ID   GP_PUUMS                Reviewed;        1148 AA.
AC   P27312; I4EPA4;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   24-JAN-2024, entry version 118.
DE   RecName: Full=Envelopment polyprotein;
DE   AltName: Full=M polyprotein;
DE   Contains:
DE     RecName: Full=Glycoprotein N {ECO:0000250|UniProtKB:P08668};
DE              Short=Gn;
DE     AltName: Full=Glycoprotein G1;
DE   Contains:
DE     RecName: Full=Glycoprotein C {ECO:0000250|UniProtKB:P08668};
DE              Short=Gc;
DE     AltName: Full=Glycoprotein G2;
DE   Flags: Precursor;
GN   Name=GP;
OS   Puumala virus (strain Sotkamo/V-2969/81).
OC   Viruses; Riboviria; Orthornavirae; Negarnaviricota; Polyploviricotina;
OC   Ellioviricetes; Bunyavirales; Hantaviridae; Mammantavirinae;
OC   Orthohantavirus; Orthohantavirus puumalaense.
OX   NCBI_TaxID=39002;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=447135; Myodes glareolus (Bank vole) (Clethrionomys glareolus).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RX   PubMed=1353107; DOI=10.1099/0022-1317-73-4-829;
RA   Vapalahti O.P., Kallio-Kokko H., Salonen E.M., Brummer-Korvenkontio M.,
RA   Vaheri A.;
RT   "Cloning and sequencing of Puumala virus Sotkamo strain S and M RNA
RT   segments: evidence for strain variation in hantaviruses and expression of
RT   the nucleocapsid protein.";
RL   J. Gen. Virol. 73:829-838(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC RNA].
RC   STRAIN=Isolate Sotkamo 2009/WHO Arbovirus collection;
RX   PubMed=22798055; DOI=10.1007/s11262-012-0780-3;
RA   Kurolt I.C., Paessler S., Markotic A.;
RT   "Resequencing of the Puumala virus strain Sotkamo from the WHO Arbovirus
RT   collection.";
RL   Virus Genes 45:389-392(2012).
RN   [3]
RP   DOMAIN (GLYCOPROTEIN N), INTERACTION WITH THE NUCLEOPROTEIN (GLYCOPROTEIN
RP   N), DOMAIN (GLYCOPROTEIN C), AND INTERACTION WITH THE NUCLEOPROTEIN
RP   (GLYCOPROTEIN C).
RX   PubMed=20444994; DOI=10.1099/vir.0.021006-0;
RA   Hepojoki J., Strandin T., Wang H., Vapalahti O., Vaheri A., Lankinen H.;
RT   "Cytoplasmic tails of hantavirus glycoproteins interact with the
RT   nucleocapsid protein.";
RL   J. Gen. Virol. 91:2341-2350(2010).
RN   [4]
RP   FUNCTION (GLYCOPROTEIN N), AND DOMAIN (GLYCOPROTEIN N).
RX   PubMed=21807393; DOI=10.1016/j.virol.2011.06.030;
RA   Strandin T., Hepojoki J., Wang H., Vaheri A., Lankinen H.;
RT   "The cytoplasmic tail of hantavirus Gn glycoprotein interacts with RNA.";
RL   Virology 418:12-20(2011).
RN   [5]
RP   REVIEW.
RX   PubMed=24755564; DOI=10.3390/v6041801;
RA   Cifuentes-Munoz N., Salazar-Quiroz N., Tischler N.D.;
RT   "Hantavirus Gn and Gc envelope glycoproteins: key structural units for
RT   virus cell entry and virus assembly.";
RL   Viruses 6:1801-1822(2014).
RN   [6]
RP   SUBUNIT (GLYCOPROTEIN N), SUBUNIT (GLYCOPROTEIN C), SUBCELLULAR LOCATION
RP   (GLYCOPROTEIN N), SUBCELLULAR LOCATION (GLYCOPROTEIN C), AND DOMAIN
RP   (GLYCOPROTEIN C).
RX   PubMed=30679542; DOI=10.1038/s41598-018-36879-y;
RA   Sperber H.S., Welke R.W., Petazzi R.A., Bergmann R., Schade M., Shai Y.,
RA   Chiantia S., Herrmann A., Schwarzer R.;
RT   "Self-association and subcellular localization of Puumala hantavirus
RT   envelope proteins.";
RL   Sci. Rep. 9:707-707(2019).
CC   -!- FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at
CC       the surface of the virion (By similarity). Attaches the virion to host
CC       cell receptors including integrin ITGAV/ITGB3 (By similarity). This
CC       attachment induces virion internalization predominantly through
CC       clathrin-dependent endocytosis (By similarity). Mediates the assembly
CC       and budding of infectious virus particles through its interaction with
CC       the nucleocapsid protein and the viral genome (PubMed:24755564). May
CC       dysregulate normal immune and endothelial cell responses through an
CC       ITAM motif (By similarity). Translocates to mitochondria, binds to host
CC       TUFM and recruits MAP1LC3B (By similarity). These interactions induce
CC       mitochondrial autophagy and therefore destruction of host MAVS leading
CC       to inhibition of type I interferon (IFN) responses (By similarity).
CC       Concomitant breakdown of glycoprotein N is apparently prevented by the
CC       nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome
CC       fusion (By similarity). Interacts with the viral genomic RNA
CC       (PubMed:21807393). {ECO:0000250|UniProtKB:P08668,
CC       ECO:0000269|PubMed:21807393, ECO:0000303|PubMed:24755564}.
CC   -!- FUNCTION: [Glycoprotein C]: Forms heterooctamers with glycoprotein N at
CC       the surface of the virion. Attaches the virion to host cell receptors
CC       including integrin ITGAV/ITGB3. This attachment induces virion
CC       internalization predominantly through clathrin-dependent endocytosis.
CC       Class II fusion protein that promotes fusion of viral membrane with
CC       host endosomal membrane after endocytosis of the virion.
CC       {ECO:0000250|UniProtKB:P08668}.
CC   -!- SUBUNIT: [Glycoprotein N]: Homodimer (PubMed:30679542). Homotetramer;
CC       forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By
CC       similarity). Interacts (via C-terminus) with the nucleoprotein
CC       (PubMed:20444994). Interacts with host TUFM; this interaction
CC       contributes to the virus-induced degradation of mitochondria by
CC       autophagy, which leads to degradation of host MAVS and inhibition of
CC       type I interferon (IFN) responses (By similarity). Interacts with host
CC       MAP1LC3B; this interaction contributes to the virus-induced degradation
CC       of mitochondria by autophagy, which leads to degradation of host MAVS
CC       and inhibition of type I interferon (IFN) responses (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000269|PubMed:20444994,
CC       ECO:0000269|PubMed:30679542}.
CC   -!- SUBUNIT: [Glycoprotein C]: Homodimer (PubMed:30679542). Homotetramer;
CC       forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation
CC       (PubMed:30679542). Homotrimer; forms homotrimer in the post-fusion
CC       conformation at acidic pH (By similarity). Interacts (via C-terminus)
CC       with the nucleoprotein (PubMed:20444994).
CC       {ECO:0000250|UniProtKB:P41266, ECO:0000269|PubMed:20444994,
CC       ECO:0000269|PubMed:30679542}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08668}; Multi-pass membrane protein
CC       {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:30679542}. Host
CC       Golgi apparatus membrane {ECO:0000269|PubMed:30679542}; Multi-pass
CC       membrane protein {ECO:0000250|UniProtKB:P08668}. Host endoplasmic
CC       reticulum membrane {ECO:0000269|PubMed:30679542}; Multi-pass membrane
CC       protein {ECO:0000250|UniProtKB:P08668}. Host mitochondrion
CC       {ECO:0000250|UniProtKB:P08668}. Note=Interaction between glycoprotein N
CC       and glycoprotein C is essential for proper targeting of glycoprotein N
CC       to the host Golgi complex, where virion budding occurs.
CC       {ECO:0000269|PubMed:30679542}.
CC   -!- SUBCELLULAR LOCATION: [Glycoprotein C]: Virion membrane
CC       {ECO:0000250|UniProtKB:P08668}; Single-pass membrane protein. Host cell
CC       surface {ECO:0000269|PubMed:30679542}. Host Golgi apparatus membrane
CC       {ECO:0000269|PubMed:30679542}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08668}. Host endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:30679542}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P08668}. Note=Budding probably takes place at
CC       the host Golgi (Probable). Glycoprotein C cytoplasmic tail is important
CC       for efficient Golgi localization (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000305}.
CC   -!- DOMAIN: [Glycoprotein N]: The YxxL motif at the C-terminus is
CC       indispensable for the interaction with MAP1LC3B and for the Gn-mediated
CC       induction of mitochondrial autophagy (By similarity). The cytoplasmic
CC       tail is involved in the inhibition of the host innate immune response
CC       (By similarity). The C-terminus of the cytoplasmic tail is involved in
CC       binding to the viral genome and the nucleocapsid (Probable)
CC       (PubMed:20444994). Contains 2 contiguous zinc-fingers (By similarity).
CC       {ECO:0000250|UniProtKB:P08668, ECO:0000250|UniProtKB:P0DTJ1,
CC       ECO:0000250|UniProtKB:Q9E006, ECO:0000269|PubMed:20444994,
CC       ECO:0000305|PubMed:21807393}.
CC   -!- DOMAIN: [Glycoprotein C]: The C-terminus is necessary for proper
CC       localization in the Golgi (PubMed:30679542). The cytoplasmic tail is
CC       involved in binding to the nucleocapsid (PubMed:20444994).
CC       {ECO:0000269|PubMed:20444994, ECO:0000269|PubMed:30679542}.
CC   -!- PTM: [Envelopment polyprotein]: Envelope polyprotein precursor is
CC       quickly cleaved in vivo just after synthesis, presumably by host signal
CC       peptidase. {ECO:0000250|UniProtKB:P08668}.
CC   -!- SIMILARITY: Belongs to the hantavirus envelope glycoprotein family.
CC       {ECO:0000305}.
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DR   EMBL; X61034; CAA43369.1; -; Genomic_RNA.
DR   EMBL; HE801634; CCH22848.1; -; Genomic_RNA.
DR   PIR; JQ1604; JQ1604.
DR   RefSeq; NP_941983.1; NC_005223.1.
DR   SMR; P27312; -.
DR   GlyCosmos; P27312; 4 sites, No reported glycans.
DR   KEGG; vg:2943082; -.
DR   Proteomes; UP000008482; Genome.
DR   Proteomes; UP000110237; 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:0033650; C:host cell mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0044228; C:host cell surface; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR   GO; GO:0039527; P:disruption by virus of host TRAF-mediated signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   GO; GO:0039503; P:suppression by virus of host innate immune response; IEA:UniProtKB-KW.
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   Gene3D; 1.10.8.1320; -; 1.
DR   InterPro; IPR016402; Envelope_glycoprot_Hantavirus.
DR   InterPro; IPR048791; Gc_C_bunya.
DR   InterPro; IPR048790; Gn-B_hanta.
DR   InterPro; IPR002532; Hanta_Gc_N.
DR   InterPro; IPR002534; Hanta_Gn-H.
DR   InterPro; IPR012316; ITAM_motif_hantavir-typ.
DR   Pfam; PF20682; Hanta_Gc_C; 1.
DR   Pfam; PF01561; Hanta_Gc_N; 1.
DR   Pfam; PF20679; Hanta_Gn-B; 1.
DR   Pfam; PF01567; Hanta_Gn-H; 1.
DR   Pfam; PF10538; ITAM_Cys-rich; 1.
DR   PIRSF; PIRSF003945; M_poly_HantaV; 1.
DR   PROSITE; PS51056; ITAM_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; 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 mitochondrion; Host-virus interaction;
KW   Inhibition of host innate immune response by virus;
KW   Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus;
KW   Membrane; Metal-binding; Phosphoprotein; Repeat; Signal; Transmembrane;
KW   Transmembrane helix; Viral attachment to host cell; Viral immunoevasion;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell;
KW   Zinc; Zinc-finger.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..1148
FT                   /note="Envelopment polyprotein"
FT                   /id="PRO_0000036831"
FT   CHAIN           24..658
FT                   /note="Glycoprotein N"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036832"
FT   CHAIN           659..1148
FT                   /note="Glycoprotein C"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000036833"
FT   TOPO_DOM        24..496
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        518..637
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        638..658
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        659..1115
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        1116..1136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        1137..1148
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          621..644
FT                   /note="ITAM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00379"
FT   ZN_FING         555..575
FT                   /note="CCHC-type 1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   ZN_FING         580..601
FT                   /note="CCHC-type 2"
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   REGION          526..543
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000269|PubMed:20444994"
FT   REGION          598..615
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000269|PubMed:20444994"
FT   REGION          621..635
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000269|PubMed:20444994"
FT   REGION          767..787
FT                   /note="Fusion loop"
FT                   /evidence="ECO:0000250|UniProtKB:P41266"
FT   REGION          1131..1148
FT                   /note="Binding to the ribonucleoprotein"
FT                   /evidence="ECO:0000269|PubMed:20444994"
FT   MOTIF           625..628
FT                   /note="YxxL"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   SITE            658..659
FT                   /note="Cleavage; by host signal peptidase"
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   CARBOHYD        142
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        357
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        409
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        937
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000250|UniProtKB:P41266"
FT   DISULFID        34..159
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        68..165
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        117..136
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        141..146
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        183..193
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        218..257
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        386..445
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        390..399
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        415..434
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        462..485
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   DISULFID        745..780
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        749..787
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        761..894
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        775..905
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        790..913
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        816..825
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        833..842
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        873..877
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        979..1009
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1002..1054
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1019..1024
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1055..1060
FT                   /evidence="ECO:0000250|UniProtKB:P08668"
FT   DISULFID        1094..1098
FT                   /evidence="ECO:0000250|UniProtKB:Q9E006"
FT   VARIANT         25
FT                   /note="K -> R (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         472
FT                   /note="M -> L (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         536
FT                   /note="R -> K (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         665
FT                   /note="D -> A (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         822
FT                   /note="G -> E (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         953
FT                   /note="L -> P (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         988
FT                   /note="T -> I (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         1020
FT                   /note="H -> D (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
FT   VARIANT         1145
FT                   /note="D -> E (in strain: isolate Sotkamo 2009/WHOArbovirus
FT                   collection)"
SQ   SEQUENCE   1148 AA;  126294 MW;  BA606F74979EE73F CRC64;
     MGKSSPVCLY LILQGLLLFD TVNAKNLNEL KMECPHTIGL GQGLVVGSVE LPPVPIQQIE
     SLKLESSCNF DLHTSTAGQQ SFTKWTWETK GDLAENTQAS STSFQTKSSE VNLRGLCLIP
     TLVVETAARM RKTIACYDLS CNQTVCQPTV YLMGPIQTCL TTKSCLLGLG DQRIQVNYER
     TYCVSGQLVE GVCFNPIHTM ALSQPSHTYD IVTIMVRCFL VIKKVTSGDS MKIEKNFETL
     VQKTGCTANG FQGYYICLIG SSSEPLYVPT LDDYRSAEVL SRMAFAPHGE DHDIEKNAVS
     ALRIAGKVTG KAPSTESSDT VQGIAFSGSP LYTSTGVLTA KDDPVYVWAP GIIMEGNHSV
     CEKKTLPLTW TGFIPLPGEI EKTTQCTVFC TLAGPGADCE AYSETGIFNI SSPTCLINRV
     QRFRGAEQQI KFVCQRVDMD ITVYCNGVKK VILTKTLVIG QCIYTFTSIF SMIPGIAHSL
     AVELCVPGLH GWATVLLLLT FCFGWVLIPT ITMILLKILI AFAYLCSKYN TDSKFRILVE
     KVKKEYQKTM GSMVCEVCQY ECETAKELES HRKSCSIGSC PYCLNPSEAT PSALQAHFKV
     CKLTSRFQEN LKKSLTMYEP MQGCYRTLSL FRYRSRFFVG LVWCMLLVLE LIVWAASAET
     QNLNDGWTDT AHGSGIIPMK ADLELDFSLP SSASYTYRRQ LQNPANEQEK IPFHLQISKQ
     VIHAEIQHLG HWMDATFNLK TAFHCYGSCE KYAYPWQTAG CFVEKDYEYE TGWGCNPPDC
     PGVGTGCTAC GVYLDKLKSV GKVFKIVSLR YTRKVCIQLG TGQTCKTVDS NDCLITTSVK
     VCLIGTISKF QPSDTLLFLG PLQQGGLIFK QWCTTTCQFG DPGDIMSTPT GMKCPELNGS
     FRKKCAFATT PVCQFDGNTI SGYKRMVATK DSFQSFNVTE PHISTSALEW IDLDSSLRDH
     INVIVSRDLS FQDLSETPCQ VDLTTSATDG AWGSGVGFNL VCTVSLTECS AFLTSIKACH
     AAMCYGSTTT NLVRGQNTIH VVGKGGHSGS KFMCCHDTKC SSTGLVAAAP HLDRVTGFNQ
     ADSDKIFDDG APECGMSCWF KKLGEWVLGV LNGNWMVVAV LIALLILSIF LFALCCPRRP
     SYKKDHKP
//