TXLNG_MOUSE
ID TXLNG_MOUSE Reviewed; 524 AA.
AC Q8BHN1; A2AFJ5; Q148Z8; Q2LGB1; Q2PMX1; Q8BP11;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Gamma-taxilin;
DE AltName: Full=Factor inhibiting ATF4-mediated transcription;
DE Short=FIAT;
DE AltName: Full=Lipopolysaccharide-responsive gene protein;
GN Name=Txlng; Synonyms=Lrg;
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] (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 1-523
RP (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND
RP INDUCTION.
RX PubMed=19913514; DOI=10.1016/j.bbrc.2009.11.047;
RA Du K., Chen Y., Dai Z., Bi Y., Cai T., Hou L., Chai Y., Song Q., Chen S.,
RA Luo W., Chen J.;
RT "Molecular cloning and functional characterization of a mouse gene
RT upregulated by lipopolysaccharide treatment reveals alternative splicing.";
RL Biochem. Biophys. Res. Commun. 391:267-271(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain cortex, Head, and Testis;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 FUNCTION, AND SUBUNIT.
RX PubMed=15911876; DOI=10.1083/jcb.200412139;
RA Yu V.W., Ambartsoumian G., Verlinden L., Moir J.M., Prud'homme J.,
RA Gauthier C., Roughley P.J., St-Arnaud R.;
RT "FIAT represses ATF4-mediated transcription to regulate bone mass in
RT transgenic mice.";
RL J. Cell Biol. 169:591-601(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [7]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=19232401; DOI=10.1016/j.gep.2009.02.002;
RA Yu V.W., Akhouayri O., St-Arnaud R.;
RT "FIAT is co-expressed with its dimerization target ATF4 in early
RT osteoblasts, but not in osteocytes.";
RL Gene Expr. Patterns 9:335-340(2009).
RN [8]
RP FUNCTION.
RX PubMed=19016261; DOI=10.1002/jcb.21995;
RA Yu V.W., El-Hoss J., St-Arnaud R.;
RT "FIAT inhibition increases osteoblast activity by modulating Atf4-dependent
RT functions.";
RL J. Cell. Biochem. 106:186-192(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Liver, 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: May be involved in intracellular vesicle traffic (By
CC similarity). Inhibits ATF4-mediated transcription, possibly by
CC dimerizing with ATF4 to form inactive dimers that cannot bind DNA. May
CC be involved in regulating bone mass density through an ATF4-dependent
CC pathway. May be involved in cell cycle progression. {ECO:0000250,
CC ECO:0000269|PubMed:15911876, ECO:0000269|PubMed:19016261,
CC ECO:0000269|PubMed:19913514}.
CC -!- SUBUNIT: Binds to the C-terminal coiled coil region of syntaxin family
CC members STX1A, STX3A and STX4A (By similarity). Forms a heterodimer
CC with ATF4 in osteoblasts. {ECO:0000250, ECO:0000269|PubMed:15911876}.
CC -!- INTERACTION:
CC Q8BHN1; Q9UHD2: TBK1; Xeno; NbExp=2; IntAct=EBI-6116854, EBI-356402;
CC -!- SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000269|PubMed:19913514}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:19913514}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=LrgW;
CC IsoId=Q8BHN1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BHN1-2; Sequence=VSP_011835, VSP_011836, VSP_011837;
CC Name=3; Synonyms=LrgS;
CC IsoId=Q8BHN1-3; Sequence=VSP_011835;
CC -!- DEVELOPMENTAL STAGE: At 16.5 dpc, expressed in osteoblasts surrounding
CC newly formed trabecular bone. At postnatal day 2, detected in most
CC osteoblasts and lining cells, and also strongly expressed in
CC osteocytes. By postnatal week 4, strongly expressed in osteocytes (at
CC protein level). {ECO:0000269|PubMed:19232401}.
CC -!- INDUCTION: By LPS. {ECO:0000269|PubMed:19913514}.
CC -!- SIMILARITY: Belongs to the taxilin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABC47035.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=ABC47035.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=ABC60327.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
CC Sequence=ABC60327.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; DQ316984; ABC47035.1; ALT_SEQ; mRNA.
DR EMBL; DQ320011; ABC60327.1; ALT_SEQ; mRNA.
DR EMBL; AK030100; BAC26785.1; -; mRNA.
DR EMBL; AK031783; BAC27547.1; -; mRNA.
DR EMBL; AK044130; BAC31791.1; -; mRNA.
DR EMBL; AK078477; BAC37296.1; -; mRNA.
DR EMBL; AL672123; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117898; AAI17899.1; -; mRNA.
DR EMBL; BC117899; AAI17900.1; -; mRNA.
DR CCDS; CCDS30510.1; -. [Q8BHN1-1]
DR CCDS; CCDS72463.1; -. [Q8BHN1-3]
DR CCDS; CCDS81194.1; -. [Q8BHN1-2]
DR RefSeq; NP_001277705.1; NM_001290776.1. [Q8BHN1-3]
DR RefSeq; NP_001277706.1; NM_001290777.1. [Q8BHN1-2]
DR RefSeq; NP_849266.1; NM_178935.5. [Q8BHN1-1]
DR AlphaFoldDB; Q8BHN1; -.
DR SMR; Q8BHN1; -.
DR IntAct; Q8BHN1; 3.
DR STRING; 10090.ENSMUSP00000038615; -.
DR iPTMnet; Q8BHN1; -.
DR PhosphoSitePlus; Q8BHN1; -.
DR EPD; Q8BHN1; -.
DR jPOST; Q8BHN1; -.
DR MaxQB; Q8BHN1; -.
DR PaxDb; Q8BHN1; -.
DR PeptideAtlas; Q8BHN1; -.
DR PRIDE; Q8BHN1; -.
DR ProteomicsDB; 298041; -. [Q8BHN1-1]
DR ProteomicsDB; 298042; -. [Q8BHN1-2]
DR ProteomicsDB; 298043; -. [Q8BHN1-3]
DR Antibodypedia; 410; 93 antibodies from 15 providers.
DR DNASU; 353170; -.
DR Ensembl; ENSMUST00000041370; ENSMUSP00000038615; ENSMUSG00000038344. [Q8BHN1-1]
DR Ensembl; ENSMUST00000112315; ENSMUSP00000107934; ENSMUSG00000038344. [Q8BHN1-2]
DR Ensembl; ENSMUST00000112316; ENSMUSP00000107935; ENSMUSG00000038344. [Q8BHN1-3]
DR GeneID; 353170; -.
DR KEGG; mmu:353170; -.
DR UCSC; uc009uuh.2; mouse. [Q8BHN1-1]
DR UCSC; uc009uui.2; mouse. [Q8BHN1-3]
DR CTD; 55787; -.
DR MGI; MGI:3590652; Txlng.
DR VEuPathDB; HostDB:ENSMUSG00000038344; -.
DR eggNOG; KOG1850; Eukaryota.
DR GeneTree; ENSGT00940000155463; -.
DR HOGENOM; CLU_025501_4_1_1; -.
DR InParanoid; Q8BHN1; -.
DR OMA; WRKKSHH; -.
DR OrthoDB; 904532at2759; -.
DR PhylomeDB; Q8BHN1; -.
DR TreeFam; TF318595; -.
DR BioGRID-ORCS; 353170; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Txlng; mouse.
DR PRO; PR:Q8BHN1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8BHN1; protein.
DR Bgee; ENSMUSG00000038344; Expressed in animal zygote and 231 other tissues.
DR ExpressionAtlas; Q8BHN1; baseline and differential.
DR Genevisible; Q8BHN1; MM.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019905; F:syntaxin binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; ISO:MGI.
DR InterPro; IPR026183; Taxilin_fam.
DR PANTHER; PTHR16127; PTHR16127; 1.
DR Pfam; PF09728; Taxilin; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Membrane;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..524
FT /note="Gamma-taxilin"
FT /id="PRO_0000189427"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 106..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 501..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 153..465
FT /evidence="ECO:0000255"
FT COMPBIAS 21..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 12
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT MOD_RES 24
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT MOD_RES 283
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT MOD_RES 512
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NUQ3"
FT VAR_SEQ 55..103
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:19913514"
FT /id="VSP_011835"
FT VAR_SEQ 289..290
FT /note="HI -> VI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011836"
FT VAR_SEQ 291..524
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_011837"
FT CONFLICT 72
FT /note="G -> D (in Ref. 1; ABC47035)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> D (in Ref. 1; ABC47035)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="A -> G (in Ref. 1; ABC47035/ABC60327)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="N -> T (in Ref. 1; ABC60327)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="L -> W (in Ref. 1; ABC47035)"
FT /evidence="ECO:0000305"
FT CONFLICT 514
FT /note="G -> S (in Ref. 1; ABC60327)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 524 AA; 60309 MW; 0228777633E4ED7C CRC64;
MATRLEEVTR GRGGGTEEAS EGGRGGRRRS PPQKFEIGTM EEARICGLGV KADMVCNSQA
NDILQHQDPS CGGTTKKHSL EGDEGSDFIT KNRNLVSSVF CTQEKREEIP GREARTGPPD
GQQDSECSRN KEKTLGKEVL LLMQALNTLS TPEEKLAALC KKYADLLEES RNVQKQMKIL
QKKQAQIVKE KVHLQSEHSK AILARSKLES LCRELQRHNK TLKEENMQQA REEEERRKEA
TAHFQITLNE IQAQLEQHDI HNAKLRQENI ELGEKLKKLI EQYALREEHI DKVFKHKELQ
QQLVDAKLQQ TTQLIKEADE KHQREREFLL KEATESRHKY EQMKQQEVQL KQQLSLYMDK
FEEFQTTMAK SNELFTTFRQ EMEKMTKKIK KLEKETIIWR TKWENNNKAL LQMAEEKTVR
DKEYKAFQIK LERLEKLCRA LQTERNELNE KVEVLKEQVS IKAADGDLVS PATQPCAVLD
SFKETSRRTL GMHLEARAKS VCEKSAAQKP SSSGSPAQGI ESVD
