P03355 (POL_MLVMS) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Gag-Pol polyprotein
Short name=Pr180gag-pol

Cleaved into the following 7 chains:

1. Matrix protein p15
   Short name=MA
2. RNA-binding phosphoprotein p12
   Alternative name(s):
   pp12
3. Capsid protein p30
   Short name=CA
4. Nucleocapsid protein p10
   Short name=NC-pol
5. Protease p14
   Short name=PR
   EC=3.4.23.-
6. Reverse transcriptase/ribonuclease H p80
   Short name=RT
   EC=2.7.7.49
   EC=2.7.7.7
   EC=3.1.26.4
7. Integrase p46
   Short name=IN

Gene names

Name:

gag-pol

Organism

Moloney murine leukemia virus (isolate Shinnick) (MoMLV) [Reference proteome]

Taxonomic identifier

928306 [NCBI]

Taxonomic lineage

Viruses › Retro-transcribing viruses › Retroviridae › Orthoretrovirinae › Gammaretrovirus › Mammalian virus group › Replication competent viruses › Murine leukemia virus › Moloney murine leukemia virus

Virus host

Mus musculus (Mouse) [TaxID: 10090]

Protein attributes

Sequence length	1738 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Gag-Pol polyprotein plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably link the viral protein to the host ESCRT pathway and facilitate release. Matrix protein p15 targets Gag and gag-pol polyproteins to the plasma membrane via a multipartite membrane binding signal, that includes its myristoylated N-terminus. Also mediates nuclear localization of the preintegration complex By similarity. Capsid protein p30 forms the spherical core of the virion that encapsulates the genomic RNA-nucleocapsid complex By similarity. Nucleocapsid protein p10 is involved in the packaging and encapsidation of two copies of the genome. Binds with high affinity to conserved UCUG elements within the packaging signal, located near the 5'-end of the genome. This binding is dependent on genome dimerization. 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 By similarity. Reverse transcriptase/ribonuclease H (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. Integrase catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions. This enzyme activity takes place after virion entry into a cell and reverse transcription of the RNA genome in dsDNA. The first step in the integration process is 3' processing. This step requires a complex comprising the viral genome, matrix protein and integrase. This complex is called the pre-integration complex (PIC). The integrase protein removes 2 nucleotides from each 3' end of the viral DNA, leaving recessed CA OH's at the 3' ends. In the second step that requires cell division, the PIC enters cell nucleus. In the third step, termed strand transfer, the integrase protein joins the previously processed 3' ends to the 5' ends of strands of target cellular DNA at the site of integration. The last step is viral DNA integration into host chromosome By similarity.
Catalytic activity	Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Endonucleolytic cleavage to 5'-phosphomonoester.
Cofactor	Binds 2 magnesium ions for reverse transcriptase polymerase activity By similarity. Binds 2 magnesium ions for ribonuclease H (RNase H) activity By similarity. Magnesium ions for integrase activity. Binds at least 1, maybe 2 magnesium ions By similarity.
Enzyme regulation	The viral protease p14 is most effciently inhibited by amprenavir, which is able to block Gag processing in MoLV-infected cells.
Subunit structure	Capsid protein p30 is a homohexamer, that further associates as homomultimer. The virus core is composed of a lattice formed from hexagonal rings, each containing six capsid monomers. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues. The reverse transcriptase is a monomer By similarity. Capsid protein p30 interacts with mouse UBE2I and mouse PIAS4. Reverse transcriptase/ribonuclease H p80 interacts (via RT and RNase domains) with host release factor ETF1; this interaction is essential for translational readthrough of amber codon between viral gag and pol genes. Gag-Pol polyprotein also interacts with host release factor ETF1. Ref.7 Ref.8 Ref.9
Subcellular location	Gag-Pol polyprotein: Host cell membrane; Lipid-anchor Potential. Matrix protein p15: Virion Potential. Capsid protein p30: Virion Potential. Nucleocapsid protein p10: Virion Potential.
Domain	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. RNA-binding phosphoprotein p12 contains one L domain: a PPXY motif which potentially interacts with the WW domain 3 of NEDD4 E3 ubiquitin ligase. PPXY motif is essential for virus egress. Matrix protein p15 contains one L domain: a PTAP/PSAP motif, which potentially interacts with the UEV domain of TSG101. The junction between the matrix protein p15 and RNA-binding phosphoprotein p12 also contains one L domain: a LYPX(n)L motif which potentially interacts with PDCD6IP. Both PSAP and LYPX(n)L domains might play little to no role in budding and possibly drive residual virus release. contains By similarity.
Post-translational modification	Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation By similarity. Ref.10 Capsid protein p30 is sumoylated; which is required for virus replication. Ref.9 RNA-binding phosphoprotein p12 is phosphorylated on serine residues. Ref.6
Miscellaneous	This protein is translated as a gag-pol fusion protein by episodic readthrough of the gag protein termination codon. Readthrough of the terminator codon TAG occurs between the codons for 538-Asp and 540-Gly. The nucleocapsid protein p10 released from Pol polyprotein (NC-pol) is a few amino acids shorter than the nucleocapsid protein p10 released from Gag polyprotein (NC-gag). 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 By similarity.
Sequence similarities	Contains 1 CCHC-type zinc finger. Contains 1 integrase catalytic domain. Contains 1 integrase-type DNA-binding domain. Contains 1 peptidase A2 domain. Contains 1 reverse transcriptase domain. Contains 1 RNase H domain.
Biophysicochemical properties	pH dependence: Optimum pH is 5.0 for protease activity.

Ontologies

Keywords
Biological process	DNA integration DNA recombination Host-virus interaction Viral genome integration Virus entry into host cell
Cellular component	Host cell membrane Host membrane Membrane Viral matrix protein Virion
Coding sequence diversity	RNA suppression of termination
Domain	Coiled coil Zinc-finger
Ligand	DNA-binding Magnesium Metal-binding RNA-binding Viral nucleoprotein Zinc
Molecular function	Aspartyl protease Capsid protein DNA-directed DNA polymerase Endonuclease Hydrolase Nuclease Nucleotidyltransferase Protease RNA-directed DNA polymerase Transferase
PTM	Lipoprotein Myristate Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	DNA integration Inferred from electronic annotation. Source: UniProtKB-KW DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW RNA-dependent DNA replication Inferred from electronic annotation. Source: InterPro establishment of integrated proviral latency Inferred from electronic annotation. Source: UniProtKB-KW nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC proteolysis Inferred from electronic annotation. Source: UniProtKB-KW viral entry into host cell Inferred from electronic annotation. Source: UniProtKB-KW virion assembly Inferred from electronic annotation. Source: InterPro
Cellular_component	host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: UniProtKB-KW viral capsid Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW DNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed DNA polymerase activity Inferred from electronic annotation. Source: UniProtKB-KW aspartic-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW ribonuclease H activity Inferred from electronic annotation. Source: EC structural molecule activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed; by host Ref.3

Chain

2 – 1738

1737

Gag-Pol polyprotein

PRO_0000390795

Chain

2 – 131

130

Matrix protein p15

PRO_5000053618

Chain

132 – 215

84

RNA-binding phosphoprotein p12

PRO_5000053619

Chain

216 – 478

263

Capsid protein p30

PRO_5000053620

Chain

479 – 534

56

Nucleocapsid protein p10

PRO_5000053621

Chain

535 – 659

125

Protease p14

PRO_5000053622

Chain

660 – 1330

671

Reverse transcriptase/ribonuclease H p80

PRO_5000053623

Chain

1331 – 1738

408

Integrase p46

PRO_5000053624

Regions

Domain

560 – 631

72

Peptidase A2

Domain

741 – 932

192

Reverse transcriptase

Domain

1174 – 1320

147

RNase H

Domain

1444 – 1602

159

Integrase catalytic

Zinc finger

502 – 519

18

CCHC-type

Coiled coil

438 – 478

41

Potential

Motif

111 – 114

4

PTAP/PSAP motif

Motif

130 – 134

5

LYPX(n)L motif

Motif

162 – 165

4

PPXY motif

Compositional bias

71 – 193

123

Pro-rich

Sites

Active site

566

1

Protease; shared with dimeric partner By similarity

Metal binding

809

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

883

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

884

1

Magnesium; catalytic; for reverse transcriptase activity By similarity

Metal binding

1183

1

Magnesium; for RNase H activity By similarity

Metal binding

1221

1

Magnesium; for RNase H activity By similarity

Metal binding

1242

1

Magnesium; for RNase H activity By similarity

Metal binding

1312

1

Magnesium; for RNase H activity By similarity

Metal binding

1455

1

Magnesium; catalytic; for integrase activity By similarity

Metal binding

1514

1

Magnesium; catalytic; for integrase activity By similarity

Site

131 – 132

2

Cleavage; by viral protease p14

Site

215 – 216

2

Cleavage; by viral protease p14

Site

478 – 479

2

Cleavage; by viral protease p14

Site

534 – 535

2

Cleavage; by viral protease p14

Site

659 – 660

2

Cleavage; by viral protease p14

Site

1330 – 1331

2

Cleavage; by viral protease p14

Amino acid modifications

Modified residue

192

1

Phosphoserine; by host Probable

Lipidation

2

1

N-myristoyl glycine; by host Ref.3

Experimental info

Mutagenesis

114

1

P → A: Slight reduction in the number of virus-like particles produced.

Mutagenesis

137

1

S → A: No effect on reverse transcription activity. Ref.6

Mutagenesis

148

1

S → A: No effect on reverse transcription activity; when associated with A-150. Ref.6

Mutagenesis

150

1

S → A: No effect on reverse transcription activity; when associated with A-148. Ref.6

Mutagenesis

165

1

Y → A: Drastic reduction in the number of virus-like particles produced. Ref.8

Mutagenesis

192

1

S → A: Complete loss of reverse transcription activity. Ref.6

Mutagenesis

192

1

S → D: Complete loss of reverse transcription activity. Ref.6

Mutagenesis

196

1

S → A: No effect on reverse transcription activity. Ref.6

Mutagenesis

209

1

S → A: Strongly reduced reverse transcription activity. Ref.6

Mutagenesis

209

1

S → D: Strongly reduced reverse transcription activity. Ref.6

Mutagenesis

212

1

S → A: No effect on reverse transcription activity. Ref.6

Secondary structure

1

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1738

Helix Strand Turn

Details...

Helix

684 – 687

4

Turn

689 – 691

3

Helix

693 – 696

4

Beta strand

702 – 704

3

Helix

727 – 742

16

Beta strand

745 – 749

5

Beta strand

757 – 760

4

Beta strand

763 – 766

4

Beta strand

769 – 772

4

Helix

775 – 778

4

Helix

791 – 795

5

Beta strand

804 – 810

7

Turn

811 – 813

3

Helix

814 – 816

3

Beta strand

817 – 819

3

Turn

821 – 823

3

Helix

824 – 827

4

Beta strand

829 – 833

5

Beta strand

834 – 836

3

Beta strand

839 – 846

8

Helix

854 – 865

12

Helix

867 – 872

6

Beta strand

877 – 881

5

Beta strand

884 – 891

8

Helix

892 – 909

18

Turn

915 – 917

3

Beta strand

919 – 927

9

Beta strand

930 – 933

4

Turn

952 – 954

3

Helix

955 – 961

7

Turn

962 – 966

5

Helix

977 – 979

3

Beta strand

1000 – 1002

3

Helix

1005 – 1009

5

Beta strand

1019 – 1021

3

Beta strand

1028 – 1033

6

Beta strand

1035 – 1040

6

Turn

1045 – 1048

4

Beta strand

1063 – 1065

3

Helix

1070 – 1083

14

Helix

1084 – 1086

3

Beta strand

1091 – 1094

4

Turn

1099 – 1102

4

Beta strand

1103 – 1105

3

Turn

1106 – 1110

5

Beta strand

1128 – 1131

4

Beta strand

1169 – 1171

3

Beta strand

1177 – 1189

13

Beta strand

1192 – 1200

9

Beta strand

1205 – 1211

7

Helix

1217 – 1231

15

Turn

1232 – 1234

3

Beta strand

1235 – 1241

7

Helix

1244 – 1249

6

Helix

1273 – 1282

10

Beta strand

1285 – 1293

9

Helix

1303 – 1321

19

Helix

1346 – 1355

10

Beta strand

1358 – 1360

3

Turn

1361 – 1364

4

Beta strand

1365 – 1368

4

Beta strand

1371 – 1374

4

Helix

1376 – 1390

15

Helix

1394 – 1404

11

Beta strand

1407 – 1410

4

Helix

1413 – 1423

11

Helix

1425 – 1431

7

Sequences

	Sequence		Length	Mass (Da)
	P03355 [UniParc]. Last modified July 13, 2010. Version 4. Checksum: EDE353E6B09F91C6	FASTA	1,738	194,841
	10 20 30 40 50 60 MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL 70 80 90 100 110 120 ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP 130 140 150 160 170 180 PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG 190 200 210 220 230 240 EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN 250 260 270 280 290 300 NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 310 320 330 340 350 360 PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG 370 380 390 400 410 420 PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL 430 440 450 460 470 480 GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT 490 500 510 520 530 540 VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDDGG 550 560 570 580 590 600 GQGQEPPPEP RITLKVGGQP VTFLVDTGAQ HSVLTQNPGP LSDKSAWVQG ATGGKRYRWT 610 620 630 640 650 660 TDRKVHLATG KVTHSFLHVP DCPYPLLGRD LLTKLKAQIH FEGSGAQVMG PMGQPLQVLT 670 680 690 700 710 720 LNIEDEHRLH ETSKEPDVSL GSTWLSDFPQ AWAETGGMGL AVRQAPLIIP LKATSTPVSI 730 740 750 760 770 780 KQYPMSQEAR LGIKPHIQRL LDQGILVPCQ SPWNTPLLPV KKPGTNDYRP VQDLREVNKR 790 800 810 820 830 840 VEDIHPTVPN PYNLLSGLPP SHQWYTVLDL KDAFFCLRLH PTSQPLFAFE WRDPEMGISG 850 860 870 880 890 900 QLTWTRLPQG FKNSPTLFDE ALHRDLADFR IQHPDLILLQ YVDDLLLAAT SELDCQQGTR 910 920 930 940 950 960 ALLQTLGNLG YRASAKKAQI CQKQVKYLGY LLKEGQRWLT EARKETVMGQ PTPKTPRQLR 970 980 990 1000 1010 1020 EFLGTAGFCR LWIPGFAEMA APLYPLTKTG TLFNWGPDQQ KAYQEIKQAL LTAPALGLPD 1030 1040 1050 1060 1070 1080 LTKPFELFVD EKQGYAKGVL TQKLGPWRRP VAYLSKKLDP VAAGWPPCLR MVAAIAVLTK 1090 1100 1110 1120 1130 1140 DAGKLTMGQP LVILAPHAVE ALVKQPPDRW LSNARMTHYQ ALLLDTDRVQ FGPVVALNPA 1150 1160 1170 1180 1190 1200 TLLPLPEEGL QHNCLDILAE AHGTRPDLTD QPLPDADHTW YTDGSSLLQE GQRKAGAAVT 1210 1220 1230 1240 1250 1260 TETEVIWAKA LPAGTSAQRA ELIALTQALK MAEGKKLNVY TDSRYAFATA HIHGEIYRRR 1270 1280 1290 1300 1310 1320 GLLTSEGKEI KNKDEILALL KALFLPKRLS IIHCPGHQKG HSAEARGNRM ADQAARKAAI 1330 1340 1350 1360 1370 1380 TETPDTSTLL IENSSPYTSE HFHYTVTDIK DLTKLGAIYD KTKKYWVYQG KPVMPDQFTF 1390 1400 1410 1420 1430 1440 ELLDFLHQLT HLSFSKMKAL LERSHSPYYM LNRDRTLKNI TETCKACAQV NASKSAVKQG 1450 1460 1470 1480 1490 1500 TRVRGHRPGT HWEIDFTEIK PGLYGYKYLL VFIDTFSGWI EAFPTKKETA KVVTKKLLEE 1510 1520 1530 1540 1550 1560 IFPRFGMPQV LGTDNGPAFV SKVSQTVADL LGIDWKLHCA YRPQSSGQVE RMNRTIKETL 1570 1580 1590 1600 1610 1620 TKLTLATGSR DWVLLLPLAL YRARNTPGPH GLTPYEILYG APPPLVNFPD PDMTRVTNSP 1630 1640 1650 1660 1670 1680 SLQAHLQALY LVQHEVWRPL AAAYQEQLDR PVVPHPYRVG DTVWVRRHQT KNLEPRWKGP 1690 1700 1710 1720 1730 YTVLLTTPTA LKVDGIAAWI HAAHVKAADP GGGPSSRLTW RVQRSQNPLK IRLTREAP

References

[1]	"Nucleotide sequence of Moloney murine leukaemia virus." Shinnick T.M., Lerner R.A., Sutcliffe J.G. Nature 293:543-548(1981) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA] (CLONE PMLV-1).
[2]	Chappey C. Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA].
[3]	"Myristyl amino-terminal acylation of murine retrovirus proteins: an unusual post-translational proteins modification." Henderson L.E., Krutzsch H.C., Oroszlan S. Proc. Natl. Acad. Sci. U.S.A. 80:339-343(1983) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-31, MYRISTOYLATION AT GLY-2.
[4]	"Primary structure of the low molecular weight nucleic acid-binding proteins of murine leukemia viruses." Henderson L.E., Copeland T.D., Sowder R.C., Smythers G.W., Oroszlan S. J. Biol. Chem. 256:8400-8406(1981) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 479-529.
[5]	"Murine leukemia virus protease is encoded by the gag-pol gene and is synthesized through suppression of an amber termination codon." Yoshinaka Y., Katoh I., Copeland T.D., Oroszlan S. Proc. Natl. Acad. Sci. U.S.A. 82:1618-1622(1985) [PubMed] [Europe PMC] [Abstract] Cited for: READTHROUGH OF AMBER CODON.
[6]	"Phosphorylated serine residues and an arginine-rich domain of the moloney murine leukemia virus p12 protein are required for early events of viral infection." Yueh A., Goff S.P. J. Virol. 77:1820-1829(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-192, MUTAGENESIS OF SER-137; SER-148; SER-150; SER-192; SER-196; SER-209 AND SER-212.
[7]	"Reverse transcriptase of Moloney murine leukemia virus binds to eukaryotic release factor 1 to modulate suppression of translational termination." Orlova M., Yueh A., Leung J., Goff S.P. Cell 115:319-331(2003) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION OF REVERSE TRANSCRIPTASE/RIBONUCLEASE H P80 WITH MOUSE RELEASE FACTOR ETF1, INTERACTION OF GAG-POL POLYPROTEIN WITH MOUSE RELEASE FACTOR ETF1.
[8]	"Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding." Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E. J. Biol. Chem. 280:27004-27012(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MOUSE NEDD4; TSG101 AND PDCD6IP/ALIX, MUTAGENESIS OF TYR-165.
[9]	"Interaction of moloney murine leukemia virus capsid with Ubc9 and PIASy mediates SUMO-1 addition required early in infection." Yueh A., Leung J., Bhattacharyya S., Perrone L.A., de los Santos K., Pu S.-Y., Goff S.P. J. Virol. 80:342-352(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH UBE2I AND PIAS4, SUMOYLATION.
[10]	"Characterization of the murine leukemia virus protease and its comparison with the human immunodeficiency virus type 1 protease." Feher A., Boross P., Sperka T., Miklossy G., Kadas J., Bagossi P., Oroszlan S., Weber I.T., Tozser J. J. Gen. Virol. 87:1321-1330(2006) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF PROTEASE P14, PROTEOLYTIC PROCESSING OF POLYPROTEIN.
[11]	"Mechanistic implications from the structure of a catalytic fragment of Moloney murine leukemia virus reverse transcriptase." Georgiadis M.M., Jessen S.M., Ogata C.M., Telesnitsky A., Goff S.P., Hendrickson W.A. Structure 3:879-892(1995) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 683-937.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF033811 Genomic RNA. Translation: AAC82568.1. Sequence problems.
J02255 Genomic RNA. No translation available.

PIR

GNMV1M. A03956.

RefSeq

NP_057933.2. NC_001501.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1D0E	X-ray	3.00	A/B	683-937	[»]
1D1U	X-ray	2.30	A	683-937	[»]
1I6J	X-ray	2.00	A	683-937	[»]
1MML	X-ray	1.80	A	669-933	[»]
1N4L	X-ray	2.00	A	683-937	[»]
1NND	X-ray	2.30	A	683-937	[»]
1QAI	X-ray	2.30	A/B	669-933	[»]
1QAJ	X-ray	2.30	A/B	683-937	[»]
1RW3	X-ray	3.00	A	683-1133	[»]
1ZTT	X-ray	1.85	A	683-937	[»]
1ZTW	X-ray	1.80	A	683-937	[»]
2FJV	X-ray	2.05	A	683-937	[»]
2FJW	X-ray	1.95	A	683-937	[»]
2FJX	X-ray	1.80	A	683-937	[»]
2FVP	X-ray	2.25	A	683-937	[»]
2FVQ	X-ray	2.30	A	683-937	[»]
2FVR	X-ray	2.20	A	683-937	[»]
2FVS	X-ray	2.35	A	683-937	[»]
2HB5	X-ray	1.59	A	1157-1330	[»]
2R2R	X-ray	2.10	A	683-937	[»]
2R2S	X-ray	2.80	A	683-937	[»]
2R2T	X-ray	2.00	A	683-937	[»]
2R2U	X-ray	2.30	A	683-937	[»]
3FSI	X-ray	1.75	A	683-937	[»]
3NNQ	X-ray	2.69	A/B	1331-1435	[»]

ProteinModelPortal

P03355.

ModBase

Search...

Protein family/group databases

MEROPS

A02.008.

PTM databases

PhosphoSite

P03355.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

Gene3D

1.10.150.180. 1 hit.
1.10.375.10. 1 hit.
2.40.70.10. 1 hit.
4.10.60.10. 1 hit.

InterPro

IPR000840. G_retro_matrix_N.
IPR002079. Gag_p12.
IPR003036. Gag_p30.
IPR001584. Integrase_cat-core.
IPR018061. Pept_A2A_retrovirus_sg.
IPR001995. Peptidase_A2_cat.
IPR021109. Peptidase_aspartic.
IPR001969. Peptidase_aspartic_AS.
IPR008919. Retrov_capsid_N.
IPR010999. Retrovr_matrix_N.
IPR012337. RNaseH-like_dom.
IPR002156. RNaseH_domain.
IPR000477. RVT.
IPR001878. Znf_CCHC.
[Graphical view]

Pfam

PF01140. Gag_MA. 1 hit.
PF01141. Gag_p12. 1 hit.
PF02093. Gag_p30. 1 hit.
PF00075. RNase_H. 1 hit.
PF00665. rve. 1 hit.
PF00077. RVP. 1 hit.
PF00078. RVT_1. 1 hit.
[Graphical view]

SMART

SM00343. ZnF_C2HC. 1 hit.
[Graphical view]

SUPFAM

SSF50630. Pept_Aspartic. 1 hit.
SSF47943. Retrov_capsid_N. 1 hit.
SSF47836. Retrovir_matrix. 1 hit.
SSF53098. RNaseH_fold. 2 hits.
SSF57756. SSF57756. 1 hit.

PROSITE

PS50175. ASP_PROT_RETROV. 1 hit.
PS00141. ASP_PROTEASE. 1 hit.
PS50994. INTEGRASE. 1 hit.
PS50879. RNASE_H. 1 hit.
PS50878. RT_POL. 1 hit.
PS50158. ZF_CCHC. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL3562.

EvolutionaryTrace

P03355.

PMAP-CutDB

O92808.

Entry information

Entry name

POL_MLVMS

Accession

Primary (citable) accession number: P03355
Secondary accession number(s): O92808

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 13, 2010
Last modified:	April 3, 2013
This is version 127 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program