IRGM_RAT
ID IRGM_RAT Reviewed; 411 AA.
AC Q6AYC2;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Immunity-related GTPase family M protein;
DE EC=3.6.5.-;
GN Name=Irgm;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Putative GTPase which is required for IFNG-mediated clearance
CC of acute protozoan and bacterial infections. Functions in innate immune
CC response probably through regulation of autophagy. May regulate pro-
CC inflammatory cytokine production and prevent endotoxemia upon
CC infection. May also play a role in macrophages adhesion and motility
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}. Cell
CC membrane {ECO:0000250}. Cytoplasmic vesicle, phagosome membrane
CC {ECO:0000250}. Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250}. Cell projection, phagocytic cup {ECO:0000250}.
CC Note=Behaves like an integral membrane protein. Recruited to the plasma
CC membrane around forming phagocytic cups, it remains associated with
CC maturing autophagosomes. Preferentially associated with cis- and
CC medial-Golgi. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
CC superfamily. IRG family. {ECO:0000255|PROSITE-ProRule:PRU01053,
CC ECO:0000305}.
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DR EMBL; BC079106; AAH79106.1; -; mRNA.
DR RefSeq; NP_001012007.1; NM_001012007.1.
DR RefSeq; XP_006246240.1; XM_006246178.2.
DR AlphaFoldDB; Q6AYC2; -.
DR SMR; Q6AYC2; -.
DR IntAct; Q6AYC2; 1.
DR STRING; 10116.ENSRNOP00000047579; -.
DR PhosphoSitePlus; Q6AYC2; -.
DR PaxDb; Q6AYC2; -.
DR PRIDE; Q6AYC2; -.
DR Ensembl; ENSRNOT00000045545; ENSRNOP00000047579; ENSRNOG00000031138.
DR GeneID; 303090; -.
DR KEGG; rno:303090; -.
DR UCSC; RGD:1305163; rat.
DR CTD; 345611; -.
DR RGD; 1305163; Irgm.
DR eggNOG; ENOG502QS9R; Eukaryota.
DR GeneTree; ENSGT00950000183007; -.
DR HOGENOM; CLU_015342_3_0_1; -.
DR InParanoid; Q6AYC2; -.
DR OMA; SCMNCNT; -.
DR OrthoDB; 688334at2759; -.
DR PhylomeDB; Q6AYC2; -.
DR TreeFam; TF331897; -.
DR PRO; PR:Q6AYC2; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000031138; Expressed in skeletal muscle tissue and 18 other tissues.
DR Genevisible; Q6AYC2; RN.
DR GO; GO:0044754; C:autolysosome; ISO:RGD.
DR GO; GO:0005776; C:autophagosome; ISO:RGD.
DR GO; GO:0000421; C:autophagosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0005770; C:late endosome; ISO:RGD.
DR GO; GO:0005764; C:lysosome; ISO:RGD.
DR GO; GO:0005739; C:mitochondrion; ISO:RGD.
DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell.
DR GO; GO:0045335; C:phagocytic vesicle; ISO:RGD.
DR GO; GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051434; F:BH3 domain binding; ISO:RGD.
DR GO; GO:0050700; F:CARD domain binding; ISO:RGD.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; ISO:RGD.
DR GO; GO:0000045; P:autophagosome assembly; ISO:RGD.
DR GO; GO:0061762; P:CAMKK-AMPK signaling cascade; ISO:RGD.
DR GO; GO:0035458; P:cellular response to interferon-beta; IBA:GO_Central.
DR GO; GO:0071346; P:cellular response to interferon-gamma; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0098586; P:cellular response to virus; ISO:RGD.
DR GO; GO:0006952; P:defense response; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; ISO:RGD.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISO:RGD.
DR GO; GO:0070431; P:nucleotide-binding oligomerization domain containing 2 signaling pathway; ISO:RGD.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; ISO:RGD.
DR GO; GO:0010508; P:positive regulation of autophagy; ISO:RGD.
DR GO; GO:0060335; P:positive regulation of interferon-gamma-mediated signaling pathway; ISO:RGD.
DR GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:RGD.
DR GO; GO:0010800; P:positive regulation of peptidyl-threonine phosphorylation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0031648; P:protein destabilization; ISO:RGD.
DR GO; GO:0061739; P:protein lipidation involved in autophagosome assembly; ISO:RGD.
DR GO; GO:0050821; P:protein stabilization; ISO:RGD.
DR GO; GO:0061635; P:regulation of protein complex stability; ISO:RGD.
DR GO; GO:0043254; P:regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:0009617; P:response to bacterium; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR030385; G_IRG_dom.
DR InterPro; IPR007743; Immunity-related_GTPase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF05049; IIGP; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51716; G_IRG; 1.
PE 2: Evidence at transcript level;
KW Autophagy; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Golgi apparatus; GTP-binding; Hydrolase; Immunity; Innate immunity;
KW Membrane; Nucleotide-binding; Reference proteome.
FT CHAIN 1..411
FT /note="Immunity-related GTPase family M protein"
FT /id="PRO_0000325751"
FT DOMAIN 77..253
FT /note="IRG-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01053"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 77..291
FT /note="Mediates targeting to cell membrane and phagosomes"
FT /evidence="ECO:0000250"
FT REGION 352..376
FT /note="Mediates targeting to the Golgi"
FT /evidence="ECO:0000250"
FT BINDING 86..93
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 111..115
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 193..195
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 234..236
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 411 AA; 46338 MW; 5FB033A84818665C CRC64;
MKPSHKSCEA APLLPKMPET STHNAPLNLS FPSVPSYQIG CSSLPEISRS TERALKEGKL
PELVYGVKET VATLSQIPVS IFVTGDSGNG MSSFINALRI IGHEEDASAP TGVVRTTQTR
AEYSSSHFPN VVLWDLPGLG ATAQTVENYI EEMKFSTCDL FIIVASEQFS SNHVKLAKII
QSMGKRFYVI WTKLDRDLST SVLSEVRLIQ NIQENIRENL QKEGVKEVPI FLVSNLDPLL
HDFPELRNTL QTDLSNIRCC EPLKTLYVIY EKIIGDKVAN WNQIIANGRL KSSLGVRDDD
DMGECLKRYR LIFGIDDESL QQIAHGMGTV VMEYKANIKS QDFHTLRRAD WKLRLMTCTT
VNALFCLFKF LPCLCHCFKR MRHKRMLLLV AKDTKNILKK ILMDAVSPPQ I
