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InterPro: IPR012344 Matrix protein, N-terminal, lentiviral and alpha-retroviral
Protein matches
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UniProtKB Matches: 21631 proteins |
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Accession
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IPR012344 Matrix_N_HIV/RSV |
Type
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Domain |
Signatures
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InterPro Relationships
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Parent
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IPR010999 Retroviral matrix, N-terminal
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Children
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IPR000071 Immunodeficiency lentiviral matrix, N-terminal
IPR014834 Gag protein p15
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Found in
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IPR004028 Retroviral Gag polyprotein, M
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GO Term annotation
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Function
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GO:0005198 structural molecule activity
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Component
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GO:0019028 viral capsid
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Retroviral matrix proteins (or major core proteins) are components of envelope-associated capsids, which line the inner surface of virus envelopes and are associated with viral membranes [1]. Matrix proteins are produced as part of Gag precursor polyproteins. During viral maturation, the Gag polyprotein is cleaved into major structural proteins by the viral protease, yielding the matrix (MA), capsid (CA), nucleocapsid (NC), and some smaller peptides. Gag-derived proteins govern the entire assembly and release of the virus particles, with matrix proteins playing key roles in Gag stability, capsid assembly, transport and budding. Although matrix proteins from different retroviruses appear to perform similar functions and can have similar structural folds, their primary sequences can be very different. This entry represents matrix proteins from primate lentiviruses, such as
human and simian immunodeficiency viruses (HIV and SIV, respectively), equine lentiviruses, such as
Equine infectious anemia virus (EIAV), and
avian alpha-retroviruses such as
Rous sarcoma virus (RSV), and type C retroviruses, such as
Avian sarcoma virus, respectively [2, 3, 4]. This entry also identifies matrix proteins from several eukaryotic endogenous retroviruses, which arise when one or more copies of the retroviral genome becomes integrated into the host genome [5].
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Structural links
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Example proteins
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O12158 Gag-Pol polyprotein
More proteins
Example Proteins Key
| InterPro entry accession number/name and structure databases |
Colour code |
| IPR010999 |
Retroviral matrix, N-terminal |
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| IPR003308 |
Integrase, N-terminal zinc-binding domain |
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| IPR010661 |
Reverse transcriptase thumb |
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| IPR012337 |
Polynucleotidyl transferase, ribonuclease H fold |
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| IPR000477 |
RNA-directed DNA polymerase (reverse transcriptase) |
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| IPR013084 |
Zinc finger, CCHC retroviral-type |
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| IPR008919 |
Retrovirus capsid, N-terminal core |
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| IPR000071 |
Immunodeficiency lentiviral matrix, N-terminal |
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| IPR000721 |
Retroviral nucleocapsid protein Gag |
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| IPR001584 |
Integrase, catalytic core |
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| IPR012344 |
Matrix protein, N-terminal, lentiviral and alpha-retroviral |
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| IPR002156 |
Ribonuclease H |
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| IPR008916 |
Retrovirus capsid, C-terminal |
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| IPR001878 |
Zinc finger, CCHC-type |
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| IPR018061 |
Peptidase A2A, retrovirus RVP subgroup |
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| IPR017856 |
Integrase, N-terminal zinc-binding domain-like |
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| IPR001995 |
Peptidase A2A, retrovirus, catalytic |
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| IPR001037 |
Integrase, C-terminal, retroviral |
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| IPR001969 |
Peptidase aspartic, active site |
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| IPR009007 |
Peptidase aspartic, catalytic |
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| IPR010659 |
Reverse transcriptase connection |
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PDB Chain |
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CATH Domain |
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SWISS-MODEL |
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Publications
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1.
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Conte MR, Matthews S.
Retroviral matrix proteins: a structural perspective.
Virology 246 191-8 1998
[PubMed: 9657938]
http://dx.doi.org/10.1006/viro.1998.9206
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2.
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Freed EO.
HIV-1 replication.
Somat. Cell Mol. Genet. 26 13-33 2001
[PubMed: 12465460]
http://dx.doi.org/10.1023/A:1021070512287
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3.
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Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI.
Structure of equine infectious anemia virus matrix protein.
J. Virol. 76 1876-83 2002
[PubMed: 11799182]
http://dx.doi.org/10.1128/JVI.76.4.1876-1883.2002
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4.
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Garbitt RA, Bone KR, Parent LJ.
Insertion of a classical nuclear import signal into the matrix domain of the Rous sarcoma virus Gag protein interferes with virus replication.
J. Virol. 78 13534-42 2004
[PubMed: 15564464]
http://dx.doi.org/10.1128/JVI.78.24.13534-13542.2004
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5.
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Gifford R, Tristem M.
The evolution, distribution and diversity of endogenous retroviruses.
Virus Genes 26 291-315 2003
[PubMed: 12876457]
http://dx.doi.org/10.1023/A:1024455415443
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Additional Reading
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Rao Z, Belyaev AS, Fry E, Roy P, Jones IM, Stuart DI.
Crystal structure of SIV matrix antigen and implications for virus assembly.
Nature 378 1995 743-7
[PubMed: 7501025]
http://dx.doi.org/10.1038/378743a0
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Saad JS, Loeliger E, Luncsford P, Liriano M, Tai J, Kim A, Miller J, Joshi A, Freed EO, Summers MF.
Point mutations in the HIV-1 matrix protein turn off the myristyl switch.
J. Mol. Biol. 366 2007 574-85
[PubMed: 17188710]
http://dx.doi.org/10.1016/j.jmb.2006.11.068
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McDonnell JM, Fushman D, Cahill SM, Zhou W, Wolven A, Wilson CB, Nelle TD, Resh MD, Wills J, Cowburn D.
Solution structure and dynamics of the bioactive retroviral M domain from Rous sarcoma virus.
J. Mol. Biol. 279 1998 921-8
[PubMed: 9642071]
http://dx.doi.org/10.1006/jmbi.1998.1788
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Tang C, Ndassa Y, Summers MF.
Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein.
Nat. Struct. Biol. 9 2002 537-43
[PubMed: 12032547]
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InterPro 23.1
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