ID   GIMA4_MOUSE             Reviewed;         328 AA.
AC   Q99JY3; D3YTN4;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   08-MAY-2019, sequence version 2.
DT   27-MAR-2024, entry version 139.
DE   RecName: Full=GTPase IMAP family member 4;
DE   AltName: Full=Immunity-associated nucleotide 1 protein {ECO:0000303|PubMed:16569770};
DE            Short=IAN-1 {ECO:0000303|PubMed:16569770};
DE   AltName: Full=Immunity-associated protein 4;
GN   Name=Gimap4; Synonyms=Ian1 {ECO:0000303|PubMed:16509771}, Imap4;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Mammary tumor;
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   [3]
RP   FUNCTION, INTERACTION WITH CALM1, SUBCELLULAR LOCATION, DISRUPTION
RP   PHENOTYPE, TISSUE SPECIFICITY, PHOSPHORYLATION, DEVELOPMENTAL STAGE, AND
RP   MUTAGENESIS OF 239-ARG--ARG-250.
RX   PubMed=16569770; DOI=10.1182/blood-2005-11-4616;
RA   Schnell S., Demolliere C., van den Berk P., Jacobs H.;
RT   "Gimap4 accelerates T-cell death.";
RL   Blood 108:591-599(2006).
RN   [4]
RP   FUNCTION, INTERACTION WITH BAX, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE,
RP   AND 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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
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).
CC   -!- FUNCTION: During thymocyte development, may play a role in the
CC       regulation of apoptosis. {ECO:0000269|PubMed:16509771,
CC       ECO:0000269|PubMed:16569770}.
CC   -!- SUBUNIT: Interacts (via IQ domain) with calmodulin/CALM1 only in the
CC       absence of Ca(2+) (PubMed:16569770). Interacts with BAX, but not with
CC       other Bcl-2 family members, including BAD, BAK1, BCL2, BCL2L1/Bcl-xL
CC       and BCL2L11/BimEL (PubMed:16509771). {ECO:0000269|PubMed:16509771,
CC       ECO:0000269|PubMed:16569770}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:16509771,
CC       ECO:0000269|PubMed:16569770}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q99JY3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q99JY3-2; Sequence=VSP_060167, VSP_060168;
CC   -!- TISSUE SPECIFICITY: Expressed in thymus (in thymocytes), spleen (in
CC       splenocytes), lymph node and lung (PubMed:16509771). Expressed in B-
CC       cells and T-cells (at protein level) (PubMed:16569770,
CC       PubMed:16509771). {ECO:0000269|PubMed:16509771,
CC       ECO:0000269|PubMed:16569770}.
CC   -!- DEVELOPMENTAL STAGE: Up-regulated during T cell development, including
CC       upon the maturation of CD4/CD8 double-positive to CD4 single-positive
CC       thymocytes. {ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:16569770}.
CC   -!- PTM: Phosphorylated at very low levels in resting splenocytes. Rapidly
CC       and transiently phosphorylated in response to splenocyte activation.
CC       Phosphorylation is increased in cells undergoing apoptosis.
CC       {ECO:0000269|PubMed:16569770}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. T-cell development,
CC       selection and activation in vivo appear to occur normally in knockout
CC       mice. {ECO:0000269|PubMed:16569770}.
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}.
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DR   EMBL; AC153894; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC005577; AAH05577.1; -; mRNA.
DR   CCDS; CCDS20110.1; -. [Q99JY3-1]
DR   CCDS; CCDS57423.1; -. [Q99JY3-2]
DR   RefSeq; NP_001230128.1; NM_001243199.1. [Q99JY3-2]
DR   RefSeq; NP_778155.2; NM_174990.4. [Q99JY3-1]
DR   AlphaFoldDB; Q99JY3; -.
DR   SMR; Q99JY3; -.
DR   IntAct; Q99JY3; 1.
DR   STRING; 10090.ENSMUSP00000087524; -.
DR   iPTMnet; Q99JY3; -.
DR   PhosphoSitePlus; Q99JY3; -.
DR   EPD; Q99JY3; -.
DR   jPOST; Q99JY3; -.
DR   MaxQB; Q99JY3; -.
DR   PaxDb; 10090-ENSMUSP00000087524; -.
DR   PeptideAtlas; Q99JY3; -.
DR   ProteomicsDB; 271222; -. [Q99JY3-1]
DR   ProteomicsDB; 357534; -.
DR   Antibodypedia; 18614; 327 antibodies from 28 providers.
DR   DNASU; 107526; -.
DR   Ensembl; ENSMUST00000067506.14; ENSMUSP00000068398.8; ENSMUSG00000054435.17. [Q99JY3-2]
DR   Ensembl; ENSMUST00000090070.6; ENSMUSP00000087524.5; ENSMUSG00000054435.17. [Q99JY3-1]
DR   GeneID; 107526; -.
DR   KEGG; mmu:107526; -.
DR   UCSC; uc009bvi.2; mouse. [Q99JY3-1]
DR   AGR; MGI:1349656; -.
DR   CTD; 55303; -.
DR   MGI; MGI:1349656; Gimap4.
DR   VEuPathDB; HostDB:ENSMUSG00000054435; -.
DR   eggNOG; ENOG502R7PE; Eukaryota.
DR   GeneTree; ENSGT00940000159317; -.
DR   HOGENOM; CLU_010468_3_3_1; -.
DR   InParanoid; Q99JY3; -.
DR   OMA; YLMEAPE; -.
DR   OrthoDB; 938643at2759; -.
DR   TreeFam; TF330845; -.
DR   BioGRID-ORCS; 107526; 1 hit in 76 CRISPR screens.
DR   ChiTaRS; Gimap4; mouse.
DR   PRO; PR:Q99JY3; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q99JY3; Protein.
DR   Bgee; ENSMUSG00000054435; Expressed in peripheral lymph node and 188 other cell types or tissues.
DR   ExpressionAtlas; Q99JY3; baseline and differential.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   CDD; cd01852; AIG1; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR006703; G_AIG1.
DR   InterPro; IPR045058; GIMA/IAN/Toc.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10903:SF170; GTPASE IMAP FAMILY MEMBER 4; 1.
DR   PANTHER; PTHR10903; GTPASE, IMAP FAMILY MEMBER-RELATED; 1.
DR   Pfam; PF04548; AIG1; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51720; G_AIG1; 1.
DR   PROSITE; PS50096; IQ; 1.
DR   Genevisible; Q99JY3; MM.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..328
FT                   /note="GTPase IMAP family member 4"
FT                   /id="PRO_0000190988"
FT   DOMAIN          28..230
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   DOMAIN          233..262
FT                   /note="IQ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          37..44
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          64..68
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          85..88
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          154..157
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          190..192
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   BINDING         37..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT   BINDING         58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT   BINDING         155..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT   BINDING         191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NUV9"
FT   VAR_SEQ         213..219
FT                   /note="VRENGGR -> FLSSRMK (in isoform 2)"
FT                   /id="VSP_060167"
FT   VAR_SEQ         220..328
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060168"
FT   MUTAGEN         239..250
FT                   /note="RMQELYREELER->QMQELYQEELEQ: Loss of interaction with
FT                   CALM1."
FT                   /evidence="ECO:0000269|PubMed:16569770"
SQ   SEQUENCE   328 AA;  38044 MW;  10C2446CD3A2D7A7 CRC64;
     MEVQCGGAGF IPESSRSSHE LGNQDQGIPQ LRIVLLGKTG AGKSSTGNSI LGEKVFNSGI
     CAKSITKVCE KRVSTWDGKE LVVVDTPGIF DTEVPDADTQ REITRYVALT SPGPHALLLV
     VPLGRYTVEE HKATQKILDM FGKQARRFMI LLLTRKDDLE DTDIHEYLEK APKFFQEVMH
     EFQNRYCLFN NRASGAEKEE QKMQLLTLVQ SMVRENGGRC FTNKMYESAE CVIQKETLRM
     QELYREELER EKARIRREYE EQIKDLRDEL EREIRRARME REFKEREAIF TKNQQNARKE
     VENTSMILEL IIKAWEIASF IFNQFMKD
//