TRIP6_MOUSE
ID TRIP6_MOUSE Reviewed; 480 AA.
AC Q9Z1Y4; Q3TX74;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Thyroid receptor-interacting protein 6;
DE Short=TR-interacting protein 6;
DE Short=TRIP-6;
DE AltName: Full=Zyxin-related protein 1;
DE Short=ZRP-1;
GN Name=Trip6; Synonyms=Zrp1;
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=C3H/HeJ;
RX PubMed=10395914; DOI=10.1016/s0378-1119(99)00168-7;
RA Wang Y., Dooher J.E., Koedood Zhao M., Gilmore T.D.;
RT "Characterization of mouse Trip6: a putative intracellular signaling
RT protein.";
RL Gene 234:403-409(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH PDLIM4 AND PTPN13, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND MUTAGENESIS OF 479-ASP-CYS-480.
RC STRAIN=C57BL/6J;
RX PubMed=10826496; DOI=10.1078/s0171-9335(04)70031-x;
RA Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B., Hendriks W.;
RT "The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor
RT protein RIL and the protein tyrosine phosphatase PTP-BL.";
RL Eur. J. Cell Biol. 79:283-293(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=11239002; DOI=10.1093/nar/29.6.1352;
RA Wilson M.D., Riemer C., Martindale D.W., Schnupf P., Boright A.P.,
RA Cheung T.L., Hardy D.M., Schwartz S., Scherer S.W., Tsui L.-C., Miller W.,
RA Koop B.F.;
RT "Comparative analysis of the gene-dense ACHE/TFR2 region on human
RT chromosome 7q22 with the orthologous region on mouse chromosome 5.";
RL Nucleic Acids Res. 29:1352-1365(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
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 [5]
RP INTERACTION WITH S.TYPHIMURIUM SSEI.
RX PubMed=17095609; DOI=10.1073/pnas.0604054103;
RA Worley M.J., Nieman G.S., Geddes K., Heffron F.;
RT "Salmonella typhimurium disseminates within its host by manipulating the
RT motility of infected cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney;
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 [8]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-25; ARG-190; ARG-209 AND ARG-242,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Relays signals from the cell surface to the nucleus to weaken
CC adherens junction and promote actin cytoskeleton reorganization and
CC cell invasiveness. Involved in lysophosphatidic acid-induced cell
CC adhesion and migration. Acts as a transcriptional coactivator for NF-
CC kappa-B and JUN, and mediates the transrepression of these
CC transcription factors induced by glucocorticoid receptor (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Specifically interacts with the ligand binding domain of the
CC thyroid receptor (TR) in the presence of thyroid hormone (By
CC similarity). Interacts (via the third LIM domain and C-terminus) with
CC PTPN13 (via the second PDZ domain). Interacts (via the second LIM
CC domain or via the third LIM domain plus C-terminus) with PDLIM4 (via
CC PDZ domain). Found in a complex with PTPN13 and PDLIM4
CC (PubMed:10826496). Interacts with SVIL isoform 2. Interacts with LPAR2
CC but not other LPA receptors. Interacts with PRKAA2. Interacts with
CC MAGI1. Interacts with SCRIB (By similarity). In case of infection,
CC interacts with S.typhimurium protein sseI (PubMed:17095609).
CC {ECO:0000250|UniProtKB:Q15654, ECO:0000269|PubMed:10826496,
CC ECO:0000269|PubMed:17095609}.
CC -!- INTERACTION:
CC Q9Z1Y4; P70271: Pdlim4; NbExp=2; IntAct=EBI-643879, EBI-7288319;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q15654}. Cell junction, focal adhesion
CC {ECO:0000250|UniProtKB:Q15654}. Nucleus {ECO:0000250|UniProtKB:Q15654}.
CC Cytoplasm {ECO:0000250|UniProtKB:Q15654}. Note=Shuttles between nucleus
CC and cytoplasm. Colocalizes with actin. {ECO:0000250|UniProtKB:Q15654}.
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, stomach, lung, heart
CC and testis. Low expression levels in brain, colon, thymus, pancreas and
CC skin. Not expressed in skeletal muscle. {ECO:0000269|PubMed:10826496}.
CC -!- DEVELOPMENTAL STAGE: Expressed throughout development in all embryonic
CC stages analyzed, 10.5 days post coitum (dpc) to 18.5 dpc. In 16.5 dpc
CC embryos highly expressed in skin, lung, thymus, duodenum and the
CC ependymal cell layer surrounding the ventricles in brain. Highly
CC expressed also in the salivary glands, tongue, vibrissae, choroid
CC plexus, blood vessel walls, esophagus and midgut. Low expression levels
CC in spinal cord, heart and liver. {ECO:0000269|PubMed:10826496}.
CC -!- DOMAIN: The LIM zinc-binding domains mediate interaction with LPAR2.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation at Tyr-55 by SRC is required for enhancement of
CC lysophosphatidic acid-induced cell migration. Tyr-55 is
CC dephosphorylated by PTPN13 (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the zyxin/ajuba family. {ECO:0000305}.
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DR EMBL; AF116823; AAD45984.1; -; mRNA.
DR EMBL; AF097511; AAC72380.1; -; mRNA.
DR EMBL; AF312033; AAK28821.1; -; Genomic_DNA.
DR EMBL; AK010435; BAB26937.1; -; mRNA.
DR EMBL; AK159387; BAE35042.1; -; mRNA.
DR CCDS; CCDS19765.1; -.
DR RefSeq; NP_035769.1; NM_011639.3.
DR AlphaFoldDB; Q9Z1Y4; -.
DR SMR; Q9Z1Y4; -.
DR BioGRID; 204317; 5.
DR IntAct; Q9Z1Y4; 6.
DR MINT; Q9Z1Y4; -.
DR STRING; 10090.ENSMUSP00000024119; -.
DR iPTMnet; Q9Z1Y4; -.
DR PhosphoSitePlus; Q9Z1Y4; -.
DR MaxQB; Q9Z1Y4; -.
DR PaxDb; Q9Z1Y4; -.
DR PRIDE; Q9Z1Y4; -.
DR ProteomicsDB; 298228; -.
DR Antibodypedia; 16676; 410 antibodies from 38 providers.
DR DNASU; 22051; -.
DR Ensembl; ENSMUST00000024119; ENSMUSP00000024119; ENSMUSG00000023348.
DR GeneID; 22051; -.
DR KEGG; mmu:22051; -.
DR UCSC; uc009acd.1; mouse.
DR CTD; 7205; -.
DR MGI; MGI:1343458; Trip6.
DR VEuPathDB; HostDB:ENSMUSG00000023348; -.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000154273; -.
DR HOGENOM; CLU_001357_10_1_1; -.
DR InParanoid; Q9Z1Y4; -.
DR OMA; SMGYPPH; -.
DR OrthoDB; 483341at2759; -.
DR PhylomeDB; Q9Z1Y4; -.
DR TreeFam; TF320310; -.
DR BioGRID-ORCS; 22051; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Trip6; mouse.
DR PRO; PR:Q9Z1Y4; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9Z1Y4; protein.
DR Bgee; ENSMUSG00000023348; Expressed in external carotid artery and 211 other tissues.
DR ExpressionAtlas; Q9Z1Y4; baseline and differential.
DR Genevisible; Q9Z1Y4; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR GO; GO:0005149; F:interleukin-1 receptor binding; ISS:UniProtKB.
DR GO; GO:0019900; F:kinase binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0043009; P:chordate embryonic development; IEP:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cytoplasm; Cytoskeleton; LIM domain;
KW Metal-binding; Methylation; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Transcription; Transcription regulation; Zinc.
FT CHAIN 1..480
FT /note="Thyroid receptor-interacting protein 6"
FT /id="PRO_0000274689"
FT DOMAIN 281..339
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 341..401
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 404..471
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 57..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 473..480
FT /note="Interaction with MAGI1 and PTPN13"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 25
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 55
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19131326"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 183
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 190
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 193
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 209
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 242
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MUTAGEN 479..480
FT /note="Missing: Interacts with PDLIM4. Loss of interaction
FT with PTPN13."
FT /evidence="ECO:0000269|PubMed:10826496"
FT CONFLICT 141
FT /note="G -> D (in Ref. 4; BAE35042)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 480 AA; 50934 MW; FA6C5A79D4834CF1 CRC64;
MSGPTWLPPK QPEPSRLPQG RSLPRGALGP PTAHGATLQP HPRVNFCPLP PEHCYQPPGV
PEDRGPTWVG SHGTPQRLQG LPPDRGIIRP GSLDAEIDSL TSMLADLDGG RSHAPRRPDR
QAFEAPPPHA YRGGSLKPSG GAVPTPMLPA SHYGGPTPAS YATASTPAGP AFPVQVKVAQ
PVRGCGLPRR GASQASGPLP GPHFPLTGRG EVWGAGYRSH REPGPGVPEG PSGVHIPAGG
GRGGGHEPQG PLGQPPEEEL ERLTKKLVHD MSHPPSGEYF GRCGGCGEDV VGDGAGVVAL
DRVFHIGCFV CSTCRAQLRG QHFYAVERRA YCESCYVATL EKCSTCSEPI LDRILRAMGK
AYHPGCFTCV VCHRGLDGIP FTVDATSQIH CIEDFHRKFA PRCSVCGGAI MPEPGQEETV
RIVALDRSFH IGCYKCEECG LLLSSEGECQ GCYPLDGHIL CKACSAWRIQ ELSATVTTDC
