GIMA7_HUMAN
ID GIMA7_HUMAN Reviewed; 300 AA.
AC Q8NHV1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=GTPase IMAP family member 7;
DE AltName: Full=Immunity-associated nucleotide 7 protein;
DE Short=IAN-7;
GN Name=GIMAP7; Synonyms=IAN7;
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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15474311; DOI=10.1016/j.gene.2004.07.005;
RA Kruecken J., Schroetel R.M.U., Mueller I.U., Saiedani N., Marinovski P.,
RA Benten W.P.M., Stamm O., Wunderlich F.;
RT "Comparative analysis of the human gimap gene cluster encoding a novel
RT GTPase family.";
RL Gene 341:291-304(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.15 ANGSTROMS) IN COMPLEX WITH GTP ANALOG,
RP FUNCTION, INTERACTION WITH GIMAP2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-103 AND GLU-136.
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).
CC -!- FUNCTION: The dimer has GTPase activity; the active site contains
CC residues from both subunits. {ECO:0000269|PubMed:23454188}.
CC -!- SUBUNIT: Monomer in the presence of bound GDP and in the absence of
CC bound nucleotide. Homodimer in the presence of bound GTP. Heterodimer
CC with GIMAP2. {ECO:0000269|PubMed:23454188}.
CC -!- INTERACTION:
CC Q8NHV1; Q9UG22: GIMAP2; NbExp=2; IntAct=EBI-16039011, EBI-15891037;
CC Q8NHV1; Q8NHV1: GIMAP7; NbExp=2; IntAct=EBI-16039011, EBI-16039011;
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:23454188}.
CC Cytoplasm {ECO:0000269|PubMed:23454188}. Endoplasmic reticulum
CC {ECO:0000269|PubMed:15474311}. Golgi apparatus
CC {ECO:0000269|PubMed:15474311}. Note=Colocalizes with GIMAP2 on the
CC surface of cytoplasmic lipid droplets.
CC -!- TISSUE SPECIFICITY: Most abundantly expressed in spleen, lymph nodes,
CC and fetal kidney, but also present in the heart and the small
CC intestine. Lower expression levels are found in lung, kidney, liver,
CC and thyroid, salivary, and mammary glands. Also detected in the thymus
CC (PubMed:15474311). Detected in T-cells (PubMed:23454188).
CC {ECO:0000269|PubMed:15474311, ECO:0000269|PubMed:23454188}.
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; BC027613; AAH27613.1; -; mRNA.
DR CCDS; CCDS5903.1; -.
DR RefSeq; NP_694968.1; NM_153236.3.
DR PDB; 3ZJC; X-ray; 3.15 A; A/B/C/D/E/F=1-300.
DR PDBsum; 3ZJC; -.
DR AlphaFoldDB; Q8NHV1; -.
DR SMR; Q8NHV1; -.
DR BioGRID; 127968; 1.
DR DIP; DIP-60142N; -.
DR IntAct; Q8NHV1; 1.
DR STRING; 9606.ENSP00000315474; -.
DR GlyGen; Q8NHV1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NHV1; -.
DR PhosphoSitePlus; Q8NHV1; -.
DR SwissPalm; Q8NHV1; -.
DR BioMuta; GIMAP7; -.
DR DMDM; 55976538; -.
DR jPOST; Q8NHV1; -.
DR MassIVE; Q8NHV1; -.
DR MaxQB; Q8NHV1; -.
DR PaxDb; Q8NHV1; -.
DR PeptideAtlas; Q8NHV1; -.
DR PRIDE; Q8NHV1; -.
DR ProteomicsDB; 73762; -.
DR Antibodypedia; 18613; 126 antibodies from 22 providers.
DR DNASU; 168537; -.
DR Ensembl; ENST00000313543.5; ENSP00000315474.4; ENSG00000179144.5.
DR GeneID; 168537; -.
DR KEGG; hsa:168537; -.
DR MANE-Select; ENST00000313543.5; ENSP00000315474.4; NM_153236.4; NP_694968.1.
DR UCSC; uc003whk.4; human.
DR CTD; 168537; -.
DR DisGeNET; 168537; -.
DR GeneCards; GIMAP7; -.
DR HGNC; HGNC:22404; GIMAP7.
DR HPA; ENSG00000179144; Tissue enhanced (lymphoid).
DR MIM; 616961; gene.
DR neXtProt; NX_Q8NHV1; -.
DR OpenTargets; ENSG00000179144; -.
DR PharmGKB; PA134915933; -.
DR VEuPathDB; HostDB:ENSG00000179144; -.
DR eggNOG; ENOG502R7PE; Eukaryota.
DR GeneTree; ENSGT00940000159509; -.
DR HOGENOM; CLU_010468_0_0_1; -.
DR InParanoid; Q8NHV1; -.
DR OMA; PHAILMV; -.
DR OrthoDB; 1108753at2759; -.
DR PhylomeDB; Q8NHV1; -.
DR TreeFam; TF330845; -.
DR PathwayCommons; Q8NHV1; -.
DR SignaLink; Q8NHV1; -.
DR BioGRID-ORCS; 168537; 7 hits in 1062 CRISPR screens.
DR ChiTaRS; GIMAP7; human.
DR GenomeRNAi; 168537; -.
DR Pharos; Q8NHV1; Tbio.
DR PRO; PR:Q8NHV1; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8NHV1; protein.
DR Bgee; ENSG00000179144; Expressed in granulocyte and 180 other tissues.
DR ExpressionAtlas; Q8NHV1; baseline and differential.
DR Genevisible; Q8NHV1; HS.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB.
DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0046039; P:GTP metabolic process; IDA:UniProtKB.
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; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW GTP-binding; Lipid droplet; Nucleotide-binding; Reference proteome.
FT CHAIN 1..300
FT /note="GTPase IMAP family member 7"
FT /id="PRO_0000190993"
FT DOMAIN 6..210
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 15..22
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 42..46
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 63..66
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 132..135
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 168..170
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT BINDING 17..23
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:3ZJC"
FT BINDING 37
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:3ZJC"
FT BINDING 133..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:3ZJC"
FT BINDING 169
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0007744|PDB:3ZJC"
FT SITE 103
FT /note="Important for catalytic activity"
FT VARIANT 83
FT /note="R -> C (in dbSNP:rs3735080)"
FT /id="VAR_049534"
FT MUTAGEN 103
FT /note="R->D: Abolishes GTPase activity. No effect on GTP
FT binding and on dimerization."
FT /evidence="ECO:0000269|PubMed:23454188"
FT MUTAGEN 136
FT /note="E->W: Impairs dimerization and abolishes GTPase
FT activity. No effect on GTP binding."
FT /evidence="ECO:0000269|PubMed:23454188"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 21..29
FT /evidence="ECO:0007829|PDB:3ZJC"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:3ZJC"
FT STRAND 55..63
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 74..88
FT /evidence="ECO:0007829|PDB:3ZJC"
FT STRAND 93..102
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 106..119
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 121..125
FT /evidence="ECO:0007829|PDB:3ZJC"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:3ZJC"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 175..195
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 204..237
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 243..261
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 264..271
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 273..287
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:3ZJC"
FT HELIX 296..298
FT /evidence="ECO:0007829|PDB:3ZJC"
SQ SEQUENCE 300 AA; 34509 MW; 1E4889F4D7A011A2 CRC64;
MAESEDRSLR IVLVGKTGSG KSATANTILG EEIFDSRIAA QAVTKNCQKA SREWQGRDLL
VVDTPGLFDT KESLDTTCKE ISRCIISSCP GPHAIVLVLL LGRYTEEEQK TVALIKAVFG
KSAMKHMVIL FTRKEELEGQ SFHDFIADAD VGLKSIVKEC GNRCCAFSNS KKTSKAEKES
QVQELVELIE KMVQCNEGAY FSDDIYKDTE ERLKQREEVL RKIYTDQLNE EIKLVEEDKH
KSEEEKEKEI KLLKLKYDEK IKNIREEAER NIFKDVFNRI WKMLSEIWHR FLSKCKFYSS
