GIMA4_HUMAN
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 03-AUG-2022, entry version 146.
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; 3.
DR IntAct; Q9NUV9; 1.
DR STRING; 9606.ENSP00000255945; -.
DR iPTMnet; Q9NUV9; -.
DR MetOSite; Q9NUV9; -.
DR PhosphoSitePlus; Q9NUV9; -.
DR BioMuta; GIMAP4; -.
DR jPOST; Q9NUV9; -.
DR MassIVE; Q9NUV9; -.
DR MaxQB; Q9NUV9; -.
DR PaxDb; Q9NUV9; -.
DR PeptideAtlas; Q9NUV9; -.
DR PRIDE; Q9NUV9; -.
DR ProteomicsDB; 82724; -.
DR Antibodypedia; 18614; 302 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 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; CKEIARC; -.
DR PhylomeDB; Q9NUV9; -.
DR TreeFam; TF330845; -.
DR PathwayCommons; Q9NUV9; -.
DR SignaLink; Q9NUV9; -.
DR BioGRID-ORCS; 55303; 12 hits in 1066 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 173 other tissues.
DR ExpressionAtlas; Q9NUV9; baseline and differential.
DR Genevisible; Q9NUV9; HS.
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 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 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
