ID CIP4_HUMAN STANDARD; PRT; 545 AA. AC Q15642; O15184; Q5TZN1; DT 01-NOV-1997 (Rel. 35, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 13-SEP-2005 (Rel. 48, Last annotation update) DE Cdc42-interacting protein 4 (Thyroid receptor-interacting protein 10) DE (TRIP-10). GN Name=TRIP10; Synonyms=CIP4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=97362357; PubMed=9210375; DOI=10.1016/S0960-9822(06)00219-3; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor RT vector."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Muscle; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 431-545. RX MEDLINE=95295737; PubMed=7776974; DOI=10.1210/me.9.2.243; 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 FCH domain. CC -!- SIMILARITY: Contains 1 SH3 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; -; mRNA. DR EMBL; BT006698; AAP35344.1; -; mRNA. DR EMBL; BT020167; AAV38969.1; -; mRNA. DR EMBL; BT020171; AAV43773.1; -; mRNA. DR EMBL; BC013002; AAH13002.1; -; mRNA. DR EMBL; L40379; AAC41729.1; -; mRNA. DR Ensembl; ENSG00000125733; Homo sapiens. DR HGNC; HGNC:12304; TRIP10. DR H-InvDB; HIX0014704; -. DR MIM; 604504; -. DR GO; GO:0005737; C:cytoplasm; NAS. DR GO; GO:0005515; F:protein binding; TAS. DR GO; GO:0030036; P:actin cytoskeleton organization and biogenesis; NAS. DR GO; GO:0007165; P:signal transduction; TAS. DR InterPro; IPR001060; Cdc15_Fes_CIP4. DR InterPro; IPR001452; SH3. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR PROSITE; PS50133; FCH; 1. DR PROSITE; PS50002; SH3; 1. KW Coiled coil; SH3 domain. FT DOMAIN 1 65 FCH. FT DOMAIN 484 545 SH3. FT COILED 101 178 Potential. FT CONFLICT 431 443 ARPPDPPASAPPD -> KHPIICRLIHFSN (in Ref. FT 4). SQ SEQUENCE 545 AA; 62592 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 //