Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Gag-Pro polyprotein

Gene

gag-pro

Organism
Mason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Matrix protein p10: Matrix protein.Curated
Nucleocapsid protein p14: Nucleocapsid protein.Curated
Capsid protein p27: capsid protein.Curated
Protease 17 kDa: 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 annotation1 Publication
Protease 13 kDa: 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 annotation1 Publication
G-patch peptide: Enhances the activity of the reverse transcriptase. May be part of the mature RT.1 Publication

Catalytic activityi

dUTP + H2O = dUMP + diphosphate.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei785Protease; shared with dimeric partnerPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri547 – 564CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri576 – 593CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAspartyl protease, DNA-binding, Hydrolase, Protease, Viral nucleoprotein
Biological processNucleotide metabolism
LigandMagnesium, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.23.B6 3195

Protein family/group databases

MEROPSiA02.009

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro polyprotein
Alternative name(s):
Pr95Imported
Cleaved into the following 9 chains:
Nucleocapsid protein-dUTPase (EC:3.6.1.231 Publication)
Short name:
NC-dUTPase
Protease 17 kDa1 Publication (EC:3.4.23.-PROSITE-ProRule annotation1 Publication)
Protease 13 kDa1 Publication (EC:3.4.23.-PROSITE-ProRule annotation1 Publication)
G-patch peptide1 Publication
Gene namesi
Name:gag-pro
OrganismiMason-Pfizer monkey virus (MPMV) (Simian Mason-Pfizer virus)
Taxonomic identifieri11855 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeBetaretrovirus
Virus hostiMacaca mulatta (Rhesus macaque) [TaxID: 9544]
Proteomesi
  • UP000008870 Componenti: Genome
  • UP000105838 Componenti: Genome

Subcellular locationi

Protease 13 kDa :
  • Virion 1 Publication
Protease 17 kDa :
  • Virion 1 Publication

GO - Cellular componenti

Keywords - Cellular componenti

Capsid protein, Viral matrix protein, Virion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi203 – 205PPY → GAA: 80% loss of virus release. 1 Publication3
Mutagenesisi210 – 211PS → AG: 30% loss of virus release. 1 Publication2
Mutagenesisi868N → I: Accelerated processing of the protease C-terminus. 1 Publication1
Mutagenesisi873A → R: 30% loss of infectivity. 1 Publication1
Mutagenesisi874Q → I: Accelerated processing of the protease C-terminus. 50% loss of RT activity. 1 Publication1
Mutagenesisi879G → A: 85% loss of infectivity and 65% loss of RT activity. 1 Publication1
Mutagenesisi880Y → A: 90% loss of infectivity and 65% loss of RT activity. 1 Publication1
Mutagenesisi880Y → S: Defective in nucleic acid binding. 80% loss of infectivity. 50% loss of RT activity. 1 Publication1
Mutagenesisi883G → A: 90% loss of infectivity and 55% loss of RT activity. 1 Publication1
Mutagenesisi885G → A: 70% loss of infectivity and 60% loss of RT activity. 1 Publication1
Mutagenesisi886L → A: 85% loss of infectivity and 60% loss of RT activity. 1 Publication1
Mutagenesisi887G → A: 95% loss of infectivity and 95% loss of RT activity. 1 Publication1
Mutagenesisi892G → A: 85% loss of infectivity and 60% loss of RT activity. 1 Publication1
Mutagenesisi907G → A: 60% loss of infectivity and 35% loss of RT activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved; by hostCurated
ChainiPRO_00001995502 – 911Gag-Pro polyproteinAdd BLAST910
ChainiPRO_00004431902 – 100Matrix protein p10Add BLAST99
ChainiPRO_0000443191101 – 216Phosphorylated protein pp24Add BLAST116
PropeptideiPRO_0000443192101 – 161CuratedAdd BLAST61
ChainiPRO_0000443193162 – 216Phosphorylated protein pp18Add BLAST55
ChainiPRO_0000443194217 – 299p12Add BLAST83
ChainiPRO_0000443195300 – 525Capsid protein p27Add BLAST226
ChainiPRO_0000443296526 – 759Nucleocapsid protein-dUTPaseAdd BLAST234
ChainiPRO_0000443196760 – 911Protease 17 kDaAdd BLAST152
ChainiPRO_0000443197760 – 873Protease 13 kDaAdd BLAST114
PeptideiPRO_0000443198874 – 911G-patch peptideAdd BLAST38

Post-translational modificationi

Protease 17 kDa: Released by autocatalytic processing. The protease can undergo further autoprocessing to yield 2 shorter but enzymatically active forms of 12 kDa and 13 kDa without the GDP domain. the 12 kDa form is monomeric.3 Publications
Gag-Pro polyprotein: 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
Gag-Pro polyprotein: Specific enzymatic cleavages in vivo yield mature proteins.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei100 – 101Cleavage; by viral proteaseBy similarity2
Sitei161 – 162Cleavage; by viral proteaseBy similarity2
Sitei216 – 217Cleavage; by viral proteaseBy similarity2
Sitei299 – 300Cleavage; by viral proteaseBy similarity2
Sitei525 – 526Cleavage; by viral proteaseBy similarity2
Sitei759 – 760Cleavage; by viral protease1 Publication2
Sitei873 – 874Cleavage; by viral protease1 Publication2

Keywords - PTMi

Lipoprotein, Myristate

Proteomic databases

PRIDEiP07570

Interactioni

Subunit structurei

Protease 17 kDa: Homodimer (By similarity). G-patch peptide: Interacts with the reverse transcriptase/ribonuclease H (PubMed:22171253). Nucleocapsid protein-dUTPase: Homotrimer (PubMed:17169987).By similarity2 Publications

Structurei

Secondary structure

1911
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi635 – 637Combined sources3
Beta strandi646 – 651Combined sources6
Beta strandi656 – 658Combined sources3
Helixi660 – 662Combined sources3
Beta strandi665 – 667Combined sources3
Beta strandi670 – 672Combined sources3
Beta strandi679 – 685Combined sources7
Helixi687 – 690Combined sources4
Turni691 – 693Combined sources3
Beta strandi694 – 696Combined sources3
Beta strandi699 – 701Combined sources3
Beta strandi711 – 718Combined sources8
Beta strandi720 – 722Combined sources3
Beta strandi727 – 735Combined sources9
Beta strandi766 – 769Combined sources4
Beta strandi770 – 775Combined sources6
Beta strandi778 – 784Combined sources7
Beta strandi792 – 794Combined sources3
Helixi795 – 797Combined sources3
Beta strandi804 – 806Combined sources3
Beta strandi808 – 811Combined sources4
Helixi816 – 818Combined sources3
Beta strandi821 – 825Combined sources5
Beta strandi827 – 830Combined sources4
Turni832 – 834Combined sources3
Beta strandi836 – 839Combined sources4
Beta strandi842 – 844Combined sources3
Helixi854 – 857Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1NSONMR-A163-267[»]
2D4LX-ray1.70A11-162[»]
2D4MX-ray1.85A11-162[»]
2D4NX-ray1.53A11-162[»]
3SQFX-ray1.63A/B163-276[»]
3TP1X-ray1.60A11-162[»]
3TPNX-ray1.65A609-759[»]
3TPSX-ray1.85A609-759[»]
3TPWX-ray1.65A11-162[»]
3TPYX-ray1.75A609-759[»]
3TQ3X-ray1.85A609-759[»]
3TQ4X-ray1.60A609-759[»]
3TQ5X-ray1.40A609-759[»]
3TRLX-ray1.80A609-759[»]
3TRNX-ray1.83A609-759[»]
3TS6X-ray1.84A609-759[»]
3TSLX-ray2.20A609-759[»]
3TTAX-ray2.00A609-759[»]
ProteinModelPortaliP07570
SMRiP07570
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07570

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini780 – 856Peptidase A2PROSITE-ProRule annotationAdd BLAST77
Domaini867 – 911G-patchPROSITE-ProRule annotation1 PublicationAdd BLAST45

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili216 – 257Sequence analysisAdd BLAST42

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi202 – 205PPXY motif1 Publication4
Motifi210 – 213PTAP/PSAP motif1 Publication4

Domaini

Gag-Pro polyprotein: 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. Phosphorylated protein pp24 and phosphorylated protein pp18 contains two L domains: a PTAP/PSAP motif which interacts with the UEV domain of TSG101, and a PPXY motif which binds to the WW domains of the ubiquitin ligase NEDD4. Both motifs contribute to viral release. The PSAP motif acts as an additional L domain and promotes the efficient release of the virions but requires an intact PPPY motif to perform its function.1 Publication
Protease 17 kDa: The glycine-rich G-patch domain (GPD) is present at the C-terminus of the protease from which it is then detached by the protease itself.2 Publications

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri547 – 564CCHC-type 1PROSITE-ProRule annotationAdd BLAST18
Zinc fingeri576 – 593CCHC-type 2PROSITE-ProRule annotationAdd BLAST18

Keywords - Domaini

Coiled coil, Repeat, Zinc-finger

Phylogenomic databases

OrthoDBiVOG09000135

Family and domain databases

CDDicd05482 HIV_retropepsin_like, 1 hit
cd07557 trimeric_dUTPase, 1 hit
Gene3Di1.10.1200.30, 1 hit
1.10.150.490, 1 hit
1.10.375.10, 1 hit
2.40.70.10, 1 hit
2.70.40.10, 1 hit
InterProiView protein in InterPro
IPR001969 Aspartic_peptidase_AS
IPR003322 B_retro_matrix
IPR038124 B_retro_matrix_sf
IPR029054 dUTPase-like
IPR036157 dUTPase-like_sf
IPR033704 dUTPase_trimeric
IPR000467 G_patch_dom
IPR000721 Gag_p24
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
IPR001878 Znf_CCHC
IPR036875 Znf_CCHC_sf
PfamiView protein in Pfam
PF00692 dUTPase, 1 hit
PF01585 G-patch, 1 hit
PF02337 Gag_p10, 1 hit
PF00607 Gag_p24, 1 hit
PF00077 RVP, 1 hit
ProDomiView protein in ProDom or Entries sharing at least one domain
PD004265 B_retro_matrix_N, 1 hit
SMARTiView protein in SMART
SM00443 G_patch, 1 hit
SM00343 ZnF_C2HC, 2 hits
SUPFAMiSSF47836 SSF47836, 1 hit
SSF47943 SSF47943, 1 hit
SSF50630 SSF50630, 1 hit
SSF51283 SSF51283, 1 hit
SSF57756 SSF57756, 1 hit
PROSITEiView protein in PROSITE
PS50175 ASP_PROT_RETROV, 1 hit
PS00141 ASP_PROTEASE, 1 hit
PS50174 G_PATCH, 1 hit
PS50158 ZF_CCHC, 1 hit

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by ribosomal frameshifting. AlignAdd to basket

Isoform Gag-Pro polyprotein (identifier: P07570-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MGQELSQHER YVEQLKQALK TRGVKVKYAD LLKFFDFVKD TCPWFPQEGT
60 70 80 90 100
IDIKRWRRVG DCFQDYYNTF GPEKVPVTAF SYWNLIKELI DKKEVNPQVM
110 120 130 140 150
AAVAQTEEIL KSNSQTDLTK TSQNPDLDLI SLDSDDEGAK SSSLQDKGLS
160 170 180 190 200
STKKPKRFPV LLTAQTSKDP EDPNPSEVDW DGLEDEAAKY HNPDWPPFLT
210 220 230 240 250
RPPPYNKATP SAPTVMAVVN PKEELKEKIA QLEEQIKLEE LHQALISKLQ
260 270 280 290 300
KLKTGNETVT HPDTAGGLSR TPHWPGQHIP KGKCCASREK EEQIPKDIFP
310 320 330 340 350
VTETVDGQGQ AWRHHNGFDF AVIKELKTAA SQYGATAPYT LAIVESVADN
360 370 380 390 400
WLTPTDWNTL VRAVLSGGDH LLWKSEFFEN CRDTAKRNQQ AGNGWDFDML
410 420 430 440 450
TGSGNYSSTD AQMQYDPGLF AQIQAAATKA WRKLPVKGDP GASLTGVKQG
460 470 480 490 500
PDEPFADFVH RLITTAGRIF GSAEAGVDYV KQLAYENANP ACQAAIRPYR
510 520 530 540 550
KKTDLTGYIR LCSDIGPSYQ QGLAMAAAFS GQTVKDFLNN KNKEKGGCCF
560 570 580 590 600
KCGKKGHFAK NCHEHAHNNA EPKVPGLCPR CKRGKHWANE CKSKTDNQGN
610 620 630 640 650
PIPPHQGNRV EGPAPGPETS LWGSQLCSSQ QKQPISKLTR ATPGSAGLDL
660 670 680 690 700
CSTSHTVLTP EMGPQALSTG IYGPLPPNTF GLILGRSSIT MKGLQVYPGV
710 720 730 740 750
IDNDYTGEIK IMAKAVNNIV TVSQGNRIAQ LILLPLIETD NKVQQPYRGQ
760 770 780 790 800
GSFGSSDIYW VQPITCQKPS LTLWLDDKMF TGLIDTGADV TIIKLEDWPP
810 820 830 840 850
NWPITDTLTN LRGIGQSNNP KQSSKYLTWR DKENNSGLIK PFVIPNLPVN
860 870 880 890 900
LWGRDLLSQM KIMMCSPNDI VTAQMLAQGY SPGKGLGKKE NGILHPIPNQ
910
GQSNKKGFGN F
Note: Produced by -1 ribosomal frameshifting between gag-pro.2 Publications
Length:911
Mass (Da):100,648
Last modified:February 28, 2018 - v2
Checksum:iD9B65A6070A3CA7D
GO
Isoform Gag polyprotein (identifier: P07567-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P07567.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by conventional translation.2 Publications
Length:657
Mass (Da):73,110
GO
Isoform Gag-Pro-Pol polyprotein (identifier: P07572-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry P07572.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Note: Produced by -1 ribosomal frameshiftings between gag-pro and pro-pol.2 Publications
Length:1,771
Mass (Da):198,014
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12349 Genomic RNA No translation available.
AF033815 Genomic RNA Translation: AAC82574.1
PIRiB25839 PRLJMP
RefSeqiNP_056892.1, NC_001550.1 [P07570-1]

Genome annotation databases

GeneIDi2746973

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Similar proteinsi

Entry informationi

Entry nameiPRO_MPMV
AccessioniPrimary (citable) accession number: P07570
Secondary accession number(s): O92810
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: February 28, 2018
Last modified: May 23, 2018
This is version 112 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health