GIMA1_MOUSE
ID GIMA1_MOUSE Reviewed; 277 AA.
AC P70224;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 3.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=GTPase IMAP family member 1;
DE AltName: Full=Immune-associated protein 38;
DE Short=IAP38;
DE AltName: Full=Immunity-associated protein 1;
GN Name=Gimap1; Synonyms=Ian2 {ECO:0000303|PubMed:16509771}, Imap1, Imap38;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/10; TISSUE=Spleen;
RX PubMed=9020038; DOI=10.1006/bbrc.1996.5876;
RA Kruecken J., Schmitt-Wrede H.-P., Markmann-Mulisch U., Wunderlich F.;
RT "Novel gene expressed in spleen cells mediating acquired testosterone-
RT resistant immunity to Plasmodium chabaudi malaria.";
RL Biochem. Biophys. Res. Commun. 230:167-170(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC STRAIN=129/Ola, and C57BL/10; TISSUE=Spleen;
RX PubMed=10446218; DOI=10.1074/jbc.274.34.24383;
RA Kruecken J., Stamm O., Schmitt-Wrede H.-P., Mincheva A., Lichter P.,
RA Wunderlich F.;
RT "Spleen-specific expression of the malaria-inducible intronless mouse gene
RT imap38.";
RL J. Biol. Chem. 274:24383-24391(1999).
RN [3]
RP IDENTIFICATION, SUBCELLULAR LOCATION, AND GTP-BINDING.
RC TISSUE=Spleen;
RX PubMed=11814688; DOI=10.1016/s0378-1119(01)00837-x;
RA Stamm O., Kruecken J., Schmitt-Wrede H.-P., Benten W.P.M., Wunderlich F.;
RT "Human ortholog to mouse gene imap38 encoding an ER-localizable G-protein
RT belongs to a gene family clustered on chromosome 7q32-36.";
RL Gene 282:159-167(2002).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103;
RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T.,
RA Kanno M., Takahama Y.;
RT "IAN family critically regulates survival and development of T
RT lymphocytes.";
RL PLoS Biol. 4:593-605(2006).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=20194894; DOI=10.1182/blood-2009-08-237586;
RA Saunders A., Webb L.M., Janas M.L., Hutchings A., Pascall J., Carter C.,
RA Pugh N., Morgan G., Turner M., Butcher G.W.;
RT "Putative GTPase GIMAP1 is critical for the development of mature B and T
RT lymphocytes.";
RL Blood 115:3249-3257(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=21487483; DOI=10.4161/self.1.3.12819;
RA Wong V.W., Saunders A.E., Hutchings A., Pascall J.C., Carter C.,
RA Bright N.A., Walker S.A., Ktistakis N.T., Butcher G.W.;
RT "The autoimmunity-related GIMAP5 GTPase is a lysosome-associated protein.";
RL Self/Nonself 1:259-268(2010).
CC -!- FUNCTION: May regulate lymphocyte survival. Required for normal levels
CC of mature T-lymphocytes and mature B-cells.
CC {ECO:0000269|PubMed:20194894}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:11814688, ECO:0000269|PubMed:21487483}; Single-pass
CC type IV membrane protein {ECO:0000305}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:21487483}; Single-pass type IV membrane protein
CC {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in thymus, spleen (in splenocytes), lymph
CC node and lung (PubMed:16509771, PubMed:20194894). Detected in mature B-
CC cells and thymocytes (at protein level) (PubMed:20194894).
CC {ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:20194894}.
CC -!- DISRUPTION PHENOTYPE: Severe lymphophenia, leading to death soon after
CC birth. {ECO:0000269|PubMed:20194894}.
CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC IAN subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA69283.2; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
CC Sequence=CAB53101.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; Y08026; CAA69283.2; ALT_SEQ; mRNA.
DR EMBL; AJ133125; CAB53101.1; ALT_SEQ; Genomic_DNA.
DR PIR; A58583; A58583.
DR RefSeq; XP_006505683.1; XM_006505620.1.
DR AlphaFoldDB; P70224; -.
DR SMR; P70224; -.
DR BioGRID; 200651; 1.
DR STRING; 10090.ENSMUSP00000062108; -.
DR iPTMnet; P70224; -.
DR PhosphoSitePlus; P70224; -.
DR EPD; P70224; -.
DR MaxQB; P70224; -.
DR PaxDb; P70224; -.
DR PeptideAtlas; P70224; -.
DR PRIDE; P70224; -.
DR ProteomicsDB; 268879; -.
DR MGI; MGI:109368; Gimap1.
DR eggNOG; ENOG502SN36; Eukaryota.
DR InParanoid; P70224; -.
DR BioGRID-ORCS; 16205; 0 hits in 72 CRISPR screens.
DR PRO; PR:P70224; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P70224; protein.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0030183; P:B cell differentiation; IMP:MGI.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR006703; G_AIG1.
DR InterPro; IPR045058; GIMA/IAN/Toc.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR10903; PTHR10903; 1.
DR Pfam; PF04548; AIG1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51720; G_AIG1; 1.
PE 1: Evidence at protein level;
KW Endoplasmic reticulum; Golgi apparatus; GTP-binding; Membrane;
KW Nucleotide-binding; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..277
FT /note="GTPase IMAP family member 1"
FT /id="PRO_0000190985"
FT TOPO_DOM 1..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..266
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..277
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 1..205
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 10..17
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 37..41
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 58..61
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 128..131
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 165..167
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT BINDING 10..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT BINDING 129..131
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 166
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
SQ SEQUENCE 277 AA; 30829 MW; F192E438A7579C5C CRC64;
MPQLRLILVG RTGTGKSATG NSILGQKCFL SRLGAVPVTR SCTLASRMWA GWQVEVVDTP
DIFSSEIPRT DPGCVETARC FVLSAPGPHA LLLVTQLGRF TMQDSQALAA VKRLFGKQVM
ARTVVVFTRQ EDLAGDSLQD YVHCTDNRAL RDLVAECGGR VCALNNRATG SEREAQAEQL
LGMVACLVRE HGGAHYSNEV YELVQDTRCA DPQDQVAKVA EIVAERMQRR TRLLAGLWGW
RKFYWKGWRR GFSVFLGVAI LIYLLFYRKG FGDQNNR
