MIPT3_MOUSE
ID MIPT3_MOUSE Reviewed; 625 AA.
AC Q149C2; Q538H5; Q80VQ3; Q9CS98;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=TRAF3-interacting protein 1;
DE AltName: Full=Intraflagellar transport protein 54 homolog;
DE AltName: Full=Microtubule-interacting protein associated with TRAF3;
DE Short=MIP-T3;
GN Name=Traf3ip1; Synonyms=Ift54, Mipt3;
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 Ma B., He C., Lee C., Elias J.A.;
RT "Mus musculus microtubule-interacting protein that associates with TRAF3.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 142-625.
RC STRAIN=C57BL/6J; TISSUE=Embryo;
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 IDENTIFICATION IN THE IFT COMPLEX B, INTERACTION WITH IFT88, AND
RP SUBCELLULAR LOCATION.
RX PubMed=19253336; DOI=10.1002/cm.20346;
RA Follit J.A., Xu F., Keady B.T., Pazour G.J.;
RT "Characterization of mouse IFT complex B.";
RL Cell Motil. Cytoskeleton 66:457-468(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-316 AND SER-409, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
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).
RN [6]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=21945076; DOI=10.1016/j.ydbio.2011.09.001;
RA Berbari N.F., Kin N.W., Sharma N., Michaud E.J., Kesterson R.A.,
RA Yoder B.K.;
RT "Mutations in Traf3ip1 reveal defects in ciliogenesis, embryonic
RT development, and altered cell size regulation.";
RL Dev. Biol. 360:66-76(2011).
RN [7]
RP FUNCTION, INTERACTION WITH MAP4, AND MUTAGENESIS OF ILE-453.
RX PubMed=26487268; DOI=10.1038/ncomms9666;
RA Bizet A.A., Becker-Heck A., Ryan R., Weber K., Filhol E., Krug P.,
RA Halbritter J., Delous M., Lasbennes M.C., Linghu B., Oakeley E.J.,
RA Zarhrate M., Nitschke P., Garfa-Traore M., Serluca F., Yang F.,
RA Bouwmeester T., Pinson L., Cassuto E., Dubot P., Elshakhs N.A., Sahel J.A.,
RA Salomon R., Drummond I.A., Gubler M.C., Antignac C., Chibout S.,
RA Szustakowski J.D., Hildebrandt F., Lorentzen E., Sailer A.W., Benmerah A.,
RA Saint-Mezard P., Saunier S.;
RT "Mutations in TRAF3IP1/IFT54 reveal a new role for IFT proteins in
RT microtubule stabilization.";
RL Nat. Commun. 6:8666-8666(2015).
CC -!- FUNCTION: Plays an inhibitory role on IL13 signaling by binding to
CC IL13RA1. Involved in suppression of IL13-induced STAT6 phosphorylation,
CC transcriptional activity and DNA-binding. Recruits TRAF3 and DISC1 to
CC the microtubules (By similarity). Involved in epithelial morphogenesis
CC and in the regulation of microtubule cytoskeleton organization. Is a
CC negative regulator of microtubule stability, acting through the control
CC of MAP4 levels (PubMed:26487268). Involved in ciliogenesis
CC (PubMed:21945076). {ECO:0000250|UniProtKB:Q8TDR0,
CC ECO:0000269|PubMed:21945076, ECO:0000269|PubMed:26487268}.
CC -!- SUBUNIT: Interacts with IL13RA1. Binds to microtubules, TRAF3 and DISC1
CC (By similarity). Component of the IFT complex B, at least composed of
CC IFT20, IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57,
CC IFT74, IFT80, IFT81, and IFT88. Interacts with IFT88. Interacts with
CC MAP4 (PubMed:26487268). {ECO:0000250, ECO:0000269|PubMed:19253336,
CC ECO:0000269|PubMed:26487268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8TDR0}. Cell projection, cilium
CC {ECO:0000269|PubMed:19253336}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:21945076}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000269|PubMed:21945076}. Note=Microtubules. In the cilium,
CC it is observed at the ciliary base, ciliary transition zone and ciliary
CC tip. {ECO:0000250|UniProtKB:Q8TDR0}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant mice are not viable and have
CC neural development defects, abnormal neural tube patterning,
CC polydactyly, cardiac edema, and variable microphthalmia. Mutant cells
CC have a marked reduction in the number of cilia.
CC {ECO:0000269|PubMed:21945076}.
CC -!- SIMILARITY: Belongs to the TRAF3IP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH46538.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AY613437; AAT72918.1; -; mRNA.
DR EMBL; BC046538; AAH46538.1; ALT_SEQ; mRNA.
DR EMBL; BC117868; AAI17869.1; -; mRNA.
DR EMBL; AK014457; BAB29364.1; -; mRNA.
DR CCDS; CCDS35664.1; -.
DR RefSeq; NP_082994.1; NM_028718.2.
DR PDB; 5FMU; X-ray; 1.59 A; A/B/C/D=1-133.
DR PDBsum; 5FMU; -.
DR AlphaFoldDB; Q149C2; -.
DR SMR; Q149C2; -.
DR BioGRID; 216428; 1.
DR ComplexPortal; CPX-5028; IFT-B complex.
DR IntAct; Q149C2; 1.
DR STRING; 10090.ENSMUSP00000042391; -.
DR iPTMnet; Q149C2; -.
DR PhosphoSitePlus; Q149C2; -.
DR jPOST; Q149C2; -.
DR MaxQB; Q149C2; -.
DR PaxDb; Q149C2; -.
DR PeptideAtlas; Q149C2; -.
DR PRIDE; Q149C2; -.
DR ProteomicsDB; 252568; -.
DR Antibodypedia; 34501; 232 antibodies from 28 providers.
DR Ensembl; ENSMUST00000047242; ENSMUSP00000042391; ENSMUSG00000034292.
DR GeneID; 74019; -.
DR KEGG; mmu:74019; -.
DR UCSC; uc007cax.2; mouse.
DR CTD; 26146; -.
DR MGI; MGI:1921269; Traf3ip1.
DR VEuPathDB; HostDB:ENSMUSG00000034292; -.
DR eggNOG; KOG3809; Eukaryota.
DR GeneTree; ENSGT00720000108822; -.
DR InParanoid; Q149C2; -.
DR OrthoDB; 1008610at2759; -.
DR PhylomeDB; Q149C2; -.
DR TreeFam; TF315473; -.
DR Reactome; R-MMU-5620924; Intraflagellar transport.
DR BioGRID-ORCS; 74019; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Traf3ip1; mouse.
DR PRO; PR:Q149C2; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q149C2; protein.
DR Bgee; ENSMUSG00000034292; Expressed in olfactory epithelium and 219 other tissues.
DR ExpressionAtlas; Q149C2; baseline and differential.
DR Genevisible; Q149C2; MM.
DR GO; GO:0005930; C:axoneme; IDA:MGI.
DR GO; GO:0005813; C:centrosome; IDA:MGI.
DR GO; GO:0036064; C:ciliary basal body; IDA:MGI.
DR GO; GO:0097546; C:ciliary base; ISS:UniProtKB.
DR GO; GO:0097542; C:ciliary tip; ISS:UniProtKB.
DR GO; GO:0035869; C:ciliary transition zone; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030992; C:intraciliary transport particle B; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0005102; F:signaling receptor binding; ISO:MGI.
DR GO; GO:0015631; F:tubulin binding; ISO:MGI.
DR GO; GO:0060271; P:cilium assembly; IMP:MGI.
DR GO; GO:0051607; P:defense response to virus; IMP:MGI.
DR GO; GO:0031076; P:embryonic camera-type eye development; IMP:MGI.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:MGI.
DR GO; GO:0035050; P:embryonic heart tube development; IMP:MGI.
DR GO; GO:0035720; P:intraciliary anterograde transport; IC:ComplexPortal.
DR GO; GO:0042073; P:intraciliary transport; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; ISS:UniProtKB.
DR GO; GO:0001738; P:morphogenesis of a polarized epithelium; IMP:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; IMP:CACAO.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:MGI.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:MGI.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISO:MGI.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
DR GO; GO:0021532; P:neural tube patterning; IMP:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0051101; P:regulation of DNA binding; ISO:MGI.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0060831; P:smoothened signaling pathway involved in dorsal/ventral neural tube patterning; IMP:MGI.
DR Gene3D; 1.10.418.50; -; 1.
DR InterPro; IPR018799; TRAF3IP1.
DR InterPro; IPR041476; TRAF3IP1_C.
DR InterPro; IPR040468; TRAF3IP1_N.
DR InterPro; IPR042576; TRAF3IP1_N_sf.
DR PANTHER; PTHR31363; PTHR31363; 1.
DR Pfam; PF10243; MIP-T3; 1.
DR Pfam; PF17749; MIP-T3_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..625
FT /note="TRAF3-interacting protein 1"
FT /id="PRO_0000299545"
FT REGION 1..322
FT /note="Abolishes microtubules binding when missing"
FT /evidence="ECO:0000250"
FT REGION 130..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..625
FT /note="DISC1-interaction domain"
FT /evidence="ECO:0000250"
FT COILED 472..600
FT /evidence="ECO:0000255"
FT COMPBIAS 149..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..432
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MUTAGEN 453
FT /note="I->R: Decreased interaction with MAP4. No effect on
FT interaction with IFT20."
FT CONFLICT 52
FT /note="L -> F (in Ref. 2; AAH46538)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="R -> K (in Ref. 2; AAI17869)"
FT /evidence="ECO:0000305"
FT CONFLICT 371
FT /note="K -> E (in Ref. 3; BAB29364)"
FT /evidence="ECO:0000305"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 32..46
FT /evidence="ECO:0007829|PDB:5FMU"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:5FMU"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 66..84
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 92..96
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 101..116
FT /evidence="ECO:0007829|PDB:5FMU"
FT HELIX 122..130
FT /evidence="ECO:0007829|PDB:5FMU"
SQ SEQUENCE 625 AA; 71037 MW; 2790471DAE271F7D CRC64;
MNAAVVRRTQ EALGKVIRRP PLTEKLLNKP PFRYLHDIIT EVIRITGFMK GLYTDAEMKS
ENVKDKDAKI SFLQKAIDVV MMVSGEPLAA KPARIVAGHE PERTNELLQL IGKCCLSKLS
SDEAVKRVLA GDKGDSRGRA QRTSKAQEPN NKSGKEEESR IHKEDKRSSE AKERSASAEH
KQKEELKEDS KPREKERDKE KAKEADRDRH RDPDRDRNRD GEREKARARA KDRDRNNRDR
DREAERDRER DRRSEGGKEK ERVKDRDRDR DKGRDRERRK SKNGEHTRDP DREKSRDADK
PEKKSSSSGE ISRKLSDGSF KDVKAEMEAD ISVGASRSST LKPSKRRSKH SLEGDSPSDA
EVEAGPAGQD KPEVMENAEV PSELPSSLRR IPRPGSARPA PPRVKRQEST ETLVVDRSGS
GKTVSSVIID SQNSDNEDDE QFVVEAAPQL SEIADIDMVP SGELEDEEKH GGLVKKILET
KKDYEKLQQS LKPGEKERSL IFESAWKKEK DIVSKEIEKL RVSIQTLCKS ALPLGKIMDY
IQEDVDAMQN ELQLWHSENR QHAEALSQEQ SITDSAVEPL KAELSELEQQ IRDQQDKICA
VKANILKNEE KIQKMVHSIN LSSRR
