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InterPro: IPR012344 Matrix protein, N-terminal, lentiviral and alpha-retroviral

Protein matchesHelp
UniProtKB
Matches:
21631 proteins
AccessionHelp IPR012344 Matrix_N_HIV/RSV
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR010999 Retroviral matrix, N-terminal
Children IPR000071 Immunodeficiency lentiviral matrix, N-terminal
IPR014834 Gag protein p15
Found in IPR004028 Retroviral Gag polyprotein, M
GO Term annotationHelp
Function GO:0005198 structural molecule activity
Component GO:0019028 viral capsid
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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].

Structural linksHelp
CATH: 1.10.150.90

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR012344 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
O12158 Gag-Pol polyprotein

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR010999 Retroviral matrix, N-terminal
IPR003308 Integrase, N-terminal zinc-binding domain
IPR010661 Reverse transcriptase thumb
IPR012337 Polynucleotidyl transferase, ribonuclease H fold
IPR000477 RNA-directed DNA polymerase (reverse transcriptase)
IPR013084 Zinc finger, CCHC retroviral-type
IPR008919 Retrovirus capsid, N-terminal core
IPR000071 Immunodeficiency lentiviral matrix, N-terminal
IPR000721 Retroviral nucleocapsid protein Gag
IPR001584 Integrase, catalytic core
IPR012344 Matrix protein, N-terminal, lentiviral and alpha-retroviral
IPR002156 Ribonuclease H
IPR008916 Retrovirus capsid, C-terminal
IPR001878 Zinc finger, CCHC-type
IPR018061 Peptidase A2A, retrovirus RVP subgroup
IPR017856 Integrase, N-terminal zinc-binding domain-like
IPR001995 Peptidase A2A, retrovirus, catalytic
IPR001037 Integrase, C-terminal, retroviral
IPR001969 Peptidase aspartic, active site
IPR009007 Peptidase aspartic, catalytic
IPR010659 Reverse transcriptase connection
PDB Chain
CATH Domain
SWISS-MODEL

PublicationsHelp
1. 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
2. Freed EO.
HIV-1 replication.
Somat. Cell Mol. Genet. 26 13-33 2001 [PubMed: 12465460]
http://dx.doi.org/10.1023/A:1021070512287
3. 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
4. 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
5. 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

Additional ReadingHelp
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
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
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
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