Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-928306-01085
Entry Name
UniProt Accession
Theoretical PI
8.6
Molecular Weight
60858.3
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Nucleocapsid protein p10
Protein Synonyms/Alias
Pr65gag; Core polyprotein; MA; pp12; CA; NC-gag;
Gene Name
gag
Gene Synonyms/Alias
Created Date
21-JUL-1986
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQTVTTPL
[1][2]
N-Myristoylation
Organism
Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
NCBI Taxa ID
928306
Reference
[1] Jacobs E, Gheysen D, Thines D, Francotte M, de Wilde M. The HIV-1 Gagprecursor Pr55gag synthesized in yeast is myristoylated and targeted to theplasma membrane. Gene. 1989 Jun 30;79(1):71-81.[PMID:2673935]
[2] Henderson LE, Krutzsch HC, Oroszlan S. Myristyl amino-terminal acylation ofmurine retrovirus proteins: an unusual post-translational proteins modification. Proc Natl Acad Sci U S A. 1983 Jan;80(2):339-43.[PMID:6340098]
Functional Description
Gag 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.
Sequence Annotation
Region: 345 393 Interaction with mouse PIAS4.
Region: 430 435 Interaction with mouse UBE2I.
Motif: 111 114 PTAP/PSAP motif.
Motif: 130 134 LYPX(n)L motif.
Motif: 162 165 PPXY motif.
Functional site: 131 132 Cleavage; by viral protease p14.
Functional site: 215 216 Cleavage; by viral protease p14.
Functional site: 478 479 Cleavage; by viral protease p14.
Modified residue: 192 192 Phosphoserine; by host.
Protein Length
538 AA.
Protein Sequence
(Canonical)
MGQTVTTPLS LTLGHWKDVE RIAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL  60
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLP PSAPSLPLEP  120
PRSTPPRSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGNGG  180
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRAG GNGQLQYWPF SSSDLYNWKN  240
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR  300
PTQLPNEVDA AFPLERPDWD YTTQAGRNHL VHYRQLLLAG LQNAGRSPTN LAKVKGITQG  360
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLKNKTL  420
GDLVREAEKI FNKRETPEER EERIRRETEE KEERRRTEDE QKEKERDRRR HREMSKLLAT  480
VVSGQKQDRQ GGERRRSQLD RDQCAYCKEK GHWAKDCPKK PRGPRGPRPQ TSLLTLDD    538
FASTA
(Canonical)
>LipidDB-928306-01085|P03332
MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDL
ITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEP
PRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGG
EATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKN
NNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGR
PTQLPNEVDAAFPLERPDWDYTTQAGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQG
PNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTL
GDLVREAEKIFNKRETPEEREERIRRETEEKEERRRTEDEQKEKERDRRRHREMSKLLAT
VVSGQKQDRQGGERRRSQLDRDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLDD
Gene Ontology
GO:0044174; C:host cell endosome; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW
GO:0003723; F:RNA binding; IEA:UniProtKB-KW
GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0039702; P:viral budding via host ESCRT complex; IEA:UniProtKB-KW
GO:0019076; P:viral release from host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR000840; G_retro_matrix_N
InterPro; IPR002079; Gag_p12
InterPro; IPR003036; Gag_P30
InterPro; IPR008919; Retrov_capsid_N
InterPro; IPR010999; Retrovr_matrix_N
InterPro; IPR001878; Znf_CCHC
Pfam
Pfam; PF01140; Gag_MA;
Pfam; PF01141; Gag_p12;
Pfam; PF02093; Gag_p30;
Pfam; PF00098; zf-CCHC;
SMART
SMART; SM00343; ZnF_C2HC;
PROSITE
PROSITE; PS50158; ZF_CCHC;
PRINTS