ID CIP4_HUMAN Reviewed; 601 AA. AC Q15642; B2R8A6; B7WP22; D6W645; O15184; Q53G22; Q5TZN1; Q6FI24; Q8NFL1; AC Q8TCY1; Q8TDX3; Q96RJ1; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2006, sequence version 3. DT 02-OCT-2024, entry version 217. DE RecName: Full=Cdc42-interacting protein 4; DE AltName: Full=Protein Felic; DE AltName: Full=Salt tolerant protein; DE Short=hSTP; DE AltName: Full=Thyroid receptor-interacting protein 10; DE Short=TR-interacting protein 10; DE Short=TRIP-10; GN Name=TRIP10; Synonyms=CIP4, STOT, STP; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH CDC42, SUBCELLULAR RP LOCATION, AND TISSUE SPECIFICITY. RX 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 has a RT potential role in regulating the actin cytoskeleton."; RL Curr. Biol. 7:479-487(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), TISSUE SPECIFICITY, AND RP INDUCTION. RX PubMed=12054674; DOI=10.1016/s0006-291x(02)00398-4; RA Wang L., Rudert W.A., Grishin A., Dombrosky-Ferlan P., Sullivan K., RA Deng X., Whitcomb D., Corey S.J.; RT "Identification and genetic analysis of human and mouse activated Cdc42 RT interacting protein-4 isoforms."; RL Biochem. Biophys. Res. Commun. 293:1426-1430(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5), INTERACTION WITH CTNNB1, RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT TYROSINE RESIDUES. RC TISSUE=Renal cell carcinoma; RX PubMed=16343437; DOI=10.1016/j.bbrc.2005.11.117; RA Tsuji E., Tsuji Y., Fujiwara T., Ogata S., Tsukamoto K., Saku K.; RT "Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin- RT mediated cell-cell adhesion: expression and function in renal cell RT carcinoma."; RL Biochem. Biophys. Res. Commun. 339:1083-1088(2006). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Lung; RA Wang L., Rudert W.A., Sullivan K., Deng X., Corey S.J.; RT "Identification of a Cdc42-interacting protein 4 longer variant (Cip4L) RT which is differentially expressed in human tissues."; RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., RA Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., RA LaBaer J.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). 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 vector."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Small intestine; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Muscle; 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 [12] RP NUCLEOTIDE SEQUENCE [MRNA] OF 487-601 (ISOFORMS 1/2). RX PubMed=7776974; DOI=10.1210/mend.9.2.7776974; 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 of RT thyroid hormone for interaction with the thyroid hormone receptor."; RL Mol. Endocrinol. 9:243-254(1995). RN [13] RP TISSUE SPECIFICITY. RX PubMed=11294612; DOI=10.1023/a:1004132919896; RA Tsuji E., Tsuji Y.; RT "Molecular cloning and chromosomal localization of human salt-tolerant RT protein."; RL Genetica 108:259-262(2000). RN [14] RP INTERACTION WITH CDC42; MICROTUBULES AND WAS, SUBCELLULAR LOCATION, AND RP MUTAGENESIS OF ILE-454 AND LEU-468. RX PubMed=10713100; DOI=10.1074/jbc.275.11.7854; RA Tian L., Nelson D.L., Stewart D.M.; RT "Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich RT syndrome protein to microtubules."; RL J. Biol. Chem. 275:7854-7861(2000). RN [15] RP FUNCTION. RX PubMed=11069762; DOI=10.1242/jcs.113.23.4165; RA Linder S., Huefner K., Wintergerst U., Aepfelbacher M.; RT "Microtubule-dependent formation of podosomal adhesion structures in RT primary human macrophages."; RL J. Cell Sci. 113:4165-4176(2000). RN [16] RP INDUCTION. RX PubMed=11691828; RA Yuan R.-Q., Fan S., Achary M., Stewart D.M., Goldberg I.D., Rosen E.M.; RT "Altered gene expression pattern in cultured human breast cancer cells RT treated with hepatocyte growth factor/scatter factor in the setting of DNA RT damage."; RL Cancer Res. 61:8022-8031(2001). RN [17] RP INTERACTION WITH ARHGAP17, AND SUBCELLULAR LOCATION. RX PubMed=11431473; DOI=10.1074/jbc.m103540200; RA Richnau N., Aspenstroem P.; RT "Rich, a rho GTPase-activating protein domain-containing protein involved RT in signaling by Cdc42 and Rac1."; RL J. Biol. Chem. 276:35060-35070(2001). RN [18] RP INTERACTION WITH CDC42; LYN AND SRC, SUBCELLULAR LOCATION, TISSUE RP SPECIFICITY, AND PHOSPHORYLATION AT TYROSINE RESIDUES. RX PubMed=12456510; DOI=10.1182/blood-2002-03-0851; RA Dombrosky-Ferlan P., Grishin A., Botelho R.J., Sampson M., Wang L., RA Rudert W.A., Grinstein S., Corey S.J.; RT "Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, RT localizes to the phagocytic cup."; RL Blood 101:2804-2809(2003). RN [19] RP INTERACTION WITH HD, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=12604778; DOI=10.1073/pnas.0437967100; RA Holbert S., Dedeoglu A., Humbert S., Saudou F., Ferrante R.J., Neri C.; RT "Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and RT biological evidence for a role in Huntington's disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2712-2717(2003). RN [20] RP INTERACTION WITH AKAP9, SUBCELLULAR LOCATION, AND PHOSPHORYLATION. RX PubMed=15047863; DOI=10.1091/mbc.e03-10-0757; RA Larocca M.C., Shanks R.A., Tian L., Nelson D.L., Stewart D.M., RA Goldenring J.R.; RT "AKAP350 interaction with cdc42 interacting protein 4 at the Golgi RT apparatus."; RL Mol. Biol. Cell 15:2771-2781(2004). RN [21] RP FUNCTION, INTERACTION WITH DNM1 AND WASL, AND SUBCELLULAR LOCATION. RX PubMed=16326391; DOI=10.1016/j.devcel.2005.11.005; RA Itoh T., Erdmann K.S., Roux A., Habermann B., Werner H., De Camilli P.; RT "Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane RT invagination by BAR and F-BAR proteins."; RL Dev. Cell 9:791-804(2005). RN [22] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [23] RP FUNCTION, INTERACTION WITH FASLG, AND SUBCELLULAR LOCATION. RX PubMed=16318909; DOI=10.1016/j.cellsig.2005.10.015; RA Qian J., Chen W., Lettau M., Podda G., Zoernig M., Kabelitz D., Janssen O.; RT "Regulation of FasL expression: a SH3 domain containing protein family RT involved in the lysosomal association of FasL."; RL Cell. Signal. 18:1327-1337(2006). RN [24] RP INTERACTION WITH DAAM1; DIAPH1 AND DIAPH2, AND SUBCELLULAR LOCATION. RX PubMed=16630611; DOI=10.1016/j.yexcr.2006.03.013; RA Aspenstroem P., Richnau N., Johansson A.-S.; RT "The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA RT and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin RT dynamics."; RL Exp. Cell Res. 312:2180-2194(2006). RN [25] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299; SER-335 AND RP SER-351, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [27] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-335; SER-351 AND RP SER-482, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296; SER-299 AND SER-482, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296 AND SER-298, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [32] RP STRUCTURE BY NMR OF 543-599. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of the CDC42-interacting protein 4."; RL Submitted (NOV-2005) to the PDB data bank. RN [33] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 10-303, DOMAIN F-BAR, COILED-COIL RP DOMAIN, AND SUBUNIT. RX PubMed=17512409; DOI=10.1016/j.cell.2007.03.040; RA Shimada A., Niwa H., Tsujita K., Suetsugu S., Nitta K., Hanawa-Suetsugu K., RA Akasaka R., Nishino Y., Toyama M., Chen L., Liu Z.-J., Wang B.C., RA Yamamoto M., Terada T., Miyazawa A., Tanaka A., Sugano S., Shirouzu M., RA Nagayama K., Takenawa T., Yokoyama S.; RT "Curved EFC/F-BAR-domain dimers are joined end to end into a filament for RT membrane invagination in endocytosis."; RL Cell 129:761-772(2007). RN [34] RP STRUCTURE BY NMR OF 388-481, AND COILED-COIL DOMAIN. RX PubMed=19387844; DOI=10.1007/s10858-009-9317-z; RA Kobashigawa Y., Kumeta H., Kanoh D., Inagaki F.; RT "The NMR structure of the TC10- and Cdc42-interacting domain of CIP4."; RL J. Biomol. NMR 44:113-118(2009). CC -!- FUNCTION: Required for translocation of GLUT4 to the plasma membrane in CC response to insulin signaling (By similarity). Required to coordinate CC membrane tubulation with reorganization of the actin cytoskeleton CC during endocytosis. Binds to lipids such as phosphatidylinositol 4,5- CC bisphosphate and phosphatidylserine and promotes membrane invagination CC and the formation of tubules. Also promotes CDC42-induced actin CC polymerization by recruiting WASL/N-WASP which in turn activates the CC Arp2/3 complex. Actin polymerization may promote the fission of CC membrane tubules to form endocytic vesicles. Required for the formation CC of podosomes, actin-rich adhesion structures specific to monocyte- CC derived cells. May be required for the lysosomal retention of CC FASLG/FASL. {ECO:0000250, ECO:0000269|PubMed:11069762, CC ECO:0000269|PubMed:16318909, ECO:0000269|PubMed:16326391}. CC -!- SUBUNIT: Interacts specifically with GTP-bound RHOQ. Interacts with CC DNM2 and PDE6G (By similarity). Homodimerizes, the dimers can CC polymerize end-to-end to form filamentous structures. Interacts CC specifically with GTP-bound CDC42. Interacts with AKAP9, ARHGAP17, CC DAAM1, DIAPH1, DIAPH2, DNM1, FASLG/FASL, GAPVD1, LYN, microtubules, CC SRC, WAS/WASP and WASL/N-WASP. Interacts with the ligand binding domain CC of the thyroid receptor (TR) in the presence of thyroid hormone. May CC interact with CTNNB1 and HD/HTT. {ECO:0000250, CC ECO:0000269|PubMed:10713100, ECO:0000269|PubMed:11431473, CC ECO:0000269|PubMed:12456510, ECO:0000269|PubMed:12604778, CC ECO:0000269|PubMed:15047863, ECO:0000269|PubMed:16318909, CC ECO:0000269|PubMed:16326391, ECO:0000269|PubMed:16343437, CC ECO:0000269|PubMed:16630611, ECO:0000269|PubMed:17512409, CC ECO:0000269|PubMed:9210375}. CC -!- INTERACTION: CC Q15642; P78325: ADAM8; NbExp=2; IntAct=EBI-739936, EBI-2625954; CC Q15642; Q1RLN5: ARHGAP12; NbExp=3; IntAct=EBI-739936, EBI-3959665; CC Q15642; Q68EM7: ARHGAP17; NbExp=3; IntAct=EBI-739936, EBI-1642807; CC Q15642; Q17R89-2: ARHGAP44; NbExp=3; IntAct=EBI-739936, EBI-10238335; CC Q15642; P48023: FASLG; NbExp=4; IntAct=EBI-739936, EBI-495538; CC Q15642; Q9H4E5: RHOJ; NbExp=3; IntAct=EBI-739936, EBI-6285694; CC Q15642; Q9Y3L3: SH3BP1; NbExp=3; IntAct=EBI-739936, EBI-346869; CC Q15642; Q969G3: SMARCE1; NbExp=3; IntAct=EBI-739936, EBI-455078; CC Q15642; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-739936, EBI-717399; CC Q15642; Q15642: TRIP10; NbExp=4; IntAct=EBI-739936, EBI-739936; CC Q15642; Q92558: WASF1; NbExp=3; IntAct=EBI-739936, EBI-1548747; CC Q15642-1; P97573: Inpp5d; Xeno; NbExp=2; IntAct=EBI-16191375, EBI-8008869; CC Q15642-2; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-6550597, EBI-11743294; CC Q15642-2; P42684-3: ABL2; NbExp=3; IntAct=EBI-6550597, EBI-10693977; CC Q15642-2; Q8IWW6-4: ARHGAP12; NbExp=3; IntAct=EBI-6550597, EBI-11959591; CC Q15642-2; Q68EM7: ARHGAP17; NbExp=3; IntAct=EBI-6550597, EBI-1642807; CC Q15642-2; Q9Y4D1: DAAM1; NbExp=2; IntAct=EBI-6550597, EBI-2817289; CC Q15642-2; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-6550597, EBI-2340258; CC Q15642-2; O43248: HOXC11; NbExp=3; IntAct=EBI-6550597, EBI-2652631; CC Q15642-2; P42858: HTT; NbExp=18; IntAct=EBI-6550597, EBI-466029; CC Q15642-2; O75564-2: JRK; NbExp=3; IntAct=EBI-6550597, EBI-17181882; CC Q15642-2; P50221: MEOX1; NbExp=3; IntAct=EBI-6550597, EBI-2864512; CC Q15642-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-6550597, EBI-16439278; CC Q15642-2; P52952: NKX2-5; NbExp=3; IntAct=EBI-6550597, EBI-936601; CC Q15642-2; P26367: PAX6; NbExp=3; IntAct=EBI-6550597, EBI-747278; CC Q15642-2; Q13671: RIN1; NbExp=3; IntAct=EBI-6550597, EBI-366017; CC Q15642-2; Q15428: SF3A2; NbExp=3; IntAct=EBI-6550597, EBI-2462271; CC Q15642-2; Q9Y3L3: SH3BP1; NbExp=3; IntAct=EBI-6550597, EBI-346869; CC Q15642-2; Q969G3: SMARCE1; NbExp=6; IntAct=EBI-6550597, EBI-455078; CC Q15642-2; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-6550597, EBI-741515; CC Q15642-2; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-6550597, EBI-6550597; CC Q15642-2; Q5T230: UTF1; NbExp=3; IntAct=EBI-6550597, EBI-12927594; CC Q15642-2; Q92558: WASF1; NbExp=3; IntAct=EBI-6550597, EBI-1548747; CC Q15642-2; O00401: WASL; NbExp=5; IntAct=EBI-6550597, EBI-957615; CC Q15642-2; O15156-2: ZBTB7B; NbExp=3; IntAct=EBI-6550597, EBI-11522250; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. CC Lysosome. Golgi apparatus. Cell membrane. Cell projection, phagocytic CC cup. Note=Translocates to the plasma membrane in response to insulin CC stimulation, and this may require active RHOQ (By similarity). CC Localizes to cortical regions coincident with F-actin, to lysosomes and CC to sites of phagocytosis in macrophages. Also localizes to the Golgi, CC and this requires AKAP9. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, perinuclear region. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; Synonyms=L; CC IsoId=Q15642-1; Sequence=Displayed; CC Name=2; Synonyms=A, W; CC IsoId=Q15642-2; Sequence=VSP_021716; CC Name=3; Synonyms=B; CC IsoId=Q15642-3; Sequence=VSP_021716, VSP_021721; CC Name=4; Synonyms=C; CC IsoId=Q15642-4; Sequence=VSP_021716, VSP_021719, VSP_021720; CC Name=5; Synonyms=V; CC IsoId=Q15642-5; Sequence=VSP_021717, VSP_021718; CC -!- TISSUE SPECIFICITY: Expressed in brain, colon, heart, kidney, liver, CC lung, megakaryocyte, ovary, pancreas, peripheral blood lymphocytes, CC placenta, prostate, skeletal muscle, small intestine, spleen, testis, CC thymus and trachea. {ECO:0000269|PubMed:11294612, CC ECO:0000269|PubMed:12054674, ECO:0000269|PubMed:12456510, CC ECO:0000269|PubMed:12604778, ECO:0000269|PubMed:9210375}. CC -!- INDUCTION: Induced by adriamycin treatment and this effect is CC counteracted by HGF/SF. Expression is reduced during differentiation. CC {ECO:0000269|PubMed:11691828, ECO:0000269|PubMed:12054674}. CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its CC concave surface. The end-to-end polymerization of dimers of these CC domains provides a curved surface that fits best membranes with around CC 600 A diameter, and may drive tubulation. CC {ECO:0000269|PubMed:17512409}. CC -!- PTM: Tyrosine phosphorylated. Also phosphorylated by PKA. CC {ECO:0000269|PubMed:12456510, ECO:0000269|PubMed:15047863, CC ECO:0000269|PubMed:16343437}. CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}. 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; AF380114; AAK77492.1; -; mRNA. DR EMBL; AY081141; AAL89588.1; -; mRNA. DR EMBL; AB072596; BAB88853.1; -; mRNA. DR EMBL; AF502289; AAM46851.1; -; mRNA. DR EMBL; CR536513; CAG38751.1; -; mRNA. DR EMBL; BT006698; AAP35344.1; -; mRNA. DR EMBL; BT020167; AAV38969.1; -; mRNA. DR EMBL; BT020171; AAV43773.1; -; mRNA. DR EMBL; AK223109; BAD96829.1; -; mRNA. DR EMBL; AK313296; BAG36103.1; -; mRNA. DR EMBL; AC008760; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW69065.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69062.1; -; Genomic_DNA. DR EMBL; CH471139; EAW69063.1; -; Genomic_DNA. DR EMBL; BC013002; AAH13002.1; -; mRNA. DR EMBL; L40379; AAC41729.1; -; mRNA. DR CCDS; CCDS12172.1; -. [Q15642-2] DR CCDS; CCDS74271.1; -. [Q15642-1] DR CCDS; CCDS74272.1; -. [Q15642-3] DR RefSeq; NP_001275891.1; NM_001288962.1. [Q15642-1] DR RefSeq; NP_001275892.1; NM_001288963.1. DR RefSeq; NP_004231.1; NM_004240.3. [Q15642-2] DR PDB; 2CT4; NMR; -; A=543-599. DR PDB; 2EFK; X-ray; 2.30 A; A=10-303. DR PDB; 2KE4; NMR; -; A=388-481. DR PDBsum; 2CT4; -. DR PDBsum; 2EFK; -. DR PDBsum; 2KE4; -. DR AlphaFoldDB; Q15642; -. DR BMRB; Q15642; -. DR SMR; Q15642; -. DR BioGRID; 114733; 127. DR DIP; DIP-39840N; -. DR IntAct; Q15642; 68. DR MINT; Q15642; -. DR STRING; 9606.ENSP00000320117; -. DR GlyGen; Q15642; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q15642; -. DR MetOSite; Q15642; -. DR PhosphoSitePlus; Q15642; -. DR BioMuta; TRIP10; -. DR DMDM; 118572632; -. DR jPOST; Q15642; -. DR MassIVE; Q15642; -. DR PaxDb; 9606-ENSP00000320117; -. DR PeptideAtlas; Q15642; -. DR ProteomicsDB; 60675; -. [Q15642-1] DR ProteomicsDB; 60676; -. [Q15642-2] DR ProteomicsDB; 60677; -. [Q15642-3] DR ProteomicsDB; 60678; -. [Q15642-4] DR ProteomicsDB; 60679; -. [Q15642-5] DR Pumba; Q15642; -. DR Antibodypedia; 11922; 312 antibodies from 34 providers. DR DNASU; 9322; -. DR Ensembl; ENST00000313244.14; ENSP00000320117.7; ENSG00000125733.18. [Q15642-1] DR Ensembl; ENST00000313285.12; ENSP00000320493.6; ENSG00000125733.18. [Q15642-2] DR GeneID; 9322; -. DR KEGG; hsa:9322; -. DR MANE-Select; ENST00000313244.14; ENSP00000320117.7; NM_001288962.2; NP_001275891.1. DR UCSC; uc002mfr.5; human. [Q15642-1] DR AGR; HGNC:12304; -. DR CTD; 9322; -. DR DisGeNET; 9322; -. DR GeneCards; TRIP10; -. DR HGNC; HGNC:12304; TRIP10. DR HPA; ENSG00000125733; Tissue enhanced (skeletal). DR MIM; 604504; gene. DR neXtProt; NX_Q15642; -. DR OpenTargets; ENSG00000125733; -. DR PharmGKB; PA36983; -. DR VEuPathDB; HostDB:ENSG00000125733; -. DR eggNOG; KOG3565; Eukaryota. DR GeneTree; ENSGT00950000183047; -. DR HOGENOM; CLU_023320_1_0_1; -. DR InParanoid; Q15642; -. DR OMA; CVAIYQF; -. DR OrthoDB; 2995634at2759; -. DR PhylomeDB; Q15642; -. DR TreeFam; TF351162; -. DR PathwayCommons; Q15642; -. DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis. DR Reactome; R-HSA-9013406; RHOQ GTPase cycle. DR SignaLink; Q15642; -. DR SIGNOR; Q15642; -. DR BioGRID-ORCS; 9322; 9 hits in 1154 CRISPR screens. DR ChiTaRS; TRIP10; human. DR EvolutionaryTrace; Q15642; -. DR GeneWiki; TRIP10; -. DR GenomeRNAi; 9322; -. DR Pharos; Q15642; Tbio. DR PRO; PR:Q15642; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q15642; protein. DR Bgee; ENSG00000125733; Expressed in lower esophagus mucosa and 177 other cell types or tissues. DR ExpressionAtlas; Q15642; baseline and differential. DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; NAS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0001891; C:phagocytic cup; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0007154; P:cell communication; NAS:UniProtKB. DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd07653; F-BAR_CIP4-like; 1. DR CDD; cd11628; HR1_CIP4_FNBP1L; 1. DR CDD; cd11911; SH3_CIP4-like; 1. DR DisProt; DP02473; -. DR Gene3D; 6.10.140.470; -; 1. DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR027267; AH/BAR_dom_sf. DR InterPro; IPR031160; F_BAR. DR InterPro; IPR001060; FCH_dom. DR InterPro; IPR011072; HR1_rho-bd. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR PANTHER; PTHR15735:SF17; CDC42-INTERACTING PROTEIN 4; 1. DR PANTHER; PTHR15735; FCH AND DOUBLE SH3 DOMAINS PROTEIN; 1. DR Pfam; PF00611; FCH; 1. DR Pfam; PF00018; SH3_1; 1. DR SMART; SM00055; FCH; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF103657; BAR/IMD domain-like; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS51741; F_BAR; 1. DR PROSITE; PS51860; REM_1; 1. DR PROSITE; PS50002; SH3; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cell membrane; Cell projection; KW Coiled coil; Cytoplasm; Cytoskeleton; Endocytosis; Golgi apparatus; KW Lipid-binding; Lysosome; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; SH3 domain. FT CHAIN 1..601 FT /note="Cdc42-interacting protein 4" FT /id="PRO_0000089766" FT DOMAIN 1..264 FT /note="F-BAR" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077" FT DOMAIN 393..470 FT /note="REM-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207" FT DOMAIN 540..601 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT REGION 1..117 FT /note="Required for podosome formation and interaction with FT AKAP9 and microtubules" FT /evidence="ECO:0000269|PubMed:15047863" FT REGION 1..117 FT /note="Required for translocation to the plasma membrane in FT response to insulin" FT /evidence="ECO:0000250" FT REGION 280..358 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 293..601 FT /note="Interaction with PDE6G" FT /evidence="ECO:0000250" FT REGION 293..537 FT /note="Interaction with CDC42" FT REGION 390..420 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 471..601 FT /note="Required for interaction with FASLG and localization FT to lysosomes" FT /evidence="ECO:0000269|PubMed:16318909" FT REGION 479..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 487..541 FT /note="Interaction with DNM2 and WASL" FT /evidence="ECO:0000250" FT REGION 529..601 FT /note="Interaction with DNM1 and WASL" FT /evidence="ECO:0000269|PubMed:16326391" FT REGION 538..601 FT /note="Required for podosome formation" FT REGION 544..601 FT /note="Interaction with WAS" FT /evidence="ECO:0000269|PubMed:10713100" FT REGION 546..601 FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2" FT /evidence="ECO:0000269|PubMed:11431473, FT ECO:0000269|PubMed:16630611" FT COILED 67..259 FT COILED 388..481 FT COMPBIAS 327..353 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 394..420 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 166 FT /note="Mediates end-to-end attachment of dimers" FT MOD_RES 296 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 298 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 299 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 335 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 351 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 482 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT VAR_SEQ 329..384 FT /note="Missing (in isoform 2, isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:12054674, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9210375, ECO:0000303|Ref.5, FT ECO:0000303|Ref.6, ECO:0000303|Ref.8" FT /id="VSP_021716" FT VAR_SEQ 330..341 FT /note="RPPPLSPLGGPV -> SRQPWDSGDRGF (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16343437" FT /id="VSP_021717" FT VAR_SEQ 342..601 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:16343437" FT /id="VSP_021718" FT VAR_SEQ 512 FT /note="S -> R (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12054674" FT /id="VSP_021719" FT VAR_SEQ 513..601 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:12054674" FT /id="VSP_021720" FT VAR_SEQ 553..601 FT /note="GSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTLN -> FT DLGPPPPPSQGPARALSLWPRVKTSVLWKKTKGTAGPGSGGKREARATCPPPTSESRSI FT EPCQRREEGGCRLLLLGHGGSQDLGTLFLTPWLRLRPV (in isoform 3)" FT /evidence="ECO:0000303|PubMed:12054674" FT /id="VSP_021721" FT MUTAGEN 454 FT /note="I->S: Abrogates interaction with CDC42." FT /evidence="ECO:0000269|PubMed:10713100" FT MUTAGEN 468 FT /note="L->S: Impairs interaction with CDC42." FT /evidence="ECO:0000269|PubMed:10713100" FT CONFLICT 158 FT /note="L -> P (in Ref. 2; AAK77492)" FT /evidence="ECO:0000305" FT CONFLICT 310 FT /note="L -> P (in Ref. 2; AAK77492)" FT /evidence="ECO:0000305" FT CONFLICT 419 FT /note="D -> G (in Ref. 8; BAD96829)" FT /evidence="ECO:0000305" FT CONFLICT 440 FT /note="P -> S (in Ref. 8; BAD96829)" FT /evidence="ECO:0000305" FT CONFLICT 473 FT /note="S -> R (in Ref. 2; AAK77492)" FT /evidence="ECO:0000305" FT CONFLICT 487..499 FT /note="ARPPDPPASAPPD -> KHPIICRLIHFSN (in Ref. 10; FT AAC41729)" FT /evidence="ECO:0000305" FT CONFLICT 553 FT /note="G -> W (in Ref. 5; CAG38751)" FT /evidence="ECO:0000305" FT HELIX 10..53 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 68..97 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 99..160 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 166..206 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 208..258 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 261..271 FT /evidence="ECO:0007829|PDB:2EFK" FT HELIX 273..275 FT /evidence="ECO:0007829|PDB:2EFK" FT STRAND 391..394 FT /evidence="ECO:0007829|PDB:2KE4" FT HELIX 396..421 FT /evidence="ECO:0007829|PDB:2KE4" FT HELIX 423..433 FT /evidence="ECO:0007829|PDB:2KE4" FT HELIX 435..437 FT /evidence="ECO:0007829|PDB:2KE4" FT HELIX 440..442 FT /evidence="ECO:0007829|PDB:2KE4" FT HELIX 444..477 FT /evidence="ECO:0007829|PDB:2KE4" FT STRAND 544..549 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 566..571 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 574..576 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 578..582 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 584..586 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 588..592 FT /evidence="ECO:0007829|PDB:2CT4" FT HELIX 593..595 FT /evidence="ECO:0007829|PDB:2CT4" FT STRAND 596..598 FT /evidence="ECO:0007829|PDB:2CT4" SQ SEQUENCE 601 AA; 68352 MW; A9BFE85520C7ABC5 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 WPFGKKNKPR PPPLSPLGGP VPSALPNGPP SPRSGRDPLA ILSEISKSVK PRLASFRSLR GSRGTVVTED FSHLPPEQQR KRLQQQLEER SRELQKEVDQ REALKKMKDV YEKTPQMGDP ASLEPQIAET LSNIERLKLE VQKYEAWLAE AESRVLSNRG DSLSRHARPP DPPASAPPDS SSNSASQDTK ESSEEPPSEE SQDTPIYTEF DEDFEEEPTS PIGHCVAIYH FEGSSEGTIS MAEGEDLSLM EEDKGDGWTR VRRKEGGEGY VPTSYLRVTL N //