Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-11619-00333
Entry Name
UniProt Accession
Theoretical PI
8.71
Molecular Weight
55607.35
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Glycoprotein G2
Protein Synonyms/Alias
SSP; GP1; GP2;
Gene Name
GPC
Gene Synonyms/Alias
GP-C;
Created Date
01-MAY-1992
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGQFISFMQ
[1]
N-Myristoylation
Organism
Junin arenavirus (JUNV)
NCBI Taxa ID
11619
Reference
[1] York J, Romanowski V, Lu M, Nunberg JH. The signal peptide of the Junínarenavirus envelope glycoprotein is myristoylated and forms an essential subunit of the mature G1-G2 complex. J Virol. 2004 Oct;78(19):10783-92.[PMID:15367645]
Functional Description
Stable signal peptide (SSP) is cleaved but is apparently retained as the third component of the GP complex. The SSP is required for efficient glycoprotein expression, post-translational cleavage of GP1 and GP2, glycoprotein transport to the cell plasma membrane, formation of infectious virus particles, and acid pH- dependent glycoprotein-mediated cell fusion (By similarity).
Sequence Annotation
Topological domain: 2 17 Extracellular.
Transmembrane: 18 32 Helical.
Topological domain: 33 33 Cytoplasmic.
Transmembrane: 34 53 Helical.
Topological domain: 54 58 Extracellular.
Topological domain: 59 424 Extracellular.
Transmembrane: 425 445 Helical.
Topological domain: 446 485 Cytoplasmic.
Region: 476 477 Involved in ER localization.
Region: 482 483 Involved in ER localization.
Functional site: 58 59 Cleavage; by host signal peptidase.
Functional site: 251 252 Cleavage; by host MBTPS1.
Protein Length
485 AA.
Protein Sequence
(Canonical)
MGQFISFMQE IPTFLQEALN IALVAVSLIA IIKGVVNLYK SGLFQFFVFL ALAGRSCTEE  60
AFKIGLHTEF QTVSFSMVGL FSNNPHDLPL LCTLNKSHLY IKGGNASFKI SFDDIAVLLP  120
EYDVIIQHPA DMSWCSKSDD QIWLSQWFMN AVGHDWYLDP PFLCRNRTKT EGFIFQVNTS  180
KTGINENYAK KFKTGMHHLY REYPDSCLDG KLCLMKAQPT SWPLQCPLDH VNTLHFLTRG  240
KNIQLPRRSL KAFFSWSLTD SSGKDTPGGY CLEEWMLVAA KMKCFGNTAV AKCNLNHDSE  300
FCDMLRLFDY NKNAIKTLND ETKKQVNLMG QTINALISDN LLMKNKIREL MSVPYCNYTK  360
FWYVNHTLSG QHSLPRCWLI KNNSYLNISD FRNDWILESD FLISEMLSKE YSDRQGKTPL  420
TLVDICFWST VFFTASLFLH LVGIPTHRHI RGEACPLPHR LNSLGGCRCG KYPNLKKPTV  480
WRRGH                                                              485
FASTA
(Canonical)
>LipidDB-11619-00333|P26313
MGQFISFMQEIPTFLQEALNIALVAVSLIAIIKGVVNLYKSGLFQFFVFLALAGRSCTEE
AFKIGLHTEFQTVSFSMVGLFSNNPHDLPLLCTLNKSHLYIKGGNASFKISFDDIAVLLP
EYDVIIQHPADMSWCSKSDDQIWLSQWFMNAVGHDWYLDPPFLCRNRTKTEGFIFQVNTS
KTGINENYAKKFKTGMHHLYREYPDSCLDGKLCLMKAQPTSWPLQCPLDHVNTLHFLTRG
KNIQLPRRSLKAFFSWSLTDSSGKDTPGGYCLEEWMLVAAKMKCFGNTAVAKCNLNHDSE
FCDMLRLFDYNKNAIKTLNDETKKQVNLMGQTINALISDNLLMKNKIRELMSVPYCNYTK
FWYVNHTLSGQHSLPRCWLIKNNSYLNISDFRNDWILESDFLISEMLSKEYSDRQGKTPL
TLVDICFWSTVFFTASLFLHLVGIPTHRHIRGEACPLPHRLNSLGGCRCGKYPNLKKPTV
WRRGH
Gene Ontology
GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW
GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW
GO:0019031; C:viral envelope; IEA:UniProtKB-KW
GO:0075512; P:clathrin-mediated endocytosis of virus by host cell; IEA:UniProtKB-KW
GO:0039654; P:fusion of virus membrane with host endosome membrane; IEA:UniProtKB-KW
GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW
Interpro
InterPro; IPR001535; Arena_glycoprot
Pfam
Pfam; PF00798; Arena_glycoprot;
SMART
PROSITE
PRINTS