MIPT3_RAT
ID MIPT3_RAT Reviewed; 653 AA.
AC Q5XIN3;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
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 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 [LARGE SCALE MRNA].
RC TISSUE=Testis;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 kidney development and
CC epithelial morphogenesis. Involved in the regulation of microtubule
CC cytoskeleton organization. Is a negative regulator of microtubule
CC stability, acting through the control of MAP4 levels. Involved in
CC ciliogenesis (By similarity). {ECO:0000250|UniProtKB:Q149C2,
CC ECO:0000250|UniProtKB:Q8TDR0}.
CC -!- SUBUNIT: Component of the IFT complex B, at least composed of IFT20,
CC IFT22, HSPB11/IFT25, IFT27, IFT46, IFT52, TRAF3IP1/IFT54, IFT57, IFT74,
CC IFT80, IFT81, and IFT88. Interacts with IFT88 (By similarity).
CC Interacts with IL13RA1. Binds to microtubules, TRAF3 and DISC1 (By
CC similarity). Interacts with MAP4 (By similarity).
CC {ECO:0000250|UniProtKB:Q149C2, ECO:0000250|UniProtKB:Q8TDR0}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q8TDR0}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q8TDR0}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q149C2}. Cytoplasm, cytoskeleton, cilium basal
CC body {ECO:0000250|UniProtKB:Q149C2}. 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 -!- SIMILARITY: Belongs to the TRAF3IP1 family. {ECO:0000305}.
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DR EMBL; BC083645; AAH83645.1; -; mRNA.
DR RefSeq; NP_001012204.1; NM_001012204.1.
DR AlphaFoldDB; Q5XIN3; -.
DR SMR; Q5XIN3; -.
DR STRING; 10116.ENSRNOP00000053451; -.
DR iPTMnet; Q5XIN3; -.
DR PhosphoSitePlus; Q5XIN3; -.
DR PaxDb; Q5XIN3; -.
DR PRIDE; Q5XIN3; -.
DR Ensembl; ENSRNOT00000056612; ENSRNOP00000053451; ENSRNOG00000024468.
DR GeneID; 363286; -.
DR KEGG; rno:363286; -.
DR UCSC; RGD:1309252; rat.
DR CTD; 26146; -.
DR RGD; 1309252; Traf3ip1.
DR eggNOG; KOG3809; Eukaryota.
DR GeneTree; ENSGT00720000108822; -.
DR HOGENOM; CLU_023216_0_0_1; -.
DR InParanoid; Q5XIN3; -.
DR PhylomeDB; Q5XIN3; -.
DR Reactome; R-RNO-5620924; Intraflagellar transport.
DR PRO; PR:Q5XIN3; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000024468; Expressed in testis and 18 other tissues.
DR ExpressionAtlas; Q5XIN3; baseline and differential.
DR GO; GO:0005930; C:axoneme; ISO:RGD.
DR GO; GO:0005813; C:centrosome; ISO:RGD.
DR GO; GO:0036064; C:ciliary basal body; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030992; C:intraciliary transport particle B; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IEA:InterPro.
DR GO; GO:0060271; P:cilium assembly; ISO:RGD.
DR GO; GO:0031076; P:embryonic camera-type eye development; ISO:RGD.
DR GO; GO:0042733; P:embryonic digit morphogenesis; ISO:RGD.
DR GO; GO:0035050; P:embryonic heart tube development; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0050687; P:negative regulation of defense response to virus; ISO:RGD.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0031333; P:negative regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:1901621; P:negative regulation of smoothened signaling pathway involved in dorsal/ventral neural tube patterning; ISO:RGD.
DR GO; GO:0032480; P:negative regulation of type I interferon production; ISO:RGD.
DR GO; GO:0021532; P:neural tube patterning; ISO:RGD.
DR GO; GO:0036342; P:post-anal tail morphogenesis; ISO:RGD.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; ISS:UniProtKB.
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 Cell projection; Cilium; Cilium biogenesis/degradation; Coiled coil;
KW Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..653
FT /note="TRAF3-interacting protein 1"
FT /id="PRO_0000299546"
FT REGION 1..306
FT /note="Abolishes microtubules binding when missing"
FT /evidence="ECO:0000250"
FT REGION 134..467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 229..653
FT /note="DISC1-interaction domain"
FT /evidence="ECO:0000250"
FT COILED 533..628
FT /evidence="ECO:0000255"
FT COMPBIAS 134..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..460
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 653 AA; 74114 MW; 3D9F9B9727F04351 CRC64;
MNAAVVRRTQ EALGKVIRRP PLTEKLLNKP PFRYLHDIIT EVIRITGFMK GLYTDAEMKS
DNVKDKDAKI SFLQKAIDVV MMVSGEPLAA KPARIVAGHE PERTNELLQL IGKCCLSKLS
SDEAVKRVLA GEKGDSRGRV LRTSKAQEPD NKSVKEEESR TQKEEKRSSE VKERSSSAEH
KQKEELKEDS KPREKERDKE KAKEADRDRH REPDRDRNRD GEREKARARA KQDRDRNNKD
RDRETERDRD RDRRSDGGKE KERQKDRDRD KGKDRERRKS KNGEHTRDPD REKSRDADKS
EKKADISVGA SKSSTLKASK RRSKNSLEGR KEDNISAKIL DSIVSGLNDE PDQETTAPEI
DDNSASLWRE NAEPEPAVKQ KGDSPSDAEG EAVPTSQDKL EVTENAEVSN ELPSSLRRIP
RPGSARPAPP RVKRQESTET LAGDRSGSGK TVSTVIIDSQ NSDNEDDEQF VVEAAPQLSE
IAEIEMVPSG DLEDEEKHGG LVKKILETKK DYEKLQQSPK PGEKERSLIF ESAWKKEKDI
VSKEIEKLRV SIQTLCKSAL PLGKIMDYIQ EDVDAMQNEL QLWHSENRQH AEALSKEQSI
TDSAVEPLKA ELSELEQQIK DQQDKICAVK ANILKNEEKI QKMVHSINLS SRR
