB:7L7R"
FT TURN 1324..1326
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1327..1333
FT /evidence="ECO:0007829|PDB:7L7R"
FT HELIX 1337..1340
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1346..1349
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1355..1359
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1367..1372
FT /evidence="ECO:0007829|PDB:7L7R"
FT HELIX 1378..1387
FT /evidence="ECO:0007829|PDB:7L7R"
FT HELIX 1391..1394
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1395..1403
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1406..1408
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1410..1419
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1423..1436
FT /evidence="ECO:0007829|PDB:7L7R"
FT STRAND 1446..1460
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1462..1469
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1471..1484
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1487..1489
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1493..1499
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1505..1513
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1516..1522
FT /evidence="ECO:0007829|PDB:7A59"
FT HELIX 1523..1527
FT /evidence="ECO:0007829|PDB:7A59"
FT TURN 1533..1535
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1536..1541
FT /evidence="ECO:0007829|PDB:7A59"
FT STRAND 1558..1561
FT /evidence="ECO:0007829|PDB:7A59"
SQ SEQUENCE 1684 AA; 186589 MW; 7CEAB4B46F74F578 CRC64;
MHISLMYAIL CLQLCGLGET HGSHNETRHN KTDTMTTPGD NPSSEPPVST ALSITLDPST
VTPTTPASGL EGSGEVYTSP PITTGSLPLS ETTPELPVTT GTDTLSAGDV DPSTQTAGGT
SAPTVRTSLP NSPSTPSTPQ DTHHPVRNLL SVTSPGPDET STPSGTGKES SATSSPHPVS
NRPPTPPATA QGPTENDSHN ATEHPESLTQ SATPGLMTSP TQIVHPQSAT PITVQDTHPS
PTNRSKRNLK MEIILTLSQG LKKYYGKILR LLQLTLEEDT EGLLEWCKRN LGLDCDDTFF
QKRIEEFFIT GEGHFNEVLQ FRTPGTLSTT ESTPAGLPTA EPFKSYFAKG FLSIDSGYYS
AKCYSGTSNS GLQLINITRH STRIVDTPGP KITNLKTINC INLKASIFKE HREVEINVLL
PQVAVNLSNC HVVIKSHVCD YSLDIDGAVR LPHIYHEGVF IPGTYKIVID KKNKLNDRCT
LFTDCVIKGR EVRKGQSVLR QYKTEIRIGK ASTGSRRLLS EEPSDDCISR TQLLRTETAE
IHGDNYGGPG DKITICNGST IVDQRLGSEL GCYTINRVRS FKLCENSATG KNCEIDSVPV
KCRQGYCLRI TQEGRGHVKL SRGSEVVLDA CDTSCEIMIP KGTGDILVDC SGGQQHFLKD
NLIDLGCPKI PLLGKMAIYI CRMSNHPKTT MAFLFWFSFG YVITCILCKA IFYLLIIVGT
LGKRLKQYRE LKPQTCTICE TTPVNAIDAE MHDLNCSYNI CPYCASRLTS DGLARHVIQC
PKRKEKVEET ELYLNLERIP WVVRKLLQVS ESTGVALKRS SWLIVLLVLF TVSLSPVQSA
PIGQGKTIEA YRAREGYTSI CLFVLGSILF IVSCLMKGLV DSVGNSFFPG LSICKTCSIS
SINGFEIESH KCYCSLFCCP YCRHCSTDKE IHKLHLSICK KRKKGSNVML AVCKLMCFRA
TMEVSNRALF IRSIINTTFV LCILILAVCV VSTSAVEMEN LPAGTWEREE DLTNFCHQEC
QVTETECLCP YEALVLRKPL FLDSTAKGMK NLLNSTSLET SLSIEAPWGA INVQSTYKPT
VSTANIALSW SSVEHRGNKI LVSGRSESIM KLEERTGISW DLGVEDASES KLLTVSVMDL
SQMYSPVFEY LSGDRQVGEW PKATCTGDCP ERCGCTSSTC LHKEWPHSRN WRCNPTWCWG
VGTGCTCCGL DVKDLFTDYM FVKWKVEYIK TEAIVCVELT SQERQCSLIE AGTRFNLGPV
TITLSEPRNI QQKLPPEIIT LHPRIEEGFF DLMHVQKVLS ASTVCKLQSC THGVPGDLQV
YHIGNLLKGD KVNGHLIHKI EPHFNTSWMS WDGCDLDYYC NMGDWPSCTY TGVTQHNHAS
FVNLLNIETD YTKNFHFHSK RVTAHGDTPQ LDLKARPTYG AGEITVLVEV ADMELHTKKI
EISGLKFASL ACTGCYACSS GISCKVRIHV DEPDELTVHV KSDDPDVVAA SSSLMARKLE
FGTDSTFKAF SAMPKTSLCF YIVEREHCKS CSEEDTKKCV NTKLEQPQSI LIEHKGTIIG
KQNSTCTAKA SCWLESVKSF FYGLKNMLSG IFGNVFMGIF LFLAPFILLI LFFMFGWRIL
FCFKCCRRTR GLFKYRHLKD DEETGYRRII EKLNNKKGKN KLLDGERLAD RRIAELFSTK
THIG
