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GIMA6_MOUSE
ID   GIMA6_MOUSE             Reviewed;         305 AA.
AC   Q8K349; Q5DU66; Q8K434;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=GTPase IMAP family member 6;
DE   AltName: Full=Immunity-associated nucleotide 6 protein;
DE            Short=IAN-6;
DE            Short=mIAN6;
GN   Name=Gimap6; Synonyms=Ian6 {ECO:0000303|PubMed:16509771};
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].
RC   STRAIN=C57BL/6J;
RA   Miazek A., Malissen B.;
RT   "IAN-6, a novel member of IAN family of GTP/GDP-binding proteins is
RT   involved in thymocyte maturation.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT   complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT   by screening of terminal sequences of cDNA clones randomly sampled from
RT   size-fractionated libraries.";
RL   DNA Res. 11:127-135(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Head;
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].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland;
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   TISSUE SPECIFICITY.
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).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:Q6P9H5}.
CC   -!- TISSUE SPECIFICITY: Expressed in thymus (in thymocytes), spleen (in
CC       splenocytes), lymph node and lung. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD90383.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown because it seems to be derived from a pre-mRNA.; Evidence={ECO:0000305};
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DR   EMBL; AF503921; AAN03835.1; -; mRNA.
DR   EMBL; AK220304; BAD90383.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; AK160244; BAE35709.1; -; mRNA.
DR   EMBL; BC028779; AAH28779.1; -; mRNA.
DR   CCDS; CCDS20111.1; -.
DR   RefSeq; NP_694815.1; NM_153175.3.
DR   AlphaFoldDB; Q8K349; -.
DR   SMR; Q8K349; -.
DR   STRING; 10090.ENSMUSP00000059371; -.
DR   PhosphoSitePlus; Q8K349; -.
DR   EPD; Q8K349; -.
DR   MaxQB; Q8K349; -.
DR   PaxDb; Q8K349; -.
DR   PRIDE; Q8K349; -.
DR   ProteomicsDB; 265747; -.
DR   Antibodypedia; 18618; 75 antibodies from 16 providers.
DR   DNASU; 231931; -.
DR   Ensembl; ENSMUST00000053661; ENSMUSP00000059371; ENSMUSG00000047867.
DR   GeneID; 231931; -.
DR   KEGG; mmu:231931; -.
DR   UCSC; uc009bvm.1; mouse.
DR   CTD; 474344; -.
DR   MGI; MGI:1918876; Gimap6.
DR   VEuPathDB; HostDB:ENSMUSG00000047867; -.
DR   eggNOG; ENOG502R7PE; Eukaryota.
DR   GeneTree; ENSGT00940000162548; -.
DR   HOGENOM; CLU_956336_0_0_1; -.
DR   InParanoid; Q8K349; -.
DR   OMA; QKGSREW; -.
DR   OrthoDB; 1092873at2759; -.
DR   PhylomeDB; Q8K349; -.
DR   TreeFam; TF330845; -.
DR   BioGRID-ORCS; 231931; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q8K349; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8K349; protein.
DR   Bgee; ENSMUSG00000047867; Expressed in interventricular septum and 158 other tissues.
DR   ExpressionAtlas; Q8K349; baseline and differential.
DR   Genevisible; Q8K349; MM.
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..305
FT                   /note="GTPase IMAP family member 6"
FT                   /id="PRO_0000333012"
FT   DOMAIN          101..302
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          37..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..117
FT                   /note="G1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          137..141
FT                   /note="G2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          158..161
FT                   /note="G3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          225..228
FT                   /note="G4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   REGION          262..264
FT                   /note="G5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01057"
FT   COMPBIAS        39..56
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110..118
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT   BINDING         131
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UG22"
FT   BINDING         226..228
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT   BINDING         263
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250|UniProtKB:Q8WWP7"
FT   CONFLICT        172
FT                   /note="T -> S (in Ref. 1; AAN03835)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182
FT                   /note="S -> P (in Ref. 1; AAN03835)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   305 AA;  34145 MW;  931A6ED7EEDD11DB CRC64;
     MDWLYRKTLG SIGSCSIETF PWPFYSFFQR IYISTPPGKP ENSPETSATE VGEQRPSCLS
     ASPVVEEEEC EHRPEKNPTR QWPLDSGQGL TKGLKEKKLT PKRLQLLLVG KTGSGKSATG
     NSILGRQAFE SKISARPVTT TFQKGTREFE GKELEVIDTP DIFSPQNQPE ATAKKICDLL
     ASPGPHAVLL VIQVGRYTAE DQAVARCLQE IFGNTILAYT ILVFTRKEDL AEGSLEEYIQ
     ENNNKSLDVL DVACERRHCG FNNKAQGDEQ EAQLKKLMEE VELILWENEG HCYTMEFPNV
     PSKTL
 
 
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