Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00214
Entry Name
UniProt Accession
Theoretical PI
5.41
Molecular Weight
67711.66
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Interferon-induced guanylate-binding protein 1
Protein Synonyms/Alias
GTP-binding protein 1; GBP-1; mGBP-1; mGBP1; Guanine nucleotide-binding protein 1; Interferon-gamma-inducible protein MAG-1;
Gene Name
Gbp1
Gene Synonyms/Alias
Gbp-1; Mag-1; Mpa1;
Created Date
01-JUL-1993
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
586
Canonical
NMPPPRSCTIL****
[1]
S-Geranylgeranylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Stickney JT, Buss JE. Murine guanylate-binding protein: incompletegeranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosinetriphosphate-binding protein. Mol Biol Cell. 2000 Jul;11(7):2191-200. PubMedPMID: 10888661; PubMed Central PMCID: PMC14912.[PMID:10888661]
Functional Description
Hydrolyzes GTP to GMP in two consecutive cleavage reactions. Exhibits antiviral activity against influenza virus (By similarity). Promote oxidative killing and deliver antimicrobial peptides to autophagolysosomes, providing broad host protection against different pathogen classes.
Sequence Annotation
Domain: 35 276 GB1/RHD3-type G.
Nucleotide-binding: 47 53 GTP.
Nucleotide-binding: 67 69 GTP.
Nucleotide-binding: 97 101 GTP.
Region: 1 309 GTPase domain (Globular).
Protein Length
589 AA.
Protein Sequence
(Canonical)
MASEIHMSEP MCLIENTEAQ LVINQEALRI LSAITQPVVV VAIVGLYRTG KSYLMNKLAG  60
KRTGFSLGST VQSHTKGIWM WCVPHPKKAG QTLVLLDTEG LEDVEKGDNQ NDCWIFALAV  120
LLSSTFIYNS IGTINQQAMD QLHYVTELTD LIKSKSSPDQ SDVDNSANFV GFFPIFVWTL  180
RDFSLDLEFD GESITPDEYL ETSLALRKGT DENTKKFNMP RLCIRKFFPK RKCFIFDRPG  240
DRKQLSKLEW IQEDQLNKEF VEQVAEFTSY IFSYSGVKTL SGGITVNGPR LKSLVQTYVS  300
AICSGELPCM ENAVLTLAQI ENSAAVQKAI TYYEEQMNQK IHMPTETLQE LLDLHRTCER  360
EAIEVFMKNS FKDVDQKFQE ELGAQLEAKR DAFVKKNMDM SSAHCSDLLE GLFAHLEEEV  420
KQGTFYKPGG YYLFLQRKQE LEKKYIQTPG KGLQAEVMLR KYFESKEDLA DTLLKMDQSL  480
TEKEKQIEME RIKAEAAEAA NRALAEMQKK HEMLMEQKEQ SYQEHMKQLT EKMEQERKEL  540
MAEQQRIISL KLQEQERLLK QGFQNESLQL RQEIEKIKNM PPPRSCTIL              589
FASTA
(Canonical)
>LipidDB-10090-00214|Q01514
MASEIHMSEPMCLIENTEAQLVINQEALRILSAITQPVVVVAIVGLYRTGKSYLMNKLAG
KRTGFSLGSTVQSHTKGIWMWCVPHPKKAGQTLVLLDTEGLEDVEKGDNQNDCWIFALAV
LLSSTFIYNSIGTINQQAMDQLHYVTELTDLIKSKSSPDQSDVDNSANFVGFFPIFVWTL
RDFSLDLEFDGESITPDEYLETSLALRKGTDENTKKFNMPRLCIRKFFPKRKCFIFDRPG
DRKQLSKLEWIQEDQLNKEFVEQVAEFTSYIFSYSGVKTLSGGITVNGPRLKSLVQTYVS
AICSGELPCMENAVLTLAQIENSAAVQKAITYYEEQMNQKIHMPTETLQELLDLHRTCER
EAIEVFMKNSFKDVDQKFQEELGAQLEAKRDAFVKKNMDMSSAHCSDLLEGLFAHLEEEV
KQGTFYKPGGYYLFLQRKQELEKKYIQTPGKGLQAEVMLRKYFESKEDLADTLLKMDQSL
TEKEKQIEMERIKAEAAEAANRALAEMQKKHEMLMEQKEQSYQEHMKQLTEKMEQERKEL
MAEQQRIISLKLQEQERLLKQGFQNESLQLRQEIEKIKNMPPPRSCTIL
Gene Ontology
GO:0031410; C:cytoplasmic vesicle; IDA:MGI
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0016020; C:membrane; IEA:UniProtKB-KW
GO:0020005; C:symbiont-containing vacuole membrane; IDA:MGI
GO:0019002; F:GMP binding; IDA:MGI
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0003924; F:GTPase activity; IEA:InterPro
GO:0044406; P:adhesion of symbiont to host; IDA:MGI
GO:0035458; P:cellular response to interferon-beta; IDA:MGI
GO:0071346; P:cellular response to interferon-gamma; IDA:MGI
GO:0050830; P:defense response to Gram-positive bacterium; IDA:MGI
GO:0042832; P:defense response to protozoan; IDA:MGI
GO:0051607; P:defense response to virus; IEA:UniProtKB-KW
Interpro
InterPro; IPR003191; Guanylate-bd_C
InterPro; IPR015894; Guanylate-bd_N
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF02263; GBP;
Pfam; PF02841; GBP_C;
SMART
PROSITE
PROSITE; PS51715; G_GB1_RHD3;
PRINTS