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GIMA8_MOUSE
ID   GIMA8_MOUSE             Reviewed;         688 AA.
AC   Q75N62; Q3UZ12;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=GTPase IMAP family member 8;
DE            Short=mGIMAP8;
DE   AltName: Full=Immune-associated nucleotide-binding protein 9;
DE            Short=IAN-9;
DE   AltName: Full=Immunity-associated protein 8;
GN   Name=Gimap8; Synonyms=Ian9 {ECO:0000303|PubMed:16509771}, Imap8;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=16088918; DOI=10.1002/jcb.20552;
RA   Kruecken J., Epe M., Benten W.P., Falkenroth N., Wunderlich F.;
RT   "Malaria-suppressible expression of the anti-apoptotic triple GTPase
RT   mGIMAP8.";
RL   J. Cell. Biochem. 96:339-348(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   STRAIN=C57BL/6J;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Exerts an anti-apoptotic effect in the immune system and is
CC       involved in responses to infections. {ECO:0000269|PubMed:16088918}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC       {ECO:0000269|PubMed:16088918}. Golgi apparatus
CC       {ECO:0000269|PubMed:16088918}. Mitochondrion
CC       {ECO:0000269|PubMed:16088918}. Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q8ND71}.
CC   -!- TISSUE SPECIFICITY: Abundantly expressed in the thymus (in thymocytes),
CC       spleen (in splenocytes), lymph node, followed by bone marrow and lung.
CC       {ECO:0000269|PubMed:16088918, ECO:0000269|PubMed:16509771}.
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; AJ617674; CAE85147.1; -; mRNA.
DR   EMBL; AB178029; BAD16741.1; -; mRNA.
DR   EMBL; AK134199; BAE22049.1; -; mRNA.
DR   EMBL; BC137943; AAI37944.1; -; mRNA.
DR   EMBL; BC137944; AAI37945.1; -; mRNA.
DR   CCDS; CCDS20108.1; -.
DR   RefSeq; NP_001070878.1; NM_001077410.1.
DR   RefSeq; NP_997651.1; NM_212486.2.
DR   AlphaFoldDB; Q75N62; -.
DR   SMR; Q75N62; -.
DR   IntAct; Q75N62; 1.
DR   STRING; 10090.ENSMUSP00000077350; -.
DR   iPTMnet; Q75N62; -.
DR   PhosphoSitePlus; Q75N62; -.
DR   EPD; Q75N62; -.
DR   MaxQB; Q75N62; -.
DR   PaxDb; Q75N62; -.
DR   PRIDE; Q75N62; -.
DR   ProteomicsDB; 267795; -.
DR   Antibodypedia; 2915; 127 antibodies from 20 providers.
DR   DNASU; 243374; -.
DR   Ensembl; ENSMUST00000203083; ENSMUSP00000145286; ENSMUSG00000064262.
DR   Ensembl; ENSMUST00000203509; ENSMUSP00000145255; ENSMUSG00000064262.
DR   GeneID; 243374; -.
DR   KEGG; mmu:243374; -.
DR   UCSC; uc009bvf.1; mouse.
DR   CTD; 155038; -.
DR   MGI; MGI:2685303; Gimap8.
DR   VEuPathDB; HostDB:ENSMUSG00000064262; -.
DR   eggNOG; ENOG502RB0C; Eukaryota.
DR   GeneTree; ENSGT00940000162462; -.
DR   HOGENOM; CLU_010468_5_1_1; -.
DR   InParanoid; Q75N62; -.
DR   OMA; QHCLELS; -.
DR   OrthoDB; 1033397at2759; -.
DR   PhylomeDB; Q75N62; -.
DR   TreeFam; TF330845; -.
DR   BioGRID-ORCS; 243374; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q75N62; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q75N62; protein.
DR   Bgee; ENSMUSG00000064262; Expressed in mesenteric lymph node and 151 other tissues.
DR   ExpressionAtlas; Q75N62; baseline and differential.
DR   Genevisible; Q75N62; MM.
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; IMP:MGI.
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   1: Evidence at protein level;
KW   Cytoplasm; Endoplasmic reticulum; Golgi apparatus; GTP-binding;
KW   Mitochondrion; Nucleotide-binding; Reference proteome; Repeat.
FT   CHAIN           1..688
FT                   /note="GTPase IMAP family member 8"
FT                   /id="PRO_0000341971"
FT   DOMAIN          46..247
FT                   /note="AIG1-type G 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   DOMAIN          282..472
FT                   /note="AIG1-type G 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   DOMAIN          473..677
FT                   /note="AIG1-type G 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          1..42
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          172..175
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          208..210
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   COMPBIAS        26..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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         173..175
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT   BINDING         209
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT   CONFLICT        204
FT                   /note="C -> Y (in Ref. 3; BAE22049)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   688 AA;  76843 MW;  8B20E5ED1336DC08 CRC64;
     MATSSHQGAA AGSQAEHRSC EASVGQGERP SASQGQEGNF KQNQGTSTLR LLLLGKQGAG
     KSATGNTILG KAVFESKFSD HMVTDRCQSE SVSVRGKQVI VIDTPDLFSS LSCSEVRQQN
     LKQCLELLAD DHCVLLLVTP IGHYTEEDRE TIEGIWGKIG PKAYRHMIVV FTREDELDED
     SLWNYIESKE SLKELIKNIG SRRCCTFNNK ADKKQRELQV FKLLDAIELL MMESPEPYFE
     PLKMESSGVQ GCGNGVTYEG DTLCGSKKRQ PQITGPDCDP DMPELRVLLM GKRGVGKSAA
     GNSILGKQVF KTQFSEKQRV TKAFASHSRV WQGKKVLIID SPEISSWKLD ESAVKNHTFP
     GPHAFLLVTP LGSSLKSDDD VFSIIKRIFG EKFTKFTIVL FTRKEDFEDQ ALDKVIKEND
     ALYNLTQKFG ERYAIFNYRA SVEEEQSQVG KLLSQIEKMV QCHSNKPCVI REKELLNIIL
     LGRSGAGKSA TGNTILGRSA FFSQLRAQPV TSSSQSGKRT LDWQDVVVVD TPSFIQTPGT
     EKDPSRLKEE IHHCLSLCEE GMKIFVLVLQ LGRFTQEDEV VVEQLEASFE ENIMKYMIVL
     FTRKEDLGDG DLHDYTNNTK NKALKKILKK CNGRVCAFNN KETGEDQETQ VKGLLKIANS
     LKKNYDEHSN SWVGQLKSTL GQITMAFK
 
 
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