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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}.
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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
 
 
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