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P11283

- POL_MMTVC

UniProt

P11283 - POL_MMTVC

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Protein

Gag-Pro-Pol polyprotein

Gene

gag-pro-pol

Organism
Mouse mammary tumor virus (strain C3H) (MMTV)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Matrix protein p10: Matrix protein.By similarity
Nucleocapsid protein p14: Nucleocapsid protein. Binds to single-stranded DNA (By similarity).By similarity
Capsid protein p27: capsid protein.By similarity
NC-dUTPase has dUTPase activity, thereby preventing incorporation of uracil into DNA.
The aspartyl protease mediates proteolytic cleavages of Gag, Gag-Pro and Gag-Pro-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 (By similarity).By similarity
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 perform 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 perform 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 (By similarity).By similarity

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).PROSITE-ProRule annotation
Endonucleolytic cleavage to 5'-phosphomonoester.PROSITE-ProRule annotation

Cofactori

RT polymerase domain: Binds 2 magnesium ions.By similarity
Magnesium ions for NC-dUTPase.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei99 – 1002Cleavage; by viral proteaseBy similarity
Sitei195 – 1962Cleavage; by viral proteaseBy similarity
Sitei228 – 2292Cleavage; by viral proteaseBy similarity
Sitei252 – 2532Cleavage; by viral proteaseBy similarity
Sitei269 – 2702Cleavage; by viral proteaseBy similarity
Sitei496 – 4972Cleavage; by viral proteaseBy similarity
Sitei745 – 7462Cleavage; by viral proteaseBy similarity
Active sitei771 – 7711Protease; shared with dimeric partnerPROSITE-ProRule annotation
Sitei833 – 8342Cleavage; by viral proteaseBy similarity
Metal bindingi970 – 9701Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi1045 – 10451Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi1046 – 10461Magnesium; catalytic; for reverse transcriptase activityBy similarity
Metal bindingi1316 – 13161Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1346 – 13461Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1366 – 13661Magnesium; catalytic; for RNase H activityBy similarity
Metal bindingi1429 – 14291Magnesium; catalytic; for RNase H activityBy similarity
Sitei1437 – 14382Cleavage; by viral proteaseBy similarity
Metal bindingi1501 – 15011Magnesium; catalytic; for integrase activityBy similarity
Metal bindingi1558 – 15581Magnesium; catalytic; for integrase activityBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri525 – 54218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri552 – 56918CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1436 – 147742Integrase-typePROSITE-ProRule annotationAdd
BLAST
DNA bindingi1653 – 170250Integrase-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. aspartic-type endopeptidase activity Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  4. nucleotide binding Source: UniProtKB-KW
  5. RNA-directed DNA polymerase activity Source: UniProtKB-KW
  6. RNA-DNA hybrid ribonuclease activity Source: UniProtKB-EC
  7. structural constituent of virion Source: UniProtKB-KW
  8. zinc ion binding Source: InterPro

GO - Biological processi

  1. DNA integration Source: UniProtKB-KW
  2. DNA recombination Source: UniProtKB-KW
  3. dUTP metabolic process Source: InterPro
  4. establishment of integrated proviral latency Source: UniProtKB-KW
  5. viral entry into host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Aspartyl protease, DNA-directed DNA polymerase, Endonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Protease, RNA-directed DNA polymerase, Transferase

Keywords - Biological processi

DNA integration, DNA recombination, Viral genome integration, Virus entry into host cell

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding, Nucleotide-binding, Viral nucleoprotein, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Gag-Pro-Pol polyprotein
Cleaved into the following 10 chains:
Gene namesi
Name:gag-pro-pol
OrganismiMouse mammary tumor virus (strain C3H) (MMTV)
Taxonomic identifieri11759 [NCBI]
Taxonomic lineageiVirusesRetro-transcribing virusesRetroviridaeOrthoretrovirinaeBetaretrovirus
Virus hostiMus musculus (Mouse) [TaxID: 10090]
ProteomesiUP000006540: Genome

Subcellular locationi

GO - Cellular componenti

  1. viral nucleocapsid Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Capsid protein, Viral matrix protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed; by hostBy similarity
Chaini2 – 17551754Gag-Pro-Pol polyproteinPRO_0000125493Add
BLAST
Chaini2 – 9998Matrix protein p10PRO_0000403612Add
BLAST
Chaini100 – 19596Phosphorylated protein pp21PRO_0000403613Add
BLAST
Chaini196 – 22833Protein p3PRO_0000403614Add
BLAST
Chaini229 – 25224Protein p8Sequence AnalysisPRO_0000403615Add
BLAST
Chaini253 – 26917Protein nPRO_0000403616Add
BLAST
Chaini270 – 496227Capsid protein p27PRO_0000403617Add
BLAST
Chaini497 – 745249Nucleocapsid protein-dUTPaseSequence AnalysisPRO_0000403618Add
BLAST
Chaini746 – 83388ProteaseSequence AnalysisPRO_0000403619Add
BLAST
Chaini834 – 1437604Reverse transcriptase/ribonuclease HSequence AnalysisPRO_0000403620Add
BLAST
Chaini1438 – 1755318IntegraseSequence AnalysisPRO_0000403621Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycine; by hostBy similarity

Post-translational modificationi

Specific enzymatic cleavages in vivo yield mature proteins.2 Publications
p10 is myristoylated.1 Publication

Keywords - PTMi

Lipoprotein, Myristate, Phosphoprotein

Interactioni

Subunit structurei

NC-dUTPase is a homotrimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliP11283.
SMRiP11283. Positions 550-580, 619-724.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini766 – 84176Peptidase A2PROSITE-ProRule annotationAdd
BLAST
Domaini905 – 1093189Reverse transcriptasePROSITE-ProRule annotationAdd
BLAST
Domaini1307 – 1435129RNase HPROSITE-ProRule annotationAdd
BLAST
Domaini1490 – 1647158Integrase catalyticPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi278 – 2814Poly-Asp
Compositional biasi716 – 7194Poly-Leu

Sequence similaritiesi

Contains 2 CCHC-type zinc fingers.PROSITE-ProRule annotation
Contains 1 integrase catalytic domain.PROSITE-ProRule annotation
Contains 1 integrase-type DNA-binding domain.PROSITE-ProRule annotation
Contains 1 integrase-type zinc finger.PROSITE-ProRule annotation
Contains 1 peptidase A2 domain.PROSITE-ProRule annotation
Contains 1 reverse transcriptase domain.PROSITE-ProRule annotation
Contains 1 RNase H domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri525 – 54218CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri552 – 56918CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1436 – 147742Integrase-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Family and domain databases

Gene3Di1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
2.70.40.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 1 hit.
InterProiIPR001969. Aspartic_peptidase_AS.
IPR003322. B_retro_matrix_N.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF00692. 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.
[Graphical view]
ProDomiPD004265. B_retro_matrix_N. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTiSM00343. ZnF_C2HC. 2 hits.
[Graphical view]
SUPFAMiSSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 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.
SSF57756. SSF57756. 2 hits.
PROSITEiPS50175. 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.
[Graphical view]

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. Align

Note: Translation results in the formation of the Gag-Pro. Ribosomal frameshifting at the gag-pro/pol genes boundary produces the Gag-Pro-Pol polyprotein.2 Publications

Isoform Gag-Pro-Pol polyprotein (identifier: P11283) [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
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG
60 70 80 90 100
GLNLQDWKRV GREMKKYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL
110 120 130 140 150
SAEAKSVTEE ELEEGLTGLL SASSQEKTYG TRGTAYAEID TEVDKLSEHI
160 170 180 190 200
YDEPYEEKEK ADKNEEKDHV RKVKKIVQRK ENSEHKRKEK DQKAFLATDW
210 220 230 240 250
NNDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVDKKKPL ALRRKPLPPV
260 270 280 290 300
GFAGAMAEAR EKGDLTFTFP VVFMGESDDD DTPVWEPLPL KTLKELQSAV
310 320 330 340 350
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK
360 370 380 390 400
SKETVQKTAG KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL
410 420 430 440 450
AWRAIPPPGV KKTVLAGLKQ GNEESYETFI SRLEEAVYRM MPRGEGSDIL
460 470 480 490 500
IKQLAWENAN SLCQDLIRPM RKTGTMQDYI RACLDASPAV VQGMAYAAAM
510 520 530 540 550
RGQKYSTFVK QTYGGGKGGQ GSEGPVCFSC GKTGHIKRDC KEEKGSKRAP
560 570 580 590 600
PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPT
610 620 630 640 650
QKGDKGKDSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS
660 670 680 690 700
LVPTLVKGTL PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA
710 720 730 740 750
AKNAVIIHKG ERIAQLLLLP YLKLPNPIIK EERGSEGFGS TSHVHWVQEI
760 770 780 790 800
SDSRPMLHIS LNGRRFLGLL DTGADKTCIA GRDWPANWPI HQTESSLQGL
810 820 830 840 850
GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD IMKEIKVRLM
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 THIQGDAVSY
1110 1120 1130 1140 1150
QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL FEILNGDSNP
1160 1170 1180 1190 1200
ISIRKLTPEA CKALQLVNER LSIARVKRLD LSRPWSLCIL KTEYTPTACL
1210 1220 1230 1240 1250
WQNGVLEWIH 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
ITAFEEVSQS FNLYTDSKYV TGLFPEIETA TLSPRTKIYT ELRHLQRLIH
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
FPQKIKTDNA PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI
1610 1620 1630 1640 1650
KAQLNKLQKA GKYYTPHHLL AHALFVLNHV NMDNQGHTAA ERHWGPISAD
1660 1670 1680 1690 1700
PKPMVMWKDL LAGSWKGPDV LITAGRGYAC VFPQDAETPI WVPDRFIRPF
1710 1720 1730 1740 1750
TERKEATPTP GTAEKTPPRD EKDQQKSPED ESSPHQREDG LATSAGVNLR

SGGGS

Note: Produced by -1 ribosomal frameshifting between gag-pro and pro-pol.

Length:1,755
Mass (Da):197,329
Last modified:January 11, 2011 - v2
Checksum:i0E99A2ADD96823A4
GO
Isoform Gag-Pro polyprotein (identifier: Q9IZT2-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry Q9IZT2.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by -1 ribosomal frameshifting between gag-pro.

Length:860
Mass (Da):95,593
GO
Isoform Gag polyprotein (identifier: P11284-1) [UniParc]FASTAAdd to Basket

The sequence of this isoform can be found in the external entry P11284.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.

Note: Produced by conventional translation.

Length:591
Mass (Da):66,351
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti857 – 8604SQDL → FTGF in AAA66625. (PubMed:3035577)Curated
Sequence conflicti867 – 8671S → T in AAA66625. (PubMed:3035577)Curated
Sequence conflicti952 – 9521P → L in AAA66625. (PubMed:3035577)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti523 – 5231E → K.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF228552 Genomic DNA. Translation: AAF31474.1.
M16766 Genomic RNA. Translation: AAA66623.1.
M16766 Genomic RNA. Translation: AAA66625.1.
PIRiB29029.

Keywords - Coding sequence diversityi

Ribosomal frameshifting

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF228552 Genomic DNA. Translation: AAF31474.1 .
M16766 Genomic RNA. Translation: AAA66623.1 .
M16766 Genomic RNA. Translation: AAA66625.1 .
PIRi B29029.

3D structure databases

ProteinModelPortali P11283.
SMRi P11283. Positions 550-580, 619-724.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.10.200. 1 hit.
1.10.1200.30. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
2.70.40.10. 1 hit.
3.30.420.10. 2 hits.
4.10.60.10. 1 hit.
InterProi IPR001969. Aspartic_peptidase_AS.
IPR003322. B_retro_matrix_N.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR000721. Gag_p24.
IPR001037. Integrase_C_retrovir.
IPR001584. Integrase_cat-core.
IPR017856. Integrase_Zn-bd_dom-like_N.
IPR003308. Integrase_Zn-bd_dom_N.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic_dom.
IPR008916. Retrov_capsid_C.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RT_dom.
IPR010661. RVT_thumb.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami 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.
[Graphical view ]
ProDomi PD004265. B_retro_matrix_N. 1 hit.
[Graphical view ] [Entries sharing at least one domain ]
SMARTi SM00343. ZnF_C2HC. 2 hits.
[Graphical view ]
SUPFAMi SSF46919. SSF46919. 1 hit.
SSF47353. SSF47353. 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.
SSF57756. SSF57756. 2 hits.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Genetics of mouse mammary tumor virus-induced mammary tumors: linkage of tumor induction to the gag gene."
    Hook L.M., Agafonova Y., Ross S.R., Turner S.J., Golovkina T.V.
    J. Virol. 74:8876-8883(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Two efficient ribosomal frameshifting events are required for synthesis of mouse mammary tumor virus gag-related polyproteins."
    Jacks T., Townsley K., Varmus H.E., Majors J.
    Proc. Natl. Acad. Sci. U.S.A. 84:4298-4302(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-591 AND 857-970, RIBOSOMAL FRAMESHIFT.
  3. "Analysis of gag proteins from mouse mammary tumor virus."
    Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Krutzsch H.C., Oroszlan S.
    J. Virol. 63:2543-2549(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-58; 65-116; 194-218; 227-241; 251-252; 270-276 AND 362-591, PROTEOLYTIC PROCESSING OF POLYPROTEIN, MYRISTOYLATION AT GLY-2.
  4. "Purification and characterization of the mouse mammary tumor virus protease expressed in Escherichia coli."
    Menendez-Arias L., Young M., Oroszlan S.
    J. Biol. Chem. 267:24134-24139(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF POLYPROTEIN.
  5. "The protein p30, encoded at the gag-pro junction of mouse mammary tumor virus, is a dUTPase fused with a nucleocapsid protein."
    Bergman A.C., Bjornberg O., Nord J., Nyman P.O., Rosengren A.M.
    Virology 204:420-424(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: RIBOSOMAL FRAMESHIFT, SUBUNIT, CHARACTERIZATION OF NC-DUTPASE.

Entry informationi

Entry nameiPOL_MMTVC
AccessioniPrimary (citable) accession number: P11283
Secondary accession number(s): Q9IZT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 11, 2011
Last modified: October 29, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3