ID CIP4_HUMAN STANDARD; PRT; 545 AA. AC Q15642; O15184; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 28-FEB-2003 (Rel. 41, Last annotation update) DE Cdc42-interacting protein 4 (Thyroid receptor interacting protein 10) DE (TRIP-10). GN TRIP10 OR CIP4. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97362357; PubMed=9210375; RA Aspenstroem P.; RT "A Cdc42 target protein with homology to the non-kinase domain of FER RT has a potential role in regulating the actin cytoskeleton."; RL Curr. Biol. 7:479-487(1997). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Muscle; RA Strausberg R.; RL Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 431-545 FROM N.A. RX MEDLINE=95295737; PubMed=7776974; RA Lee J.W., Choi H.-S., Gyuris J., Brent R., Moore D.D.; RT "Two classes of proteins dependent on either the presence or absence RT of thyroid hormone for interaction with the thyroid hormone RT receptor."; RL Mol. Endocrinol. 9:243-254(1995). CC -!- FUNCTION: May act as a link between CDC42 signaling and regulation CC of the actin cytoskeleton. CC -!- SUBUNIT: SPECIFICALLY INTERACT WITH THE LIGAND BINDING DOMAIN OF CC THE THYROID RECEPTOR (TR). REQUIRES THE PRESENCE OF THYROID CC HORMONE FOR ITS INTERACTION. BINDS TO CDC42. CC -!- TISSUE SPECIFICITY: EXPRESSED MOST ABUNDANTLY IN SKELETAL MUSCLE, CC HEART AND placenta, present at lower levels in pancreas, lung, CC liver, and kidney, and barely detectable in brain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC -!- SIMILARITY: Contains 1 FCH domain. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AJ000414; CAA04062.1; -. DR EMBL; BC013002; AAH13002.1; -. DR EMBL; L40379; AAC41729.1; -. DR Genew; HGNC:12304; TRIP10. DR MIM; 604504; -. DR InterPro; IPR001060; Cdc15_Fes_CIP4. DR InterPro; IPR001452; SH3. DR Pfam; PF00018; SH3; 1. DR Pfam; PF00611; FCH; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS50133; FCH; 1. DR PROSITE; PS50002; SH3; 1. KW SH3 domain; Coiled coil. FT DOMAIN 1 65 FCH. FT DOMAIN 101 178 COILED COIL (POTENTIAL). FT DOMAIN 484 545 SH3. FT CONFLICT 431 443 ARPPDPPASAPPD -> KHPIICRLIHFSN (IN REF. FT 3). SQ SEQUENCE 545 AA; 62591 MW; 9C9D72EA734BC6E2 CRC64; MDWGTELWDQ FEVLERHTQW GLDLLDRYVK FVKERTEVEQ AYAKQLRSLV KKYLPKRPAK DDPESKFSQQ QSFVQILQEV NDFAGQRELV AENLSVRVCL ELTKYSQEMK QERKMHFQEG RRAQQQLENG FKQLENSKRK FERDCREAEK AAQTAERLDQ DINATKADVE KAKQQAHLRS HMAEESKNEY AAQLQRFNRD QAHFYFSQMP QIFDKLQDMD ERRATRLGAG YGLLSEAELE VVPIIAKCLE GMKVAANAVD PKNDSHVLIE LHKSGFARPG DVEFEDFSQP MNRAPSDSSL GTPSDGRPEL RGPGRSRTKR WPFGKKNKTV VTEDFSHLPP EQQRKRLQQQ LEERSRELQK EVDQREALKK MKDVYEKTPQ MGDPASLEPQ IAETLSNIER LKLEVQKYEA WLAEAESRVL SNRGDSLSRH ARPPDPPASA PPDSSSNSAS QDTKESSEEP PSEESQDTPI YTEFDEDFEE EPTSPIGHCV AIYHFEGSSE GTISMAEGED LSLMEEDKGD GWTRVRRKEG GEGYVPTSYL RVTLN //