GP_BUNSH
ID GP_BUNSH Reviewed; 1441 AA.
AC P04875;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 snowshoe hare.
OC Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC Ellioviricetes; Bunyavirales; Peribunyaviridae; Orthobunyavirus;
OC Snowshoe hare orthobunyavirus.
OX NCBI_TaxID=11580;
OH NCBI_TaxID=7158; Aedes.
OH NCBI_TaxID=9913; Bos taurus (Bovine).
OH NCBI_TaxID=9615; Canis lupus familiaris (Dog) (Canis familiaris).
OH NCBI_TaxID=7174; Culex.
OH NCBI_TaxID=174825; Culiseta.
OH NCBI_TaxID=9796; Equus caballus (Horse).
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=48086; Lepus americanus (Snowshoe hare).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX PubMed=6091326; DOI=10.1016/0042-6822(84)90215-0;
RA Eshita Y., Bishop D.H.L.;
RT "The complete sequence of the M RNA of snowshoe hare bunyavirus reveals the
RT presence of internal hydrophobic domains in the viral glycoprotein.";
RL Virology 137:227-240(1984).
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).
RN [3]
RP PROTEOLYTIC PROCESSING OF POLYPROTEIN.
RX PubMed=2974218;
RA Fazakerley J.K., Gonzalez-Scarano F., Strickler J., Dietz-Schold B.,
RA Karush F., Nathanson N.;
RT "Organization of the middle RNA segment of snowshoe hare Bunyavirus.";
RL Virology 167:422-432(1988).
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 that their interaction is essential for
CC proper 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K02539; AAA47827.1; -; Genomic_RNA.
DR EMBL; J02392; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR PIR; A04102; GNVUSV.
DR SMR; P04875; -.
DR PRIDE; P04875; -.
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 1: Evidence at protein level;
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 CHAIN 14..1441
FT /note="Envelopment polyprotein"
FT /id="PRO_0000036794"
FT CHAIN 14..299
FT /note="Glycoprotein N"
FT /id="PRO_0000036795"
FT CHAIN 300..473
FT /note="Non-structural protein M"
FT /id="PRO_0000036796"
FT CHAIN 474..1441
FT /note="Glycoprotein C"
FT /id="PRO_0000036797"
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"
SQ SEQUENCE 1441 AA; 162390 MW; 51F01DB268D1A08B CRC64;
MICILILFAV TAASPVYQRC FQDGAIVKQN PSKEAVTEVC LKDDVSMIKT EARYIKNATG
VFSNNVAIRK WLVSDWHDCR PKKITGGHIN VIEVGDDLSL HTESYVCSAD CTIGVDKETA
QVRLQTDTTN HFEIAGTIVK SGWFKSTTYI TLDQTCEHLK VSCGPKSIQF HACFNQHMSC
VRFLHRTILP GSIANSICQN IEIIILVTLT LLIFILLSVL SKTYICYLLM PVFIPIAYAY
GIIYNKSCKK CKLCGLVYHP FTECGTHCVC GARYDTSDRM KLHRASGLCP GYKSLRAARV
MCKSKGPASI LSVITAILIL TFVTPINSMV VGESKEVFEL EQLPDDMLDM ALRINFYYFV
CIMNYAVTWG LIIIGLLIGL LFKKYQHRFS NLYAMYCEEC DMYHDRSGLK RNGDFTNKCR
QCTCGQYEDA TGLMTHRKTY NCLVRYKAKW VMNFLIAYML LTLIKDSAIV VQAAGTDFTT
CLETENINWN CTGPFLNLGN CQKQQKKEPY ANIATQLKGL QAISVLDMPM IASIPEDIAG
ALRYIEEKET FHVQLTAEYA MLSRYCDYYA QFSDNSGYSQ TTWRVYLRSH DFDACILYPN
QHFCRCVKRG DKCSSSNGDF ANEMKNYYSG KQNKFDKDLN LALMALHHAF RGTSSAYIAT
MLSKKSNDDL IAYTNKIKEK FPGNALLKAI VDYIAYMKSL SEMSSFKYDE FWDDLLYKSA
PTKAPSLSRG SEPSYNFKLV VSSRSIKSCK NVKSVVCLSP RSGVSYDSII ACGDPNGPSV
YRKPSDGVFQ SNADQSTYCL ADSHCLEDFE VVSQEELDAI KKSKCWEAEY PDVKLSKLTD
GVKSCRMKDS GNCNVAANRW PIIQCENDKF YYSELQKDYD KTQDIGHFCL SPGCSTVRFP
INPKHISNCN WQVSRSSIAK IDVHNIEDID QYRKAITQKL QTSLSLFKYA KTKNLPHIKP
IYKYITIEGT ETAEGIESAY IESEIPALAG TSIGFKITSK EGKHLLDVIG YVKSASCSSI
YTKLYTTGPT SGINTKHDEL CTGPCPAKIN HQTGWLTFAK ERTSSWGCEE FGCLAISDGC
VFGSCQDIIR DELTVYRKET DEVTDVELCL TFSDKTYCTN LNPITPIITD LFEVQFKTVE
TYSLPRIVAI QNHEIKIGQV NDLGVYSKGC GNVQKVNGTV YGNGVPKFDY LCHLASRKEV
IVRKCFDNDY QACKFLQSPA SYRLEEDSGT VTVIDYKKIL GTIKMKAILG DVKYKTFADN
VDMTAEGSCT GCINCFENIH CELTLHTTIE ASCPIVSTCT VFHDRILVTP NEHKYALKVV
CTEKPGNTLT IRICNTKVEA SLALVDAKPI LELAPVDQTA YIREKDERCK TWMCRVRDEG
LQVILEPFKN LFGSYIGIFY TFIISIIALL IIIYIVLPIC FKLRDTLRKH EDAYKREMKI
R
