GIMA3_MOUSE
ID GIMA3_MOUSE Reviewed; 301 AA.
AC Q99MI6; Q4VBX0; Q549W4; Q8CF04;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2003, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=GTPase IMAP family member 3;
DE AltName: Full=Immunity-associated nucleotide 4 protein;
DE Short=IAN-4 {ECO:0000303|PubMed:11238997};
GN Name=Gimap3;
GN Synonyms=Ian4 {ECO:0000303|PubMed:11238997, ECO:0000303|PubMed:16509771};
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], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11238997; DOI=10.1093/nar/29.6.1308;
RA Daheron L., Zenz T., Siracusa L.D., Brenner C., Calabretta B.;
RT "Molecular cloning of Ian4: a BCR/ABL-induced gene that encodes an outer
RT membrane mitochondrial protein with GTP-binding activity.";
RL Nucleic Acids Res. 29:1308-1316(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH BAD; BAK1; BAX;
RP BCL2; BCL2L1 AND BCL2L11, DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 236-301.
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25808953; DOI=10.1534/genetics.115.175596;
RA Jokinen R., Lahtinen T., Marttinen P., Myoehaenen M., Ruotsalainen P.,
RA Yeung N., Shvetsova A., Kastaniotis A.J., Hiltunen J.K., Oehman T.,
RA Nyman T.A., Weiler H., Battersby B.J.;
RT "Quantitative changes in Gimap3 and Gimap5 expression modify mitochondrial
RT DNA segregation in mice.";
RL Genetics 200:221-235(2015).
CC -!- FUNCTION: During thymocyte development, may support the positive
CC selection of CD4 and CD8 T cells (PubMed:16509771). May play a role in
CC mitochondrial DNA segregation in hematopoietic tissues
CC (PubMed:25808953). Binds GTP (PubMed:11238997).
CC {ECO:0000269|PubMed:11238997, ECO:0000269|PubMed:16509771,
CC ECO:0000269|PubMed:25808953}.
CC -!- SUBUNIT: Interacts with BAD, BAK1, BAX, BCL2, BCL2L1/Bcl-xL and
CC BCL2L11/BimEL (PubMed:16509771). The interaction with BAX is increased,
CC when cells initiate apoptosis upon IL2 withdrawal (PubMed:16509771).
CC {ECO:0000269|PubMed:16509771}.
CC -!- INTERACTION:
CC Q99MI6; P10417: Bcl2; NbExp=4; IntAct=EBI-15572304, EBI-526314;
CC Q99MI6; Q07812: BAX; Xeno; NbExp=2; IntAct=EBI-15572304, EBI-516580;
CC Q99MI6; Q07817-1: BCL2L1; Xeno; NbExp=3; IntAct=EBI-15572304, EBI-287195;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:25808953}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:11238997}. Note=The mitochondrial localization
CC originally reported was observed with C-terminally tagged protein and
CC was not confirmed in later publications. {ECO:0000305|PubMed:11238997,
CC ECO:0000305|PubMed:25808953}.
CC -!- TISSUE SPECIFICITY: Expressed in thymus (in thymocytes), spleen (in
CC splenocytes), lymph node and, at lower levels, in lung
CC (PubMed:16509771, PubMed:25808953). Highly expressed in T lymphocytes
CC (PubMed:16509771). {ECO:0000269|PubMed:16509771,
CC ECO:0000269|PubMed:25808953}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated upon the maturation of CD4/CD8
CC double-positive to CD4 single-positive thymocytes.
CC {ECO:0000269|PubMed:16509771}.
CC -!- INDUCTION: By BCR-ABL oncogene.
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=AAK31138.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF337052; AAK31138.1; ALT_FRAME; mRNA.
DR EMBL; AB164418; BAD14959.1; -; mRNA.
DR EMBL; BC094914; AAH94914.1; -; mRNA.
DR EMBL; AK008376; BAC25217.1; -; mRNA.
DR CCDS; CCDS20115.1; -.
DR RefSeq; NP_112537.2; NM_031247.3.
DR AlphaFoldDB; Q99MI6; -.
DR SMR; Q99MI6; -.
DR BioGRID; 219916; 3.
DR DIP; DIP-29182N; -.
DR IntAct; Q99MI6; 6.
DR STRING; 10090.ENSMUSP00000047435; -.
DR EPD; Q99MI6; -.
DR MaxQB; Q99MI6; -.
DR PaxDb; Q99MI6; -.
DR PRIDE; Q99MI6; -.
DR ProteomicsDB; 267794; -.
DR DNASU; 83408; -.
DR Ensembl; ENSMUST00000038811; ENSMUSP00000047435; ENSMUSG00000039264.
DR Ensembl; ENSMUST00000204036; ENSMUSP00000145211; ENSMUSG00000039264.
DR GeneID; 83408; -.
DR KEGG; mmu:83408; -.
DR UCSC; uc009bvt.1; mouse.
DR CTD; 83408; -.
DR MGI; MGI:1932723; Gimap3.
DR VEuPathDB; HostDB:ENSMUSG00000039264; -.
DR eggNOG; ENOG502RB0C; Eukaryota.
DR GeneTree; ENSGT00940000154844; -.
DR HOGENOM; CLU_010468_1_1_1; -.
DR InParanoid; Q99MI6; -.
DR OMA; LHKEICA; -.
DR OrthoDB; 1092873at2759; -.
DR PhylomeDB; Q99MI6; -.
DR TreeFam; TF330845; -.
DR BioGRID-ORCS; 83408; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Gimap3; mouse.
DR PRO; PR:Q99MI6; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q99MI6; protein.
DR Bgee; ENSMUSG00000039264; Expressed in lymph node and 42 other tissues.
DR Genevisible; Q99MI6; MM.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0005525; F:GTP binding; IDA:MGI.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IMP:MGI.
DR GO; GO:0043011; P:myeloid dendritic cell differentiation; ISO:MGI.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; ISO:MGI.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; ISO:MGI.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; ISO:MGI.
DR GO; GO:0050868; P:negative regulation of T cell activation; ISO:MGI.
DR GO; GO:0010524; P:positive regulation of calcium ion transport into cytosol; ISO:MGI.
DR GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0045588; P:positive regulation of gamma-delta T cell differentiation; ISO:MGI.
DR GO; GO:0002925; P:positive regulation of humoral immune response mediated by circulating immunoglobulin; ISO:MGI.
DR GO; GO:0045838; P:positive regulation of membrane potential; ISO:MGI.
DR GO; GO:0002729; P:positive regulation of natural killer cell cytokine production; ISO:MGI.
DR GO; GO:0045954; P:positive regulation of natural killer cell mediated cytotoxicity; ISO:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI.
DR GO; GO:0043029; P:T cell homeostasis; ISO:MGI.
DR GO; GO:0001659; P:temperature homeostasis; ISO: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; GTP-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..301
FT /note="GTPase IMAP family member 3"
FT /id="PRO_0000190994"
FT TOPO_DOM 1..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..300
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 301
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT DOMAIN 20..223
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 263..301
FT /note="Required for targeting to the endoplasmic reticulum"
FT /evidence="ECO:0000269|PubMed:25808953"
FT BINDING 29..37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 50
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT BINDING 147..149
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 184
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT CONFLICT 99
FT /note="Y -> C (in Ref. 3; AAH94914)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="C -> R (in Ref. 3; AAH94914)"
FT /evidence="ECO:0000305"
FT CONFLICT 257
FT /note="E -> G (in Ref. 4; BAC25217)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34179 MW; 4169A8D897727357 CRC64;
METLQNVVTG GKKGGCTSGS RPLRILLVGK SGCGKSATGN SLLRRPAFES RLRGQSVTRT
SQAETGTWEG RSILVVDTPP IFESKAQNQD MDKDIGDCYL LCAPGPHVLL LVTQLGRFTA
EDVMAVRMVK EVFGVGVMRH MIVLFTRKED LAEKSLEEFV THTDNRSLRS LVQECGRRYC
AFNNRASGEE QQGQLAELMA LVRRLEQECE GSFHSNDLFL HAETLLREGY SVHQEAYRCY
LAKVRQEVEK QRWELEEQEG SWVLKVLPIG KKLEVLHSDF CWYLVLAILI FFVFFFLLFY
V
