GIMA6_RAT
ID GIMA6_RAT Reviewed; 304 AA.
AC Q5FVN6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=GTPase IMAP family member 6;
DE AltName: Full=Immunity-associated nucleotide 6 protein;
DE Short=IAN-6;
GN Name=Gimap6; Synonyms=Ian6;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Brown Norway;
RX PubMed=16103028; DOI=10.1093/intimm/dxh302;
RA Dion C., Carter C., Hepburn L., Coadwell W.J., Morgan G., Graham M.,
RA Pugh N., Anderson G., Butcher G.W., Miller J.R.;
RT "Expression of the Ian family of putative GTPases during T cell development
RT and description of an Ian with three sets of GTP/GDP-binding motifs.";
RL Int. Immunol. 17:1257-1268(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Rutledge E.A., Van Yserloo B., Fuller J.M., Moralejo D.H., Ettinger R.A.,
RA Gaur P., Peterson M.R., Hoehna J.L., Lernmark A.;
RT "Expression of the gimap gene cluster is reduced in the type 1 diabetes BB
RT lymphopenic rat.";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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).
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q6P9H5}.
CC -!- TISSUE SPECIFICITY: Expressed in B and T-cells and peritoneal
CC macrophages. {ECO:0000269|PubMed:16103028}.
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; AJ633683; CAG17878.1; -; mRNA.
DR EMBL; DQ125342; ABB03711.1; -; mRNA.
DR EMBL; DQ125343; ABB03704.1; -; mRNA.
DR EMBL; BC089859; AAH89859.1; -; mRNA.
DR RefSeq; NP_001011968.1; NM_001011968.3.
DR AlphaFoldDB; Q5FVN6; -.
DR SMR; Q5FVN6; -.
DR STRING; 10116.ENSRNOP00000047855; -.
DR PaxDb; Q5FVN6; -.
DR Ensembl; ENSRNOT00000049038; ENSRNOP00000047855; ENSRNOG00000033338.
DR GeneID; 297076; -.
DR KEGG; rno:297076; -.
DR UCSC; RGD:1305041; rat.
DR CTD; 474344; -.
DR RGD; 1305041; Gimap6.
DR eggNOG; ENOG502R7PE; Eukaryota.
DR GeneTree; ENSGT00940000162548; -.
DR HOGENOM; CLU_956336_0_0_1; -.
DR InParanoid; Q5FVN6; -.
DR OMA; QKGSREW; -.
DR OrthoDB; 1092873at2759; -.
DR PhylomeDB; Q5FVN6; -.
DR TreeFam; TF330845; -.
DR PRO; PR:Q5FVN6; -.
DR Proteomes; UP000002494; Chromosome 4.
DR Bgee; ENSRNOG00000033338; Expressed in thymus and 17 other tissues.
DR Genevisible; Q5FVN6; RN.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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 2: Evidence at transcript level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..304
FT /note="GTPase IMAP family member 6"
FT /id="PRO_0000333013"
FT DOMAIN 100..301
FT /note="AIG1-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 39..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 109..116
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 136..140
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 157..160
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 224..227
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 261..263
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT COMPBIAS 43..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 109..117
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 130
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT BINDING 225..227
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 262
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
SQ SEQUENCE 304 AA; 33691 MW; 1851F4905F014945 CRC64;
MNWLYSKTLG SIGSCCIDTL PWPFHSFFQR NLLALPGEPG NPLESSATES GKQSRSCLSA
SPVMEEEGCE HSLQKNPTRQ LPLDPGQELT KDLKEKKLTP KRLQLLLVGK TGSGKSATGN
SILGRQVFES KISARPVTMA FQKGSRELEG KELEVIDTPD ILSPQNQPEA TAKKICDILA
SPGPHAVLLV IQVGRYTTED QEAARCLQEI FGNGILAYTI LVFTRKEELA EGSLEEYIKE
NNNKTLDALD VACERRHCGF NNRAQGDEQE AQLQKLMEEI ESILWENEGH CYTMELPNVS
SKTL
