| Tag |
Content |
LipidDB ID |
LipidDB-11809-01087 |
Entry Name |
|
UniProt Accession |
|
Theoretical PI |
6.28 |
Molecular Weight |
61209.46 |
Genbank Protein ID |
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Genbank Nucleotide ID |
|
Protein Name |
Nucleocapsid protein p10 |
Protein Synonyms/Alias |
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] | N-Myristoylation |
|
Organism |
Moloney murine sarcoma virus (MoMSV) |
NCBI Taxa ID |
11809 |
Reference |
[1] 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 (By similarity). |
Sequence Annotation |
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.
Functional site: 215 216 Cleavage; by viral protease.
Functional site: 478 479 Cleavage; by viral protease.
|
Protein Length |
538 AA. |
Protein Sequence
(Canonical) |
MGQTVTTPLS LTLDHWKDVE RLAHNQSVDV KKRRWVTFCS AEWPTFNVGW PRDGTFNRDL 60
ITQVKIKVFS PGPHGHPDQV PYIVTWEALA FDPPPWVKPF VHPKPPPPLL PSAPSLPLEP 120
PLSTPPQSSL YPALTPSLGA KPKPQVLSDS GGPLIDLLTE DPPPYRDPRP PPSDRDGDSG 180
EATPAGEAPD PSPMASRLRG RREPPVADST TSQAFPLRTG GNGQLQYWPF SSSDLYNWKN 240
NNPSFSEDPG KLTALIESVL ITHQPTWDDC QQLLGTLLTG EEKQRVLLEA RKAVRGDDGR 300
PTQLPNEVDA AFPLERPDWE YTTQAGRNHL VHYRQLLIAG LQNAGRSPTN LAKVKGITQG 360
PNESPSAFLE RLKEAYRRYT PYDPEDPGQE TNVSMSFIWQ SAPDIGRKLE RLEDLRNKTL 420
GDLVREAERI FNKRETPEER EERIRREREE KEERRRTEDE QKEKERDRRR HREMSRLLAT 480
VVSGQRQDRQ EGERRRSQLD CDQCTYCEEQ GHWAKDCPRR PRGPRGPRPQ TSLLTLDD 538
|
FASTA
(Canonical) |
>LipidDB-11809-01087|P03334
MGQTVTTPLSLTLDHWKDVERLAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDL
ITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLLPSAPSLPLEP
PLSTPPQSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGDSG
EATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRTGGNGQLQYWPFSSSDLYNWKN
NNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGR
PTQLPNEVDAAFPLERPDWEYTTQAGRNHLVHYRQLLIAGLQNAGRSPTNLAKVKGITQG
PNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLRNKTL
GDLVREAERIFNKRETPEEREERIRREREEKEERRRTEDEQKEKERDRRRHREMSRLLAT
VVSGQRQDRQEGERRRSQLDCDQCTYCEEQGHWAKDCPRRPRGPRGPRPQTSLLTLDD
|
Gene Ontology |
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:0003676; F:nucleic acid binding; IEA:InterPro 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 |
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Pfam |
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SMART |
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PROSITE |
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PRINTS |
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