GP_BUNL7
ID GP_BUNL7 Reviewed; 1441 AA.
AC P09612;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Envelopment polyprotein;
DE AltName: Full=M polyprotein;
DE Contains:
DE RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P04505};
DE Short=Gn;
DE AltName: Full=Glycoprotein G2;
DE Contains:
DE RecName: Full=Non-structural protein M {ECO:0000250|UniProtKB:P04505};
DE Short=NSm;
DE Contains:
DE RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P04505};
DE Short=Gc;
DE AltName: Full=Glycoprotein G1;
DE Flags: Precursor;
GN Name=GP;
OS Bunyavirus La Crosse (isolate Aedes triseriatus/United States/L74/1974).
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC La Crosse orthobunyavirus.
OX NCBI_TaxID=11578;
OH NCBI_TaxID=9850; Cervidae (deer).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=7162; Ochlerotatus triseriatus (Eastern treehole mosquito) (Aedes triseriatus).
OH NCBI_TaxID=13712; Tamias.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=3694177; DOI=10.1099/0022-1317-68-12-3057;
RA Grady L.J., Sanders M.L., Campbell W.P.;
RT "The sequence of the M RNA of an isolate of La Crosse virus.";
RL J. Gen. Virol. 68:3057-3071(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 1-46.
RX PubMed=7086954; DOI=10.1128/jvi.41.1.119-128.1982;
RA Clerx-Van Haaster C.M., Akashi H., Auperin D.D., Bishop D.H.L.;
RT "Nucleotide sequence analyses and predicted coding of bunyavirus genome RNA
RT species.";
RL J. Virol. 41:119-128(1982).
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 a cell receptor and to promote fusion of membranes after
CC endocytosis of the virion (By similarity). {ECO:0000250}.
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=Glycoprotein C
CC alone is retained in the membrane of the endoplasmic reticulum, but not
CC transported to the Golgi. Coexpression of Glycoprotein C and
CC Glycoprotein N results in efficient transport of Glycoprotein C to the
CC Golgi complex, indicating thattheir interaction is essential for proper
CC targeting to this organelle, where virion budding occurs (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Glycoprotein N]: 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}. Note=Glycoprotein N is retained in the Golgi complex
CC through a Golgi retention signal, which resides in the Glycoprotein N
CC transmembrane region. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Non-structural protein M]: 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 nonstructural protein NSm, glycoprotein C, and glycoprotein
CC N.
CC -!- SIMILARITY: Belongs to the orthobunyavirus envelope glycoprotein
CC family. {ECO:0000305}.
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DR EMBL; D10370; BAA01201.1; -; Genomic_RNA.
DR EMBL; J02231; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; A29377; GNVULC.
DR SMR; P09612; -.
DR TCDB; 1.G.20.1.4; the hantavirus gc envelope fusion glycoprotein (gc-efg) family.
DR PRIDE; P09612; -.
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:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR GO; GO:0019048; P:modulation by virus of host process; IEA:InterPro.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR InterPro; IPR005167; Bunya_G1.
DR InterPro; IPR005168; Bunya_G2.
DR InterPro; IPR026400; Bunya_nonstruc_pro_NSm.
DR InterPro; IPR014413; M_poly_OrthobunV.
DR Pfam; PF03557; Bunya_G1; 1.
DR Pfam; PF03563; Bunya_G2; 1.
DR PIRSF; PIRSF003944; M_poly_OrthobunV; 1.
DR TIGRFAMs; TIGR04210; bunya_NSm; 1.
PE 3: Inferred from homology;
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; Signal; Transmembrane;
KW Transmembrane helix; Viral attachment to host cell;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..13
FT /evidence="ECO:0000255"
FT CHAIN 14..1441
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036790"
FT CHAIN 22..299
FT /note="Glycoprotein N"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036791"
FT CHAIN 300..473
FT /note="Non-structural protein M"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036792"
FT CHAIN 474..1441
FT /note="Glycoprotein C"
FT /evidence="ECO:0000250"
FT /id="PRO_0000036793"
FT TOPO_DOM 14..200
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..365
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..1395
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 1396..1416
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1417..1441
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT SITE 473..474
FT /note="Cleavage; by host signal peptidase"
FT /evidence="ECO:0000250"
FT CARBOHYD 57
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 490
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 1177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CONFLICT 40
FT /note="C -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1441 AA; 162541 MW; 50973CE30973C55B CRC64;
MIRMLVLIVV TAASPVYQRC FQDGAIVKQN PSKEAVTEVC LKDDVSMIKT EARYVKNATG
VFSNNVAIRK WLVSDWHDCR PKKIVGGHIN VIEVGDDLSL HTESYVCSAD CTIGVDKETA
QVRLQTDTTN HFEIAGTTVK SGWFKSTTYI TLDQTCEHLK VSCAPKSVQF HACFNQHMSC
VRFLHRTILP GSIANSICQN IEIIILVTLT LLIFILLSIL SKTYICYLLM PIFIPIAYMY
GVIYNKSCKK CKLCGLVYHP FTECGTHCVC GARYDTSDRM KLHRASGLCP GYKSLRAARV
MCKSKGPASI LSIITAVLVL TFVTPINSMV LGESKETFEL EELPDDMLEM ALRINSYYFT
CILNYAVSWG LIIAGLLVGL IFKKYQHRFL NIYAMYCEEC NMYHDKSGLK RHGDFTNKCR
QCTCGQYEDA TGLITHRKTY NCLVQYKAKW MMNFLIIYIF LILIKDSAIV GQATGTDFTT
CLETESINWN CTGPFLNLGN CQKQQKKEPY TNIATQLKGL KAISVLDIPI ITSIPDDIAG
ALRYIEEKED FHVQLTTEYA MLSKYCDYYT QFSDNSGYSQ TTWRVYLRSH DFEACILYPN
QHFCKCVKNG EKCSSSNWDF ANGMKNYYSG KQAKFDKDLN LALTALHHAF RGTSSAYIAA
MLSKKSNDDL IAYTNKIKAK FPGNALLKAI IDYIAYMKGL PEMANFKYDE FWDELLYKPN
PAKASNLARG KESSYNFKLA ISSKSIKTCK NVKDVACLSP RSGAIYSSII ACGEPNGPSV
YRKPSGGVFQ SSTDRSIYCL LDSHCLEEFE AISQEELDAV KKSKCWEIEY PDVRPLQESD
GAKSCRMKDS GNCNVATNRW PVMQCENDKF YYSELQKDYD KTQDIGHYCL SPGCTTIRYP
INPKHISNCN WQVSRSSIAK IDVHNVEDIE QYKKAITQKL QTSLSLFKYA KTKNLPHIRP
IYKYITMKET ETAEGIESAY IESEVPALAG TSVGFKINSK EGKHLLDVIA YVKSASYSSV
YAKLYSTGPT SGINTKHDEL CTGPCPANIN HQVGWLTFAR ERTSSWGCEE FGCLAVSDGC
VFGSCQDIIK EELSVYRKET EEVTNVELCL TFSDKTYCTN LNPVTPIITD LFEVQFKTVE
TYSLPRIVAV QNHEIKIGQI NDLGVYSKGC GNVQKVNGTV YGNGVPRFDY LCHLASRKEV
IVRKCFDNDY QACKFLQSPA SYRLEEDSGT VTIIDYKKIL GTIKMKAILG DVKYKTFADS
VDITAEGSCA GCINCFQNIH CELTLHTTIE ASCPIKSSCT VFHDRILVTP NEHKYALKIV
CTEKPGNTLT IKVCNTRIEA SMALVDAKPI IELAPVDQTA YIREKDERCK TWMCRVRDEG
LQVILEPFKN LFGSYIGIFY TFIISIIALL VIIYVLLPIC FKLRDTLRKH DDAYKREMKI
R
