CIP4_HUMAN
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 03-AUG-2022, entry version 205.
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}.
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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; 112.
DR DIP; DIP-39840N; -.
DR IntAct; Q15642; 54.
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 EPD; Q15642; -.
DR jPOST; Q15642; -.
DR MassIVE; Q15642; -.
DR MaxQB; Q15642; -.
DR PeptideAtlas; Q15642; -.
DR PRIDE; 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 Antibodypedia; 11922; 269 antibodies from 33 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 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; QERKTHF; -.
DR OrthoDB; 348563at2759; -.
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 1076 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 175 other tissues.
DR ExpressionAtlas; Q15642; baseline and differential.
DR Genevisible; Q15642; HS.
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 DisProt; DP02473; -.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR028498; CIP4.
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; PTHR15735:SF17; 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; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 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; Reference proteome;
KW 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
