TRIP6_BOVIN
ID TRIP6_BOVIN Reviewed; 481 AA.
AC Q3SX26;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Thyroid receptor-interacting protein 6;
DE Short=TR-interacting protein 6;
DE Short=TRIP-6;
GN Name=TRIP6;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC Interacts with SVIL isoform 2. Interacts with LPAR2 but not other LPA
CC receptors. Interacts with PRKAA2. Interacts with MAGI1. Interacts with
CC SCRIB (By similarity). {ECO:0000250|UniProtKB:Q15654,
CC ECO:0000250|UniProtKB:Q9Z1Y4}.
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 -!- 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; BC104544; AAI04545.1; -; mRNA.
DR RefSeq; NP_001030546.1; NM_001035469.1.
DR AlphaFoldDB; Q3SX26; -.
DR SMR; Q3SX26; -.
DR STRING; 9913.ENSBTAP00000001503; -.
DR PaxDb; Q3SX26; -.
DR PeptideAtlas; Q3SX26; -.
DR PRIDE; Q3SX26; -.
DR Ensembl; ENSBTAT00000001503; ENSBTAP00000001503; ENSBTAG00000024772.
DR GeneID; 615869; -.
DR KEGG; bta:615869; -.
DR CTD; 7205; -.
DR VEuPathDB; HostDB:ENSBTAG00000024772; -.
DR VGNC; VGNC:107000; TRIP6.
DR eggNOG; KOG1701; Eukaryota.
DR GeneTree; ENSGT00940000154273; -.
DR HOGENOM; CLU_001357_10_1_1; -.
DR InParanoid; Q3SX26; -.
DR OMA; SMGYPPH; -.
DR OrthoDB; 483341at2759; -.
DR TreeFam; TF320310; -.
DR Proteomes; UP000009136; Chromosome 25.
DR Bgee; ENSBTAG00000024772; Expressed in vas deferens and 100 other tissues.
DR ExpressionAtlas; Q3SX26; baseline.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
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; IEA:Ensembl.
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 2: Evidence at transcript 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..481
FT /note="Thyroid receptor-interacting protein 6"
FT /id="PRO_0000245358"
FT DOMAIN 284..321
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 344..403
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 404..472
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..481
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 COMPBIAS 141..156
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q9Z1Y4"
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:0000250|UniProtKB:Q15654"
FT MOD_RES 111
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 185
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 192
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 195
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 211
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 243
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q15654"
SQ SEQUENCE 481 AA; 50883 MW; 7E0A0BD8D673311D CRC64;
MSGPTWLPPK QPEPARAPQG RALPRGASGP PLAHGAALQP HPRVNFCPLP SEQCYQTPGE
PEDRGLAWVG CHGAPQHSQG LPPDRGGLRP GSLDAEIDSL TSMLAELDGG RGHAPRRPDR
QAYEPPEPPA YRSGSGPLRP NGGALPPPPL PGSPYGAPTP ASYATASTPA GPAFPVQVKV
ARPVRGCGPP RRGASQASGP SPGPHFPLPG RGEVWGAGYR SHREPGPGVK EEAPGVSGPA
GARGGGYGPQ VPLSQPPEEE LERLTKKLVH DMNHPPSGEY FGRCGGCGED VVGDGAGVVA
LDRVFHVGCF VCSTCRAQLR GQHFYAVERR AYCESCYVAT LEKCSTCSQP ILDRILRAMG
KAYHPGCFTC VVCHRGLDGI PFTVDATSQI HCIEDFHRKF APRCSVCGGA IMPEPGQEET
VRIVALDRSF HIGCYKCEEC GLLLSSEGEC QGCYPLDGHI LCKTCSAWRI QELSATVTTD
C
