Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-00662
Entry Name
UniProt Accession
Theoretical PI
8.56
Molecular Weight
46551.8
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Immunity-related GTPase family M protein 1
Protein Synonyms/Alias
3.6.5.-; Interferon-inducible GTPase 3; Interferon-inducible protein 1; LPS-stimulated RAW 264.7 macrophage protein 47; LRG-47;
Gene Name
Irgm1
Gene Synonyms/Alias
Ifi1; Iigp3; Irgm;
Created Date
18-MAR-2008
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
258
Canonical
DLSNIRCCEPLKTLY
[2]
S-Palmitoylation
371
Canonical
RLLRFLPCVCCCLRR
[1]
S-Palmitoylation
373
Canonical
LRFLPCVCCCLRRLR
[1]
S-Palmitoylation
374
Canonical
RFLPCVCCCLRRLRH
[1]
S-Palmitoylation
375
Canonical
FLPCVCCCLRRLRHK
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Henry SC, Schmidt EA, Fessler MB, Taylor GA. Palmitoylation of the immunityrelated GTPase, Irgm1: impact on membrane localization and ability to promotemitochondrial fission. PLoS One. 2014 Apr 21;9(4):e95021. doi:10.1371/journal.pone.0095021. eCollection 2014.[PMID:24751652]
[2] Predicted from GPS-Lipid
Functional Description
Putative GTPase which is required for IFNG-mediated clearance of acute protozoan and bacterial infections. Functions in innate immune response probably through regulation of autophagy. May regulate proinflammatory cytokine production and prevent endotoxemia upon infection. Required for macrophage motility and possibly also for adhesion.
Sequence Annotation
Domain: 75 251 IRG-type G.
Nucleotide-binding: 84 91 GTP.
Nucleotide-binding: 109 113 GTP.
Nucleotide-binding: 191 193 GTP.
Nucleotide-binding: 232 234 GTP.
Region: 75 289 Mediates targeting to cell membrane andphagosomes.
Region: 350 374 Mediates targeting to the Golgi.
Modified residue: 202 202 Phosphoserine.
Protein Length
409 AA.
Protein Sequence
(Canonical)
MKPSHSSCEA APLLPNMAET HYAPLSSAFP FVTSYQTGSS RLPEVSRSTE RALREGKLLE  60
LVYGIKETVA TLSQIPVSIF VTGDSGNGMS SFINALRVIG HDEDASAPTG VVRTTKTRTE  120
YSSSHFPNVV LWDLPGLGAT AQTVEDYVEE MKFSTCDLFI IIASEQFSSN HVKLSKIIQS  180
MGKRFYIVWT KLDRDLSTSV LSEVRLLQNI QENIRENLQK EKVKYPPVFL VSSLDPLLYD  240
FPKLRDTLHK DLSNIRCCEP LKTLYGTYEK IVGDKVAVWK QRIANESLKN SLGVRDDDNM  300
GECLKVYRLI FGVDDESVQQ VAQSMGTVVM EYKDNMKSQN FYTLRREDWK LRLMTCAIVN  360
AFFRLLRFLP CVCCCLRRLR HKRMLFLVAQ DTKNILEKIL RDSIFPPQI              409
FASTA
(Canonical)
>LipidDB-10090-00662|Q60766
MKPSHSSCEAAPLLPNMAETHYAPLSSAFPFVTSYQTGSSRLPEVSRSTERALREGKLLE
LVYGIKETVATLSQIPVSIFVTGDSGNGMSSFINALRVIGHDEDASAPTGVVRTTKTRTE
YSSSHFPNVVLWDLPGLGATAQTVEDYVEEMKFSTCDLFIIIASEQFSSNHVKLSKIIQS
MGKRFYIVWTKLDRDLSTSVLSEVRLLQNIQENIRENLQKEKVKYPPVFLVSSLDPLLYD
FPKLRDTLHKDLSNIRCCEPLKTLYGTYEKIVGDKVAVWKQRIANESLKNSLGVRDDDNM
GECLKVYRLIFGVDDESVQQVAQSMGTVVMEYKDNMKSQNFYTLRREDWKLRLMTCAIVN
AFFRLLRFLPCVCCCLRRLRHKRMLFLVAQDTKNILEKILRDSIFPPQI
Gene Ontology
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW
GO:0005783; C:endoplasmic reticulum; TAS:MGI
GO:0005794; C:Golgi apparatus; IEA:UniProtKB-KW
GO:0005770; C:late endosome; IDA:UniProtKB
GO:0005764; C:lysosome; IDA:UniProtKB
GO:0005886; C:plasma membrane; IEA:UniProtKB-KW
GO:0005525; F:GTP binding; IEA:UniProtKB-KW
GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro
GO:0006914; P:autophagy; IEA:UniProtKB-KW
GO:0006952; P:defense response; IMP:MGI
GO:0045087; P:innate immune response; IEA:UniProtKB-KW
Interpro
InterPro; IPR007743; Interferon-induced_GTPase
InterPro; IPR027417; P-loop_NTPase
Pfam
Pfam; PF05049; IIGP;
SMART
PROSITE
PROSITE; PS51716; G_IRG;
PRINTS