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UniProtKB - Q89905 (GP_SINV)

Entry version 73 (25 May 2022)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
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Protein

Envelopment polyprotein

Gene

GP

Organism
Sin Nombre orthohantavirus (SNV) (Sin Nombre virus)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Forms homotetramers with glycoprotein C at the surface of the virion (By similarity).

Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (Probable). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity).

Mediates the assembly and budding of infectious virus particles through its interaction with the nucleocapsid protein and the viral genome (By similarity).

May dysregulate normal immune and endothelial cell responses through an ITAM motif (By similarity).

Translocates to mitochondria, binds to host TUFM and recruits MAP1LC3B (By similarity).

These interactions induce mitochondrial autophagy and therefore destruction of host MAVS leading to inhibition of type I interferon (IFN) responses (By similarity).

Concomitant breakdown of glycoprotein N is apparently prevented by the nucleoprotein that may inhibit Gn-stimulated autophagosome-lysosome fusion (By similarity).

Interacts with the viral genomic RNA (By similarity).

By similarity1 Publication

Forms homotetramers with glycoprotein N at the surface of the virion (By similarity).

Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (Probable). This attachment induces virion internalization predominantly through clathrin-dependent endocytosis (By similarity).

Class II fusion protein that promotes fusion of viral membrane with host endosomal membrane after endocytosis of the virion (By similarity).

By similarity1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri549 – 569CCHC-type 1By similarityAdd BLAST21
Zinc fingeri574 – 595CCHC-type 2By similarityAdd BLAST22

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processActivation of host autophagy by virus, Fusion of virus membrane with host endosomal membrane, Fusion of virus membrane with host membrane, Host-virus interaction, Inhibition of host innate immune response by virus, Inhibition of host MAVS by virus, Inhibition of host RLR pathway by virus, Inhibition of host TRAFs by virus, Viral attachment to host cell, Viral immunoevasion, Viral penetration into host cytoplasm, Virus endocytosis by host, Virus entry into host cell
LigandMetal-binding, Zinc

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Envelopment polyprotein
Alternative name(s):
M polyprotein
Cleaved into the following 2 chains:
Glycoprotein NBy similarity
Short name:
Gn
Alternative name(s):
Glycoprotein G1
Glycoprotein CBy similarity
Short name:
Gc
Alternative name(s):
Glycoprotein G2
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GP
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSin Nombre orthohantavirus (SNV) (Sin Nombre virus)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1980491 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiViruses › Riboviria › Orthornavirae › Negarnaviricota › Polyploviricotina › Ellioviricetes › Bunyavirales › Hantaviridae › Mammantavirinae › Orthohantavirus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section only exists in viral entries and indicates the host(s) either as a specific organism or taxonomic group of organisms that are susceptible to be infected by a virus.<p><a href='/help/virus_host' target='_top'>More...</a></p>Virus hostiHomo sapiens (Human) [TaxID: 9606]
Peromyscus maniculatus (North American deer mouse) [TaxID: 10042]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000167429 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome
  • UP000113911 Componenti: Genome
  • UP000204632 Componenti: Genome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini18 – 480LumenalSequence analysisAdd BLAST463
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei490 – 510HelicalSequence analysisAdd BLAST21
Topological domaini511 – 631CytoplasmicSequence analysisAdd BLAST121
Transmembranei632 – 652HelicalSequence analysisAdd BLAST21
Topological domaini653 – 1108LumenalSequence analysisAdd BLAST456
Transmembranei1109 – 1129HelicalSequence analysisAdd BLAST21
Topological domaini1130 – 1140CytoplasmicSequence analysisAdd BLAST11

Keywords - Cellular componenti

Host endoplasmic reticulum, Host Golgi apparatus, Host membrane, Host mitochondrion, Membrane, Viral envelope protein, Virion

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 17Sequence analysisAdd BLAST17
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000045519718 – 1140Envelopment polyproteinAdd BLAST1123
ChainiPRO_000045519818 – 652Glycoprotein NAdd BLAST635
ChainiPRO_0000455199653 – 1140Glycoprotein CAdd BLAST488

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi30 ↔ 155By similarity
Disulfide bondi64 ↔ 161By similarity
Disulfide bondi113 ↔ 132By similarity
Disulfide bondi137 ↔ 142By similarity
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi138N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi179 ↔ 189By similarity
Disulfide bondi214 ↔ 251By similarity
Glycosylationi351N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi380 ↔ 439By similarity
Disulfide bondi384 ↔ 393By similarity
Glycosylationi403N-linked (GlcNAc...) asparagine; by hostSequence analysis1
Disulfide bondi409 ↔ 428By similarity
Disulfide bondi456 ↔ 479By similarity
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei619PhosphotyrosinePROSITE-ProRule annotation1
Modified residuei632PhosphotyrosinePROSITE-ProRule annotation1
Disulfide bondi739 ↔ 774By similarity
Disulfide bondi743 ↔ 781By similarity
Disulfide bondi755 ↔ 888By similarity
Disulfide bondi769 ↔ 899By similarity
Disulfide bondi784 ↔ 907By similarity
Disulfide bondi810 ↔ 819By similarity
Disulfide bondi827 ↔ 836By similarity
Disulfide bondi867 ↔ 871By similarity
Glycosylationi931N-linked (GlcNAc...) asparagine; by hostBy similarity1
Disulfide bondi973 ↔ 1003By similarity
Disulfide bondi996 ↔ 1048By similarity
Disulfide bondi1013 ↔ 1018By similarity
Disulfide bondi1049 ↔ 1054By similarity
Disulfide bondi1088 ↔ 1092By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Envelope polyprotein precursor is quickly cleaved in vivo just after synthesis, presumably by host signal peptidase.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei652 – 653Cleavage; by host signal peptidaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (By similarity). Homotetramer; forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation (By similarity).

Interacts (via C-terminus) with the nucleoprotein (By similarity).

Interacts with host TUFM; this interaction contributes to the virus-induced degradation of mitochondria by autophagy, which leads to degradation of host MAVS and inhibition of type I interferon (IFN) responses (By similarity).

Interacts with host MAP1LC3B; this interaction contributes to the virus-induced degradation of mitochondria by autophagy, which leads to degradation of host MAVS and inhibition of type I interferon (IFN) responses (By similarity).

By similarity

Homodimer. Homotetramer; forms heterotetrameric Gn-Gc spikes in the pre-fusion conformation. Homotrimer; forms homotrimer in the post-fusion conformation at acidic pH (By similarity).

Interacts (via C-terminus) with the nucleoprotein (By similarity).

By similarity

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q89905

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini615 – 638ITAMPROSITE-ProRule annotationAdd BLAST24

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni520 – 537Binding to the ribonucleoproteinBy similarityAdd BLAST18
Regioni592 – 609Binding to the ribonucleoproteinBy similarityAdd BLAST18
Regioni596 – 607Binding to the ribonucleoproteinBy similarityAdd BLAST12
Regioni615 – 629Binding to the ribonucleoproteinBy similarityAdd BLAST15
Regioni761 – 781Fusion loopBy similarityAdd BLAST21
Regioni1125 – 1140Binding to the ribonucleoproteinBy similarityAdd BLAST16

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi619 – 622YxxLBy similarity4

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The YxxL motif at the C-terminus is indispensable for the interaction with MAP1LC3B and for the Gn-mediated induction of mitochondrial autophagy (By similarity). The cytoplasmic tail is involved in the inhibition of the host innate immune response (By similarity). The C-terminus of the cytoplasmic tail is involved in binding to the viral genome and the nucleocapsid (By similarity). Contains 2 contiguous zinc-fingers (By similarity).By similarity
The C-terminus is necessary for proper localization in the Golgi (By similarity). The cytoplasmic tail is involved in binding to the nucleocapsid (By similarity).By similarity

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the hantavirus envelope glycoprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri549 – 569CCHC-type 1By similarityAdd BLAST21
Zinc fingeri574 – 595CCHC-type 2By similarityAdd BLAST22

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix, Zinc-finger

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR016402, Envelope_glycoprot_Hantavirus
IPR002532, Hanta_Gc
IPR002534, Hanta_Gn
IPR012316, ITAM_motif_hantavir-typ

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01567, Hanta_G1, 1 hit
PF01561, Hanta_G2, 1 hit
PF10538, ITAM_Cys-rich, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF003945, M_poly_HantaV, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51056, ITAM_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

Q89905-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVGWVCIFLV VLTTATAGLT RNLYELKIEC PHTVGLGQGY VTGSVEITPI 
        60         70         80         90        100
LLTQVADLKI ESSCNFDLHV PATTTQKYNQ VDWTKKSSTT ESTNAGATTF 
       110        120        130        140        150
EAKTKEINLK GTCNIPPTTF EAAYKSRKTV ICYDLACNQT HCLPTVHLIA 
       160        170        180        190        200
PVQTCMSVRS CMIGLLSSRI QVIYEKTYCV TGQLIEGLCF IPTHTIALTQ 
       210        220        230        240        250
PGHTYDTMTL PVTCFLVAKK LGTQLKLAVE LEKLITGVSC TENSFQGYYI 
       260        270        280        290        300
CFIGKHSEPL FVPTMEDYRS AELFTRMVLN PRGEDHDPDQ NGQGLMRIAG 
       310        320        330        340        350
PVTAKVPSTE TTETMQGIAF AGAPMYSSFS TLVRKADPEY VFSPGIIAES 
       360        370        380        390        400
NHSVCDKKTV PLTWTGFLAV SGEIEKITGC TVFCTLAGPG ASCEAYSETG 
       410        420        430        440        450
IFNISSPTCL VNKVQKFRGS EQRINFMCQR VDQDVVVYCN GQKKVILTKT 
       460        470        480        490        500
LVIGQCIYTF TSLFSLIPGV AHSLAVELCV PGLHGWATTA LLITFCFGWL 
       510        520        530        540        550
LIPAVTLIIL KILRLLTFSC SHYSTESKFK VILERVKVEY QKTMGSMVCD 
       560        570        580        590        600
ICHHECETAK ELETHKKSCP EGQCPYCMTI TESTESALQA HFAICKLTNR 
       610        620        630        640        650
FQENLKKSLK RPEVRKGCYR TLGVFRYKSR CYVGLVWGIL LTTELIIWAA 
       660        670        680        690        700
SADTPLMESG WSDTAHGVGI IPMKTDLELD FALASSSSYS YRRKLVNPAN 
       710        720        730        740        750
QEETLPFHFQ LDKQVVHAEI QNLGHWMDGT FNIKTAFHCY GECKKYAYPW 
       760        770        780        790        800
QTAKCFFEKD YQYETSWGCN PPDCPGVGTG CTACGVYLDK LRSVGKAYKI 
       810        820        830        840        850
VSLKYTRKVC IQLGTEQTCK HIDVNDCLVT PSVKVCMIGT ISKLQPGDTL 
       860        870        880        890        900
LFLGPLEQGG IILKQWCTTS CVFGDPGDIM STTSGMRCPE HTGSFRKICG 
       910        920        930        940        950
FATTPTCEYQ GNTVSGFQRM MATRDSFQSF NVTEPHITSN RLEWIDPDSS 
       960        970        980        990       1000
IKDHINMVLN RDVSFQDLSD NPCKVDLHTQ SIDGAWGSGV GFTLVCTVGL 
      1010       1020       1030       1040       1050
TECANFITSI KACDSAMCYG ATVTNLLRGS NTVKVVGKGG HSGSLFKCCH 
      1060       1070       1080       1090       1100
DTDCTEEGLA ASPPHLDRVT GYNQIDSDKV YDDGAPPCTI KCWFTKSGEW 
      1110       1120       1130       1140
LLGILNGNWV VVAVLIVILI LSILLFSFFC PVRSRKNKAN
Length:1,140
Mass (Da):125,735
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4678FD536AB7DBC0
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1140N → KKKY in AIA08876 (PubMed:24778254).Curated1
Sequence conflicti1140N → KKKY in AIA08879 (PubMed:24778254).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti47I → T in strain:77734. 1 Publication1
Natural varianti107I → V in strain:77734. 1 Publication1
Natural varianti302V → I in strain:77734. 1 Publication1
Natural varianti472H → R in strain:77734. 1 Publication1
Natural varianti504A → T in strain:77734. 1 Publication1
Natural varianti1120I → V in strain:77734. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
L25783 Viral cRNA Translation: AAA75530.1
L37903 Genomic RNA Translation: AAC42202.1
KF537002 Viral cRNA Translation: AIA08876.1
KF537005 Viral cRNA Translation: AIA08879.1

NCBI Reference Sequences

More...RefSeqi		NP_941974.1, NC_005215.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2654026

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		vg:2654026

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25783 Viral cRNA Translation: AAA75530.1
L37903 Genomic RNA Translation: AAC42202.1
KF537002 Viral cRNA Translation: AIA08876.1
KF537005 Viral cRNA Translation: AIA08879.1
RefSeqiNP_941974.1, NC_005215.1

3D structure databases

SMRiQ89905
ModBaseiSearch...

Genome annotation databases

GeneIDi2654026
KEGGivg:2654026

Family and domain databases

InterProiView protein in InterPro
IPR016402, Envelope_glycoprot_Hantavirus
IPR002532, Hanta_Gc
IPR002534, Hanta_Gn
IPR012316, ITAM_motif_hantavir-typ
PfamiView protein in Pfam
PF01567, Hanta_G1, 1 hit
PF01561, Hanta_G2, 1 hit
PF10538, ITAM_Cys-rich, 1 hit
PIRSFiPIRSF003945, M_poly_HantaV, 1 hit
PROSITEiView protein in PROSITE
PS51056, ITAM_2, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGP_SINV
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q89905
Secondary accession number(s): A0A059WG88
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 25, 2022
Last sequence update: November 1, 1996
Last modified: May 25, 2022
This is version 73 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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