ID   GIMA4_HUMAN             Reviewed;         329 AA.
AC   Q9NUV9;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 155.
DE   RecName: Full=GTPase IMAP family member 4;
DE   AltName: Full=Immunity-associated nucleotide 1 protein;
DE            Short=IAN-1;
DE            Short=hIAN1;
DE   AltName: Full=Immunity-associated protein 4;
GN   Name=GIMAP4; Synonyms=IAN1, IMAP4; ORFNames=MSTP062;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC   TISSUE=T-cell lymphoma;
RX   PubMed=11964296; DOI=10.1182/blood.v99.9.3293;
RA   Cambot M., Aresta S., Kahn-Perles B., de Gunzburg J., Romeo P.-H.;
RT   "Human immune associated nucleotide 1: a member of a new guanosine
RT   triphosphatase family expressed in resting T and B cells.";
RL   Blood 99:3293-3301(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Heart;
RA   Liu Y.Q., Liu B., Zhao B., Wang X.Y., Song L., Ye J., Sheng H., Gao Y.,
RA   Zhang C.L., Zhang J., Wei Y.J., Sun Y.H., Jiang Y.X., Zhao X.W., Liu S.,
RA   Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Quiang B.Q., Yuan J.G., Liew C.C.,
RA   Zhao M.S., Hui R.T.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
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).
RN   [5]
RP   INTERACTION WITH BAX.
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   [6]
RP   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=23454188; DOI=10.1016/j.str.2013.01.014;
RA   Schwefel D., Arasu B.S., Marino S.F., Lamprecht B., Kochert K.,
RA   Rosenbaum E., Eichhorst J., Wiesner B., Behlke J., Rocks O., Mathas S.,
RA   Daumke O.;
RT   "Structural insights into the mechanism of GTPase activation in the GIMAP
RT   family.";
RL   Structure 21:550-559(2013).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 20-240 IN COMPLEX WITH MAGNESIUM
RP   AND GDP.
RG   Structural genomics consortium (SGC);
RT   "Crystal structure of human GTPase imap family member 4.";
RL   Submitted (MAR-2010) to the PDB data bank.
CC   -!- FUNCTION: During thymocyte development, may play a role in the
CC       regulation of apoptosis (By similarity). GTPase which exhibits a higher
CC       affinity for GDP than for GTP. {ECO:0000250,
CC       ECO:0000250|UniProtKB:Q99JY3}.
CC   -!- SUBUNIT: May interact (via IQ domain) with calmodulin/CALM1 only in the
CC       absence of Ca(2+) (By similarity). Interacts with BAX, but not with
CC       other Bcl-2 family members (By similarity).
CC       {ECO:0000250|UniProtKB:Q99JY3}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:23454188}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in spleen and peripheral blood
CC       leukocytes that contain mostly T- and B-lymphocytes. Expressed
CC       specifically in resting T- and B-lymphocytes and expression
CC       significantly decreases during B- or T-lymphocyte activation. Expressed
CC       at lower levels in thymus, ovary, colon and small intestine.
CC       {ECO:0000269|PubMed:23454188}.
CC   -!- PTM: Phosphorylated at very low levels in resting splenocytes. Rapidly
CC       and transiently phosphorylated in response to splenocyte activation.
CC       {ECO:0000250|UniProtKB:Q99JY3}.
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; AF117333; AAO15308.1; -; mRNA.
DR   EMBL; AK001972; BAA92010.1; -; mRNA.
DR   EMBL; BC020657; AAH20657.1; -; mRNA.
DR   CCDS; CCDS5904.1; -.
DR   RefSeq; NP_060796.1; NM_018326.2.
DR   PDB; 3LXX; X-ray; 2.15 A; A=20-240.
DR   PDBsum; 3LXX; -.
DR   AlphaFoldDB; Q9NUV9; -.
DR   SMR; Q9NUV9; -.
DR   BioGRID; 120589; 4.
DR   IntAct; Q9NUV9; 2.
DR   MINT; Q9NUV9; -.
DR   STRING; 9606.ENSP00000419545; -.
DR   iPTMnet; Q9NUV9; -.
DR   MetOSite; Q9NUV9; -.
DR   PhosphoSitePlus; Q9NUV9; -.
DR   BioMuta; GIMAP4; -.
DR   jPOST; Q9NUV9; -.
DR   MassIVE; Q9NUV9; -.
DR   MaxQB; Q9NUV9; -.
DR   PaxDb; 9606-ENSP00000255945; -.
DR   PeptideAtlas; Q9NUV9; -.
DR   ProteomicsDB; 82724; -.
DR   Antibodypedia; 18614; 327 antibodies from 28 providers.
DR   DNASU; 55303; -.
DR   Ensembl; ENST00000255945.4; ENSP00000255945.2; ENSG00000133574.10.
DR   GeneID; 55303; -.
DR   KEGG; hsa:55303; -.
DR   MANE-Select; ENST00000255945.4; ENSP00000255945.2; NM_018326.3; NP_060796.1.
DR   UCSC; uc003whl.4; human.
DR   AGR; HGNC:21872; -.
DR   CTD; 55303; -.
DR   DisGeNET; 55303; -.
DR   GeneCards; GIMAP4; -.
DR   HGNC; HGNC:21872; GIMAP4.
DR   HPA; ENSG00000133574; Tissue enhanced (lymphoid).
DR   MIM; 608087; gene.
DR   neXtProt; NX_Q9NUV9; -.
DR   OpenTargets; ENSG00000133574; -.
DR   PharmGKB; PA128394681; -.
DR   VEuPathDB; HostDB:ENSG00000133574; -.
DR   eggNOG; ENOG502R7PE; Eukaryota.
DR   GeneTree; ENSGT00940000159317; -.
DR   HOGENOM; CLU_010468_0_0_1; -.
DR   InParanoid; Q9NUV9; -.
DR   OMA; YLMEAPE; -.
DR   OrthoDB; 938643at2759; -.
DR   PhylomeDB; Q9NUV9; -.
DR   TreeFam; TF330845; -.
DR   PathwayCommons; Q9NUV9; -.
DR   SignaLink; Q9NUV9; -.
DR   BioGRID-ORCS; 55303; 12 hits in 1144 CRISPR screens.
DR   ChiTaRS; GIMAP4; human.
DR   EvolutionaryTrace; Q9NUV9; -.
DR   GeneWiki; GIMAP4; -.
DR   GenomeRNAi; 55303; -.
DR   Pharos; Q9NUV9; Tbio.
DR   PRO; PR:Q9NUV9; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q9NUV9; Protein.
DR   Bgee; ENSG00000133574; Expressed in monocyte and 175 other cell types or tissues.
DR   ExpressionAtlas; Q9NUV9; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; 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   Genevisible; Q9NUV9; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Cytoplasm; GTP-binding; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..329
FT                   /note="GTPase IMAP family member 4"
FT                   /id="PRO_0000190987"
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..26
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   COILED          188..300
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         37..45
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3LXX"
FT   BINDING         58
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3LXX"
FT   BINDING         155..157
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3LXX"
FT   BINDING         191
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000269|Ref.8, ECO:0007744|PDB:3LXX"
FT   VARIANT         128
FT                   /note="E -> D (in dbSNP:rs2293172)"
FT                   /id="VAR_017306"
FT   STRAND          30..36
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           43..51
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   STRAND          70..76
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   STRAND          79..85
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           97..109
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   TURN            110..112
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   STRAND          115..122
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           129..145
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   STRAND          149..154
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           156..158
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           173..182
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:3LXX"
FT   HELIX           195..215
FT                   /evidence="ECO:0007829|PDB:3LXX"
SQ   SEQUENCE   329 AA;  37534 MW;  9D64BA4FB1C5DF72 CRC64;
     MAAQYGSMSF NPSTPGASYG PGRQEPRNSQ LRIVLVGKTG AGKSATGNSI LGRKVFHSGT
     AAKSITKKCE KRSSSWKETE LVVVDTPGIF DTEVPNAETS KEIIRCILLT SPGPHALLLV
     VPLGRYTEEE HKATEKILKM FGERARSFMI LIFTRKDDLG DTNLHDYLRE APEDIQDLMD
     IFGDRYCALN NKATGAEQEA QRAQLLGLIQ RVVRENKEGC YTNRMYQRAE EEIQKQTQAM
     QELHRVELER EKARIREEYE EKIRKLEDKV EQEKRKKQME KKLAEQEAHY AVRQQRARTE
     VESKDGILEL IMTALQIASF ILLRLFAED
//