Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10886-00347
Entry Name
UniProt Accession
Theoretical PI
5.02
Molecular Weight
76270.67
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Outer capsid protein mu-1C
Protein Synonyms/Alias
Mu1;
Gene Name
M2
Gene Synonyms/Alias
Created Date
01-JUL-1989
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNASSIVQ
[1]
N-Myristoylation
Organism
Reovirus type 3 (strain Dearing) (T3D) (Mammalian orthoreovirus 3)
NCBI Taxa ID
10886
Reference
[1] Tillotson L, Shatkin AJ. Reovirus polypeptide sigma 3 and N-terminalmyristoylation of polypeptide mu 1 are required for site-specific cleavage to mu 1C in transfected cells. J Virol. 1992 Apr;66(4):2180-6.[PMID:1548757]
Functional Description
Major outer capsid protein involved in host cell membrane penetration. In the endocytic compartment, outer-capsid protein sigma-3 is removed by cathepsin proteases, which exposes the viral membrane-penetration protein mu-1. Both myristoylated peptides mu-1N and phi are released during infectious subvirion particles (ISVP) formation in the endosome. They associate with host membranes and mu-1N induces permeabilization and delivery of transcriptionally active viral particles into the host cell cytoplasm. Seems to induce apoptosis in the host cell (By similarity).
Sequence Annotation
Functional site: 42 43 Cleavage.
Protein Length
708 AA.
Protein Sequence
(Canonical)
MGNASSIVQT INVTGDGNVF KPSAETSSTA VPSLSLSPGM LNPGGVPWIA VGDETSVTSP  60
GALRRMTSKD IPETAIINTD NSSGAVPSES ALVPYIDEPL VVVTEHAITN FTKAEMALEF  120
NREFLDKMRV LSVSPKYSDL LTYVDCYVGV SARQALNNFQ KQVPVITPTR QTMYVDSIQA  180
ALKALEKWEI DLRVAQTLLP TNVPIGEVSC PMQSVVKLLD DQLPDDSLIR RYPKEAAVAL  240
AKRNGGIQWM DVSEGTVMNE AVNAVAASAL APSASAPPLE EKSKLTEQAM DLVTAAEPEI  300
IASLAPVPAP VFAIPPKPAD YNVRTLRIDE ATWLRMIPKS MNTPFQIQVT DNTGTNWHLN  360
LRGGTRVVNL DQIAPMRFVL DLGGKSYKET SWDPNGKKVG FIVFQSKIPF ELWTAASQIG  420
QATVVNYVQL YAEDSSFTAQ SIIATTSLAY NYEPEQLNKT DPEMNYYLLA TFIDSAAITP  480
TNMTQPDVWD ALLTMSPLSA GEVTVKGAVV SEVVPADLIG SYTPESLNAS LPNDAARCMI  540
DRASKIAEAI KIDDDAGPDE YSPNSVPIQG QLAISQLETG YGVRIFNPKG ILSKIASRAM  600
QAFIGDPSTI ITQAAPVLSD KNNWIALAQG VKTSLRTKSL SAGVKTAVSK LSSSESIQNW  660
TQGFLDKVSA HFPAPKPDCP TSGDSGESSN RRVKRDSYAG VVKRGYTR               708
FASTA
(Canonical)
>LipidDB-10886-00347|P11078
MGNASSIVQTINVTGDGNVFKPSAETSSTAVPSLSLSPGMLNPGGVPWIAVGDETSVTSP
GALRRMTSKDIPETAIINTDNSSGAVPSESALVPYIDEPLVVVTEHAITNFTKAEMALEF
NREFLDKMRVLSVSPKYSDLLTYVDCYVGVSARQALNNFQKQVPVITPTRQTMYVDSIQA
ALKALEKWEIDLRVAQTLLPTNVPIGEVSCPMQSVVKLLDDQLPDDSLIRRYPKEAAVAL
AKRNGGIQWMDVSEGTVMNEAVNAVAASALAPSASAPPLEEKSKLTEQAMDLVTAAEPEI
IASLAPVPAPVFAIPPKPADYNVRTLRIDEATWLRMIPKSMNTPFQIQVTDNTGTNWHLN
LRGGTRVVNLDQIAPMRFVLDLGGKSYKETSWDPNGKKVGFIVFQSKIPFELWTAASQIG
QATVVNYVQLYAEDSSFTAQSIIATTSLAYNYEPEQLNKTDPEMNYYLLATFIDSAAITP
TNMTQPDVWDALLTMSPLSAGEVTVKGAVVSEVVPADLIGSYTPESLNASLPNDAARCMI
DRASKIAEAIKIDDDAGPDEYSPNSVPIQGQLAISQLETGYGVRIFNPKGILSKIASRAM
QAFIGDPSTIITQAAPVLSDKNNWIALAQGVKTSLRTKSLSAGVKTAVSKLSSSESIQNW
TQGFLDKVSAHFPAPKPDCPTSGDSGESSNRRVKRDSYAGVVKRGYTR
Gene Ontology
GO:0044165; C:host cell endoplasmic reticulum; IEA:UniProtKB-KW
GO:0033650; C:host cell mitochondrion; IEA:UniProtKB-KW
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0039624; C:viral outer capsid; IEA:UniProtKB-KW
GO:0046812; F:host cell surface binding; IEA:InterPro
GO:0006915; P:apoptotic process; IEA:UniProtKB-KW
GO:0009405; P:pathogenesis; IEA:InterPro
GO:0039665; P:permeabilization of host organelle membrane involved in viral entry into host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR009113; Mu1/VP4
InterPro; IPR015962; Mu1_membr_pen_a-bundle_sub2
InterPro; IPR015961; Mu1_membr_pen_a/b_sub
InterPro; IPR015960; Mu1_membr_pen_b-sand_sub
Pfam
Pfam; PF05993; Reovirus_M2;
SMART
PROSITE
PRINTS