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Entry version 125 (07 Oct 2020)
Sequence version 3 (20 Dec 2017)
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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Mouse mammary tumor virus (strain BR6) (MMTV)
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>
-Experimental evidence at protein leveli <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

Matrix protein.Curated
Nucleocapsid protein p14: Binds strongly to viral nucleic acids and promote their aggregation. Also destabilizes the nucleic acids duplexes via highly structured zinc-binding motifs.Curated
Capsid protein.Curated
NC-dUTPase has dUTPase activity, thereby preventing incorporation of uracil into DNA.By similarity
The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.PROSITE-ProRule annotation
RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.PROSITE-ProRule annotation
Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions.By similarity

Miscellaneous

The reverse transcriptase is an error-prone enzyme that lacks a proof-reading function. High mutations rate is a direct consequence of this characteristic. RT also displays frequent template swiching leading to high recombination rate. Recombination mostly occurs between homologous regions of the two copackaged RNA genomes. If these two RNA molecules derive from different viral strains, reverse transcription will give rise to highly recombinated proviral DNAs.PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Protein has several cofactor binding sites:

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by pepstatin A.1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 4-6.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei771Protease; shared with dimeric partnerPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi970Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1045Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1046Magnesium; catalytic; for reverse transcriptase activityPROSITE-ProRule annotation1
Metal bindingi1316Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1346Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1366Magnesium; catalytic; for RNase H activityPROSITE-ProRule annotation1
Metal bindingi1429MagnesiumPROSITE-ProRule annotation1
Metal bindingi1501Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1558Magnesium; catalytic; for integrase activityPROSITE-ProRule annotation1
Metal bindingi1594Magnesium; catalytic; for integrase activityBy similarity1

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 fingeri525 – 542CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri552 – 569CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1436 – 1477Integrase-typePROSITE-ProRule annotationAdd BLAST42
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi1653 – 1702Integrase-typePROSITE-ProRule annotationAdd BLAST50

<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 - Molecular functioni

GO - Biological processi

<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

Molecular functionAspartyl protease, DNA-binding, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Protease, RNA-binding, RNA-directed DNA polymerase, Transferase, Viral nucleoprotein
Biological processDNA integration, DNA recombination, Viral genome integration, Virus entry into host cell
LigandMagnesium, Metal-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:
Gag-Pro-Pol polyprotein
Cleaved into the following 10 chains:
Nucleocapsid protein-dUTPase (EC:3.6.1.23By similarity)
Short name:
NC-dUTPase
Protease (EC:3.4.23.-PROSITE-ProRule annotation1 Publication)
Reverse transcriptase/ribonuclease H (EC:2.7.7.49PROSITE-ProRule annotation, EC:2.7.7.7PROSITE-ProRule annotation, EC:3.1.26.4PROSITE-ProRule annotation)
Short name:
RT
Integrase (EC:2.7.7.-By similarity, EC:3.1.-.-By similarity)
Short name:
IN
<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:gag-pro-pol
<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>OrganismiMouse mammary tumor virus (strain BR6) (MMTV)
<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 identifieri11758 [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 lineageiVirusesRiboviriaPararnaviraeArtverviricotaRevtraviricetesOrterviralesRetroviridaeOrthoretrovirinaeBetaretrovirus
<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 hostiMus musculus (Mouse) [TaxID: 10090]
<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
  • UP000228400 <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

<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

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Viral matrix 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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved; by hostSequence analysis
<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_00001254922 – 1755Gag-Pro-Pol polyproteinAdd BLAST1754
ChainiPRO_00004424702 – 99Matrix protein p10Add BLAST98
ChainiPRO_0000442471100 – 195Phosphorylated protein pp21Add BLAST96
ChainiPRO_0000442472196 – 228Protein p3Add BLAST33
ChainiPRO_0000442473229 – 254Protein p8Add BLAST26
ChainiPRO_0000442474255 – 269Protein nAdd BLAST15
ChainiPRO_0000442475270 – 496Capsid protein p27Add BLAST227
ChainiPRO_0000442476497 – 745Nucleocapsid protein-dUTPaseAdd BLAST249
ChainiPRO_0000442477746 – 860ProteaseAdd BLAST115
ChainiPRO_0000434771861 – 1436Reverse transcriptase/ribonuclease HAdd BLAST576
ChainiPRO_00004347721437 – 1755IntegraseAdd BLAST319

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi2N-myristoyl glycine; by hostBy similarity1

<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

Specific enzymatic cleavages in vivo yield mature proteins.1 Publication
Released by autocatalytic processing.1 Publication
Myristoylated. Myristoylation of the matrix (MA) domain mediates the transport and binding of Gag polyproteins to the host plasma membrane and is required for the assembly of viral particles.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>Sitei99 – 100Cleavage; by viral protease1 Publication2
Sitei195 – 196Cleavage; by viral protease1 Publication2
Sitei228 – 229Cleavage; by viral protease1 Publication2
Sitei254 – 255Cleavage; by viral protease1 Publication2
Sitei269 – 270Cleavage; by viral protease1 Publication2
Sitei496 – 497Cleavage; by viral protease1 Publication2
Sitei745 – 746Cleavage; by viral protease1 Publication2
Sitei1436 – 1437Cleavage; by viral protease1 Publication2

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P03365

<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; when myristoylated.

1 Publication

Homodimer.

1 Publication

Homooctamer.

1 Publication1 Publication

Homotrimer.

1 PublicationBy 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

Secondary structure

11755
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P03365

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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>Domaini766 – 841Peptidase A2PROSITE-ProRule annotationAdd BLAST76
Domaini905 – 1093Reverse transcriptasePROSITE-ProRule annotationAdd BLAST189
Domaini1307 – 1437RNase HPROSITE-ProRule annotationAdd BLAST131
Domaini1490 – 1647Integrase catalyticPROSITE-ProRule annotationAdd BLAST158

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>Motifi305 – 308PTAP/PSAP motifCurated4

<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

Late-budding domains (L domains) are short sequence motifs essential for viral particle release. They can occur individually or in close proximity within structural proteins. They interacts with sorting cellular proteins of the multivesicular body (MVB) pathway. Most of these proteins are class E vacuolar protein sorting factors belonging to ESCRT-I, ESCRT-II or ESCRT-III complexes. Gag-p27 contains one L domain: a PTAP/PSAP motif, which interacts with the UEV domain of TSG101.Curated

<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 retroviral Pol polyprotein family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri525 – 542CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri552 – 569CCHC-type 2PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri1436 – 1477Integrase-typePROSITE-ProRule annotationAdd BLAST42

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05482, HIV_retropepsin_like, 1 hit
cd07557, trimeric_dUTPase, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.200, 1 hit
1.10.1200.30, 1 hit
1.10.150.490, 1 hit
1.10.375.10, 1 hit
2.30.30.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
3.30.420.10, 2 hits
3.30.70.270, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001969, Aspartic_peptidase_AS
IPR003322, B_retro_matrix
IPR038124, B_retro_matrix_sf
IPR043502, DNA/RNA_pol_sf
IPR029054, dUTPase-like
IPR036157, dUTPase-like_sf
IPR033704, dUTPase_trimeric
IPR000721, Gag_p24
IPR017856, Integrase-like_N
IPR036862, Integrase_C_dom_sf_retrovir
IPR001037, Integrase_C_retrovir
IPR001584, Integrase_cat-core
IPR003308, Integrase_Zn-bd_dom_N
IPR001995, Peptidase_A2_cat
IPR021109, Peptidase_aspartic_dom_sf
IPR034170, Retropepsin-like_cat_dom
IPR018061, Retropepsins
IPR008916, Retrov_capsid_C
IPR008919, Retrov_capsid_N
IPR010999, Retrovr_matrix
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR012337, RNaseH-like_sf
IPR002156, RNaseH_domain
IPR036397, RNaseH_sf
IPR000477, RT_dom
IPR010661, RVT_thumb
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00692, dUTPase, 1 hit
PF02337, Gag_p10, 1 hit
PF00607, Gag_p24, 1 hit
PF00552, IN_DBD_C, 1 hit
PF02022, Integrase_Zn, 1 hit
PF00075, RNase_H, 1 hit
PF00665, rve, 1 hit
PF00077, RVP, 1 hit
PF00078, RVT_1, 1 hit
PF06817, RVT_thumb, 1 hit
PF00098, zf-CCHC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00343, ZnF_C2HC, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46919, SSF46919, 1 hit
SSF47836, SSF47836, 1 hit
SSF47943, SSF47943, 1 hit
SSF50122, SSF50122, 1 hit
SSF50630, SSF50630, 1 hit
SSF51283, SSF51283, 1 hit
SSF53098, SSF53098, 2 hits
SSF56672, SSF56672, 1 hit
SSF57756, SSF57756, 2 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50175, ASP_PROT_RETROV, 1 hit
PS00141, ASP_PROTEASE, 1 hit
PS50994, INTEGRASE, 1 hit
PS51027, INTEGRASE_DBD, 1 hit
PS50879, RNASE_H, 1 hit
PS50878, RT_POL, 1 hit
PS50158, ZF_CCHC, 1 hit
PS50876, ZF_INTEGRASE, 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>Sequences (3)i

<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.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by ribosomal frameshifting. AlignAdd to basket
Isoform Gag-Pro-Pol polyprotein (identifier: P03365-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG
60 70 80 90 100
GLNLQDWKRV GREMKRYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL
110 120 130 140 150
SAEAKSVTEE ELEEGLTGLL STSSQEKTYG TRGTAYAEID TEVDKLSEHI
160 170 180 190 200
YDEPYEEKEK ADKNEEKDHV RKIKKVVQRK ENSEGKRKEK DSKAFLATDW
210 220 230 240 250
NDDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVVKKKPQ ALRRKPLPPV
260 270 280 290 300
GFAGAMAEAR EKGDLTFTFP VVFMGESDED DTPVWEPLPL KTLKELQSAV
310 320 330 340 350
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK
360 370 380 390 400
SKEMVQKAAG KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL
410 420 430 440 450
AWRAIPPPGV KKTVLAGLKQ GNEESYETFI SRLEEAVYRM MPRGEGSDIL
460 470 480 490 500
IKQLAWENAN SLCQDLIRPI RKTGTIQDYI RACLDASPAV VQGMAYAAAM
510 520 530 540 550
RGQKYSTFVK QTYGGGKGGQ GAEGPVCFSC GKTGHIRKDC KDEKGSKRAP
560 570 580 590 600
PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPA
610 620 630 640 650
QKGDGVKGSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS
660 670 680 690 700
LVPTLVKGTL PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA
710 720 730 740 750
AKNAVIIHKG ERIAQLLLLP YLKLPNPVIK EERGSEGFGS TSHVHWVQEI
760 770 780 790 800
SDSRPMLHIY LNGRRFLGLL DTGADKTCIA GRDWPANWPI HQTESSLQGL
810 820 830 840 850
GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD IMKDIKVRLM
860 870 880 890 900
TDSPDDSQDL MIGAIESNLF ADQISWKSDQ PVWLNQWPLK QEKLQALQQL
910 920 930 940 950
VTEQLQLGHL EESNSPWNTP VFVIKKKSGK WRLLQDLRAV NATMHDMGAL
960 970 980 990 1000
QPGLPSPVAV PKGWEIIIID LQDCFFNIKL HPEDCKRFAF SVPSPNFKRP
1010 1020 1030 1040 1050
YQRFQWKVLP QGMKNSPTLC QKFVDKAILT VRDKYQDSYI VHYMDDILLA
1060 1070 1080 1090 1100
HPSRSIVDEI LTSMIQALNK HGLVVSTEKI QKYDNLKYLG THIQGDSVSY
1110 1120 1130 1140 1150
QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL FEILNGDSNP
1160 1170 1180 1190 1200
ISTRKLTPEA CKALQLMNER LSTARVKRLD LSQPWSLCIL KTEYTPTACL
1210 1220 1230 1240 1250
WQDGVVEWIH LPHISPKVIT PYDIFCTQLI IKGRHRSKEL FSKDPDYIVV
1260 1270 1280 1290 1300
PYTKVQFDLL LQEKEDWPIS LLGFLGEVHF HLPKDPLLTF TLQTAIIFPH
1310 1320 1330 1340 1350
MTSTTPLEKG IVIFTDGSAN GRSVTYIQGR EPIIKENTQN TAQQAEIVAV
1360 1370 1380 1390 1400
ITAFEEVSQP FNLYTDSKYV TGLFPEIETA TLSPRTKIYT ELKHLQRLIH
1410 1420 1430 1440 1450
KRQEKFYIGH IRGHTGLPGP LAQGNAYADS LTRILTALES AQESHALHHQ
1460 1470 1480 1490 1500
NAAALRFQFH ITREQAREIV KLCPNCPDWG HAPQLGVNPR GLKPRVLWQM
1510 1520 1530 1540 1550
DVTHVSEFGK LKYVHVTVDT YSHFTFATAR TGEATKDVLQ HLAQSFAYMG
1560 1570 1580 1590 1600
IPQKIKTDNA PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI
1610 1620 1630 1640 1650
KAQLNKLQKA GKYYTPHHLL AHALFVLNHV NMDNQGHTAA ERHWGPISAD
1660 1670 1680 1690 1700
PKPMVMWKDL LTGSWKGPDV LITAGRGYAC VFPQDAETPI WVPDRFIRPF
1710 1720 1730 1740 1750
TERKEATPTP GTAEKTPPRD EKDQQESPKN ESSPHQREDG LATSAGVDLR

SGGGP
Note: Produced by -1 ribosomal frameshiftings between gag-pro and pro-pol.1 Publication
Length:1,755
Mass (Da):197,115
Last modified:December 20, 2017 - v3
<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:i524B997C251D50F1
GO
Isoform Gag-Pro polyprotein (identifier: P10271-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P10271.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:860
Mass (Da):95,409
GO
Isoform Gag polyprotein (identifier: P10258-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P10258.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:591
Mass (Da):66,269
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 conflicti1481H → S in AAA46540 (PubMed:6197754).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M15122 Genomic RNA Translation: AAA46542.1
K01707 Genomic RNA Translation: AAA46540.1

Protein sequence database of the Protein Information Resource

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PIRi
A05073
C26795, GNMVMM

Keywords - Coding sequence diversityi

Ribosomal frameshifting

<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
M15122 Genomic RNA Translation: AAA46542.1
K01707 Genomic RNA Translation: AAA46540.1
PIRiA05073
C26795, GNMVMM

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3JCAelectron microscopy4.80A/B/E/F1437-1701[»]
C/D/G/H1653-1701[»]
5CZ1X-ray1.70A/B/C/D1487-1648[»]
5CZ2X-ray2.72A/B/C/D/E/F/G/H/I/J/K/L1437-1646[»]
5D7UX-ray1.50A/B1648-1702[»]
SMRiP03365
ModBaseiSearch...
PDBe-KBiSearch...

Proteomic databases

PRIDEiP03365

Family and domain databases

CDDicd05482, HIV_retropepsin_like, 1 hit
cd07557, trimeric_dUTPase, 1 hit
Gene3Di1.10.10.200, 1 hit
1.10.1200.30, 1 hit
1.10.150.490, 1 hit
1.10.375.10, 1 hit
2.30.30.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
3.30.420.10, 2 hits
3.30.70.270, 2 hits
InterProiView protein in InterPro
IPR001969, Aspartic_peptidase_AS
IPR003322, B_retro_matrix
IPR038124, B_retro_matrix_sf
IPR043502, DNA/RNA_pol_sf
IPR029054, dUTPase-like
IPR036157, dUTPase-like_sf
IPR033704, dUTPase_trimeric
IPR000721, Gag_p24
IPR017856, Integrase-like_N
IPR036862, Integrase_C_dom_sf_retrovir
IPR001037, Integrase_C_retrovir
IPR001584, Integrase_cat-core
IPR003308, Integrase_Zn-bd_dom_N
IPR001995, Peptidase_A2_cat
IPR021109, Peptidase_aspartic_dom_sf
IPR034170, Retropepsin-like_cat_dom
IPR018061, Retropepsins
IPR008916, Retrov_capsid_C
IPR008919, Retrov_capsid_N
IPR010999, Retrovr_matrix
IPR043128, Rev_trsase/Diguanyl_cyclase
IPR012337, RNaseH-like_sf
IPR002156, RNaseH_domain
IPR036397, RNaseH_sf
IPR000477, RT_dom
IPR010661, RVT_thumb
IPR001878, Znf_CCHC
IPR036875, Znf_CCHC_sf
PfamiView protein in Pfam
PF00692, dUTPase, 1 hit
PF02337, Gag_p10, 1 hit
PF00607, Gag_p24, 1 hit
PF00552, IN_DBD_C, 1 hit
PF02022, Integrase_Zn, 1 hit
PF00075, RNase_H, 1 hit
PF00665, rve, 1 hit
PF00077, RVP, 1 hit
PF00078, RVT_1, 1 hit
PF06817, RVT_thumb, 1 hit
PF00098, zf-CCHC, 1 hit
SMARTiView protein in SMART
SM00343, ZnF_C2HC, 2 hits
SUPFAMiSSF46919, SSF46919, 1 hit
SSF47836, SSF47836, 1 hit
SSF47943, SSF47943, 1 hit
SSF50122, SSF50122, 1 hit
SSF50630, SSF50630, 1 hit
SSF51283, SSF51283, 1 hit
SSF53098, SSF53098, 2 hits
SSF56672, SSF56672, 1 hit
SSF57756, SSF57756, 2 hits
PROSITEiView protein in PROSITE
PS50175, ASP_PROT_RETROV, 1 hit
PS00141, ASP_PROTEASE, 1 hit
PS50994, INTEGRASE, 1 hit
PS51027, INTEGRASE_DBD, 1 hit
PS50879, RNASE_H, 1 hit
PS50878, RT_POL, 1 hit
PS50158, ZF_CCHC, 1 hit
PS50876, ZF_INTEGRASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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 nameiPOL_MMTVB
<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: P03365
<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: July 21, 1986
Last sequence update: December 20, 2017
Last modified: October 7, 2020
This is version 125 of the entry and version 3 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

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
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