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   08-NOV-2023, entry version 105.
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   Orthobunyavirus khatangaense.
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}.
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DR   EMBL; K02539; AAA47827.1; -; Genomic_RNA.
DR   EMBL; J02392; -; NOT_ANNOTATED_CDS; Genomic_RNA.
DR   PIR; A04102; GNVUSV.
DR   SMR; P04875; -.
DR   GlyCosmos; P04875; 3 sites, No reported glycans.
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:0016020; C: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   NCBIfam; TIGR04210; bunya_NSm; 1.
DR   Pfam; PF03557; Bunya_G1; 1.
DR   Pfam; PF03563; Bunya_G2; 1.
DR   PIRSF; PIRSF003944; M_poly_OrthobunV; 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
//