GIMA8_RAT
ID GIMA8_RAT Reviewed; 688 AA.
AC Q4KLG2; Q3LF72;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=GTPase IMAP family member 8;
DE AltName: Full=Immune-associated nucleotide-binding protein 9;
DE Short=IAN-9;
DE AltName: Full=Protein IanT;
GN Name=Gimap8; Synonyms=Ian9, Iant;
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=PVG.RT1A; TISSUE=Thymus;
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].
RC STRAIN=BBDR.lyp-;
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 -!- FUNCTION: Exerts an anti-apoptotic effect in the immune system and is
CC involved in responses to infections. {ECO:0000250|UniProtKB:Q75N62}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:Q75N62}. Golgi apparatus
CC {ECO:0000250|UniProtKB:Q75N62}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q75N62}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q8ND71}.
CC -!- TISSUE SPECIFICITY: Spleen, thymus and T-cells. Greatly reduced in T-
CC cells from lymphopenic rats. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ633685; CAG17880.1; -; mRNA.
DR EMBL; DQ125335; ABB03698.1; -; mRNA.
DR EMBL; DQ125336; ABB03699.1; -; mRNA.
DR EMBL; BC099228; AAH99228.1; -; mRNA.
DR RefSeq; NP_001029095.1; NM_001033923.1.
DR AlphaFoldDB; Q4KLG2; -.
DR SMR; Q4KLG2; -.
DR STRING; 10116.ENSRNOP00000055946; -.
DR PaxDb; Q4KLG2; -.
DR PRIDE; Q4KLG2; -.
DR Ensembl; ENSRNOT00000059173; ENSRNOP00000055946; ENSRNOG00000020169.
DR GeneID; 500112; -.
DR KEGG; rno:500112; -.
DR UCSC; RGD:1564570; rat.
DR CTD; 155038; -.
DR RGD; 1564570; Gimap8.
DR eggNOG; ENOG502RB0C; Eukaryota.
DR GeneTree; ENSGT00940000162462; -.
DR HOGENOM; CLU_010468_5_1_1; -.
DR InParanoid; Q4KLG2; -.
DR PhylomeDB; Q4KLG2; -.
DR TreeFam; TF330845; -.
DR PRO; PR:Q4KLG2; -.
DR Proteomes; UP000002494; Chromosome 4.
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:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0070232; P:regulation of T cell apoptotic process; ISO:RGD.
DR Gene3D; 3.40.50.300; -; 3.
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; 3.
DR SUPFAM; SSF52540; SSF52540; 3.
DR PROSITE; PS51720; G_AIG1; 3.
PE 2: Evidence at transcript level;
KW Coiled coil; Cytoplasm; Endoplasmic reticulum; Golgi apparatus;
KW GTP-binding; Mitochondrion; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..688
FT /note="GTPase IMAP family member 8"
FT /id="PRO_0000341972"
FT DOMAIN 46..246
FT /note="AIG1-type G 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT DOMAIN 281..471
FT /note="AIG1-type G 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT DOMAIN 472..681
FT /note="AIG1-type G 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 22..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..62
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 82..86
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 103..106
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 171..174
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT REGION 207..209
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT BINDING 55..63
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT BINDING 172..174
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT BINDING 208
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT CONFLICT 151
FT /note="I -> F (in Ref. 1; CAG17880)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="T -> A (in Ref. 1; CAG17880)"
FT /evidence="ECO:0000305"
FT CONFLICT 417
FT /note="E -> G (in Ref. 1; CAG17880)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 688 AA; 77072 MW; 4897B08BB5535B03 CRC64;
MATSSHQGAA AGSQMEHRLC ETSIGQGERP RASRGQESNF KQSQGTSTLR LLLLGKQGAG
KSATGNTILG KAVFESRFSH HMVTKRCQSE SVSVRGKQVI VIDTPDLFSS LGCPEVQQQN
LRQCLDLLAD PYVLLLVTPI GHSTEEDKKT IEGIQGVFGP QAYRHMIVVF TREDELGEDT
LQNHIESKKY LKKLIENIGS QRCCAFNNKA DKKQQELQVS QFLDAIEFLM MESPGTYFEP
LKTENSGVQG CGTGVTYKGD NLCGSKKRQP QITGPGWDRD TPELRVLLMG KRGVGKSAAG
NSILGKQVFK TQFSEKQRVT EAFASHSRLW NQKKFLIIDS PEISSWKLDE SDVKEHTFPG
PHAFLLVTPL GSSLKSGDSV FSIIKRIFGE KFIKFTIILF TRKEDFEGQD LDTFTKENDA
LCNLIQIFEG RYAVFNYRAT VEEEQSQVGK LLSQIESVVQ HHNNKPCVIR EKELLNIILL
GRSGVGKSAT GNTILGRPAF VSQLRAQPVT SRSQSGRRTL DWQDIVVVDT PSLNQMSGTE
KNPAQLKKEI KQCLLQNCEE GMKVFVLVFQ LGRFTQEDEA VVEQLEASFE ENIMKYMIVL
FTRKEDLGDG DLYDFTNNTK NKVLKRIFKK CKGRVCAFNN KETGEDQETQ VKALLTIAND
LKRSYDEHST SWMDQLKSAV GQITTVFK