ID RFIP3_HUMAN Reviewed; 756 AA. AC O75154; B0QYI8; B0QYT8; B1AHQ0; B4DEI7; B4DZR6; Q4VXV7; Q7Z5E9; Q9H155; AC Q9H1G0; Q9NUI0; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 29-MAY-2024, entry version 197. DE RecName: Full=Rab11 family-interacting protein 3 {ECO:0000303|PubMed:11495908}; DE Short=FIP3 {ECO:0000303|PubMed:31204173}; DE Short=FIP3-Rab11 {ECO:0000303|PubMed:15601896}; DE Short=Rab11-FIP3 {ECO:0000303|PubMed:11495908}; DE AltName: Full=Arfophilin-1 {ECO:0000303|PubMed:17030804}; DE AltName: Full=EF hands-containing Rab-interacting protein {ECO:0000303|PubMed:11481332}; DE Short=Eferin {ECO:0000303|PubMed:11481332}; DE AltName: Full=MU-MB-17.148; GN Name=RAB11FIP3 {ECO:0000312|HGNC:HGNC:17224}; Synonyms=ARFO1, KIAA0665; 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 1). RX PubMed=11481332; DOI=10.1074/jbc.m106133200; RA Prekeris R., Davies J.M., Scheller R.H.; RT "Identification of a novel Rab11/25 binding domain present in eferin and RT rip proteins."; RL J. Biol. Chem. 276:38966-38970(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9734811; DOI=10.1093/dnares/5.3.169; RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., RA Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. X. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE RP [LARGE SCALE MRNA] OF 311-756 (ISOFORM 3). RC TISSUE=Cerebellum, and Testis; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11157797; DOI=10.1093/hmg/10.4.339; RA Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., RA Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 Mb of RT the short arm of human chromosome 16."; RL Hum. Mol. Genet. 10:339-352(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15616553; DOI=10.1038/nature03187; RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M., RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., RA Myers R.M., Rubin E.M., Pennacchio L.A.; RT "The sequence and analysis of duplication-rich human chromosome 16."; RL Nature 432:988-994(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 532-756. RX PubMed=12800201; DOI=10.1002/ijc.11208; RA Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., RA Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., RA Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., RA Asmuss H.-P., Bise K., Mautner J.; RT "Novel tumor antigens identified by autologous antibody screening of RT childhood medulloblastoma cDNA libraries."; RL Int. J. Cancer 106:244-251(2003). RN [8] RP INTERACTION WITH RAB11A; RAB11B AND RAB25, AND SUBCELLULAR LOCATION. RX PubMed=11495908; DOI=10.1074/jbc.m104831200; RA Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., RA Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R.; RT "Identification and characterization of a family of Rab11-interacting RT proteins."; RL J. Biol. Chem. 276:39067-39075(2001). RN [9] RP INTERACTION WITH RAB11FIP4. RX PubMed=12470645; DOI=10.1016/s0006-291x(02)02720-1; RA Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W.; RT "Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its RT overexpression condenses the Rab11 positive compartment in HeLa cells."; RL Biochem. Biophys. Res. Commun. 299:770-779(2002). RN [10] RP SUBCELLULAR LOCATION. RX PubMed=15158446; DOI=10.1016/j.bbrc.2004.04.157; RA Horgan C.P., Walsh M., Zurawski T.H., McCaffrey M.W.; RT "Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment RT during interphase and to the cleavage furrow during cytokinesis."; RL Biochem. Biophys. Res. Commun. 319:83-94(2004). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EXOC7; RAB11A AND ARF6, RP MUTAGENESIS OF ILE-738, AND CAUTION. RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803; RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., RA Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.; RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane RT traffic in cytokinesis."; RL EMBO J. 24:3389-3399(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11A, AND MUTAGENESIS OF RP ILE-738. RX PubMed=15601896; DOI=10.1091/mbc.e04-10-0927; RA Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., RA Frey A.M., Peden A.A., Gould G.W., Prekeris R.; RT "The FIP3-Rab11 protein complex regulates recycling endosome targeting to RT the cleavage furrow during late cytokinesis."; RL Mol. Biol. Cell 16:849-860(2005). RN [13] RP FUNCTION, AND INTERACTION WITH RAB11A AND ARF6. RX PubMed=17628206; DOI=10.1016/j.ejcb.2007.05.004; RA Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D., RA Holmes R.K., Prekeris R.; RT "Molecular characterization of Rab11-FIP3 binding to ARF GTPases."; RL Eur. J. Cell Biol. 86:417-431(2007). RN [14] RP INTERACTION WITH RAB11A. RX PubMed=17229837; DOI=10.1073/pnas.0610500104; RA Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R., RA Scheller R.H., Jackson P.K., Eldridge A.G.; RT "Identification of Rab11 as a small GTPase binding protein for the Evi5 RT oncogene."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007). RN [15] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=17394487; DOI=10.1111/j.1600-0854.2007.00543.x; RA Horgan C.P., Oleksy A., Zhdanov A.V., Lall P.Y., White I.J., Khan A.R., RA Futter C.E., McCaffrey J.G., McCaffrey M.W.; RT "Rab11-FIP3 is critical for the structural integrity of the endosomal RT recycling compartment."; RL Traffic 8:414-430(2007). RN [16] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH RACGAP1. RX PubMed=18511905; DOI=10.1038/emboj.2008.112; RA Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., RA Gould G.W., Glotzer M., Prekeris R.; RT "Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow RT ingression and abscission during cytokinesis."; RL EMBO J. 27:1791-1803(2008). RN [17] RP FUNCTION. RX PubMed=19327867; DOI=10.1016/j.ejcb.2009.02.186; RA Jing J., Tarbutton E., Wilson G., Prekeris R.; RT "Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell RT motility by modulating the actin cytoskeleton."; RL Eur. J. Cell Biol. 88:325-341(2009). RN [18] RP FUNCTION, INTERACTION WITH DYNC1LI1, SUBCELLULAR LOCATION, REGION, AND RP MUTAGENESIS OF ILE-738. RX PubMed=20026645; DOI=10.1242/jcs.052670; RA Horgan C.P., Hanscom S.R., Jolly R.S., Futter C.E., McCaffrey M.W.; RT "Rab11-FIP3 links the Rab11 GTPase and cytoplasmic dynein to mediate RT transport to the endosomal-recycling compartment."; RL J. Cell Sci. 123:181-191(2010). RN [19] RP PHOSPHORYLATION AT SER-102; SER-281; SER-348; SER-488; SER-538; SER-647 AND RP SER-648. RX PubMed=22401586; DOI=10.1186/1471-2121-13-4; RA Collins L.L., Simon G., Matheson J., Wu C., Miller M.C., Otani T., Yu X., RA Hayashi S., Prekeris R., Gould G.W.; RT "Rab11-FIP3 is a cell cycle-regulated phosphoprotein."; RL BMC Cell Biol. 13:4-4(2012). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-102, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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 [21] RP FUNCTION, AND INTERACTION WITH DYNEIN INTERMEDIATE CHAIN AND DCTN1. RX PubMed=25035494; DOI=10.1126/science.1254198; RA McKenney R.J., Huynh W., Tanenbaum M.E., Bhabha G., Vale R.D.; RT "Activation of cytoplasmic dynein motility by dynactin-cargo adapter RT complexes."; RL Science 345:337-341(2014). RN [22] RP FUNCTION, INTERACTION WITH ARF4; RAB11A; RAB3IP; ASAP1 AND RHO, AND RP SUBCELLULAR LOCATION. RX PubMed=25673879; DOI=10.1242/jcs.162925; RA Wang J., Deretic D.; RT "The Arf and Rab11 effector FIP3 acts synergistically with ASAP1 to direct RT Rabin8 in ciliary receptor targeting."; RL J. Cell Sci. 128:1375-1385(2015). RN [23] RP FUNCTION, AND INTERACTION WITH RAB11A AND RAB3IP. RX PubMed=31204173; DOI=10.1016/j.devcel.2019.05.022; RA Walia V., Cuenca A., Vetter M., Insinna C., Perera S., Lu Q., Ritt D.A., RA Semler E., Specht S., Stauffer J., Morrison D.K., Lorentzen E., RA Westlake C.J.; RT "Akt Regulates a Rab11-Effector Switch Required for Ciliogenesis."; RL Dev. Cell 50:229-246(2019). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 695-756 IN COMPLEX WITH RAB11A, RP SUBCELLULAR LOCATION, AND HOMODIMERIZATION. RX PubMed=17007872; DOI=10.1016/j.jmb.2006.08.064; RA Eathiraj S., Mishra A., Prekeris R., Lambright D.G.; RT "Structural basis for Rab11-mediated recruitment of FIP3 to recycling RT endosomes."; RL J. Mol. Biol. 364:121-135(2006). RN [25] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 715-756 IN COMPLEX WITH RAB11A, RP DOMAIN RBD-FIP, HOMODIMERIZATION, INTERACTION WITH RAB11A; ARF5 AND ARF6, RP AND MUTAGENESIS OF TYR-737; ASP-739; MET-746 AND GLU-747. RX PubMed=17030804; DOI=10.1073/pnas.0605357103; RA Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., RA Wakatsuki S.; RT "Structural basis for Rab11-dependent membrane recruitment of a family of RT Rab11-interacting protein 3 (FIP3)/Arfophilin-1."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006). RN [26] {ECO:0007744|PDB:4UJ3, ECO:0007744|PDB:4UJ4} RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 695-756, IN COMPLEX WITH RAB11A RP AND RAB3IP, AND FUNCTION. RX PubMed=26258637; DOI=10.1038/nsmb.3065; RA Vetter M., Stehle R., Basquin C., Lorentzen E.; RT "Structure of Rab11-FIP3-Rabin8 reveals simultaneous binding of FIP3 and RT Rabin8 effectors to Rab11."; RL Nat. Struct. Mol. Biol. 22:695-702(2015). CC -!- FUNCTION: Downstream effector molecule for Rab11 GTPase which is CC involved in endocytic trafficking, cytokinesis and intracellular CC ciliogenesis by participating in membrane delivery (PubMed:15601896, CC PubMed:16148947, PubMed:17394487, PubMed:17628206, PubMed:18511905, CC PubMed:19327867, PubMed:20026645, PubMed:25673879, PubMed:26258637, CC PubMed:31204173). Recruited by Rab11 to endosomes where it links Rab11 CC to dynein motor complex (PubMed:20026645). The functional Rab11- CC RAB11FIP3-dynein complex regulates the movement of peripheral sorting CC endosomes (SE) along microtubule tracks toward the microtubule CC organizing center/centrosome, generating the endocytic recycling CC compartment (ERC) during interphase of cell cycle (PubMed:17394487, CC PubMed:20026645). Facilitates the interaction between dynein and CC dynactin and activates dynein processivity (PubMed:25035494). Binding CC with ASAP1 is needed to regulate the pericentrosomal localization of CC recycling endosomes (By similarity). The Rab11-RAB11FIP3 complex is CC also implicated in the transport during telophase of vesicles derived CC from recycling endosomes to the cleavage furrow via centrosome-anchored CC microtubules, where the vesicles function to deliver membrane during CC late cytokinesis and abscission (PubMed:15601896, PubMed:16148947). The CC recruitment of Rab11-RAB11FIP3-containing endosomes to the cleavage CC furrow and tethering to the midbody is co-mediated by RAB11FIP3 CC interaction with ARF6-exocyst and RACGAP1-MKLP1 tethering complexes CC (PubMed:17628206, PubMed:18511905). Also involved in the Rab11-Rabin8- CC Rab8 ciliogenesis cascade by facilitating the orderly assembly of a CC ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP, CC RAB11FIP3 and ARF4, which directs preciliary vesicle trafficking to CC mother centriole and ciliogenesis initiation (PubMed:26258637, CC PubMed:31204173). Also promotes the activity of Rab11 and ASAP1 in the CC ARF4-dependent Golgi-to-cilia transport of the sensory receptor CC rhodopsin (PubMed:25673879). Competes with WDR44 for binding to Rab11, CC which controls intracellular ciliogenesis pathway (PubMed:31204173). CC May play a role in breast cancer cell motility by regulating actin CC cytoskeleton (PubMed:19327867). {ECO:0000250|UniProtKB:Q8CHD8, CC ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:17628206, CC ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:19327867, CC ECO:0000269|PubMed:20026645, ECO:0000269|PubMed:25035494, CC ECO:0000269|PubMed:25673879, ECO:0000269|PubMed:26258637, CC ECO:0000269|PubMed:31204173}. CC -!- SUBUNIT: Homodimer (PubMed:17007872, PubMed:17030804). Interacts with CC RAB11A; the interaction is direct and is required for the recruitment CC to endosomes (PubMed:11495908, PubMed:15601896, PubMed:17030804, CC PubMed:17229837, PubMed:31204173). Interacts with RAB11B CC (PubMed:11495908). Forms a ternary complex with RAB11A and dynein CC intermediate chain DYNC1LI1; RAB11FIP3 links RAB11A to dynein and the CC interaction regulates endocytic trafficking (PubMed:20026645). CC Interacts with dynein intermediate chain and dynactin (DCTN1); the CC interaction activates dynein processivity (PubMed:25035494). Interacts CC with ARF6 and EXOC7; the interaction serves for recruitment and CC tethering of recycling endosomes-derived vesicles to the cleavage CC furrow/midbody (PubMed:16148947, PubMed:17030804, PubMed:17628206). CC Interacts with RACGAP1/MgcRacGAP; the interaction occurs at late CC telophase and is required for recruitment and tethering of recycling CC endosomes-derived vesicles to the cleavage furrow/midbody CC (PubMed:18511905). Forms a complex with RAB11A and Rabin8/RAB3IP, CC probably a heterohexamer with two of each protein subunit, where RAB3IP CC and RAB11FIP3 simultaneously bind to RAB11A; the complex promotes CC preciliary trafficking (PubMed:26258637, PubMed:31204173). Forms a CC complex containing RAB11A, ASAP1, RAB3IP, RAP11FIP3 and ARF4; the CC complex promotes preciliary trafficking; the complex binds to RHO in CC photoreceptor cells and promotes RHO ciliary transport CC (PubMed:25673879, PubMed:26258637). Interacts with RAB11FIP4 CC (PubMed:12470645). Interacts with RAB25 (PubMed:11495908). CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:12470645, CC ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17030804, CC ECO:0000269|PubMed:17229837, ECO:0000269|PubMed:17628206, CC ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:20026645, CC ECO:0000269|PubMed:25035494, ECO:0000269|PubMed:25673879, CC ECO:0000269|PubMed:26258637, ECO:0000269|PubMed:31204173}. CC -!- INTERACTION: CC O75154; Q9H0H5: RACGAP1; NbExp=7; IntAct=EBI-7942186, EBI-717233; CC O75154-1; P18085: ARF4; NbExp=2; IntAct=EBI-15605207, EBI-1237085; CC O75154-1; P62491: RAB11A; NbExp=16; IntAct=EBI-15605207, EBI-745098; CC O75154-1; Q96QF0-2: RAB3IP; NbExp=6; IntAct=EBI-15605207, EBI-747865; CC -!- SUBCELLULAR LOCATION: Endosome membrane. Recycling endosome membrane CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17394487, CC ECO:0000269|PubMed:20026645}; Peripheral membrane protein CC {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, CC centrosome {ECO:0000269|PubMed:15158446, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:18511905}. Cleavage CC furrow {ECO:0000269|PubMed:15158446, ECO:0000269|PubMed:15601896}. CC Midbody {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:18511905}. Golgi apparatus membrane CC {ECO:0000269|PubMed:25673879}; Peripheral membrane protein CC {ECO:0000305}. Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:25673879}; Peripheral membrane protein CC {ECO:0000305}. Note=During interphase, localized in vesicles CC continuously moving from peripheral sorting endosomes in the cell CC towards the pericentrosomal endosomal recycling compartment (ERC) CC (PubMed:17394487, PubMed:20026645). In early mitosis remains diffuse CC and distributed through the cell. The onset of anaphase sequesters CC these vesicles to the centrosomes at the opposite poles of the cell. CC During telophase these vesicles move from the centrosomes, to the CC furrow, and then to the midbody to aid in abscission (PubMed:15158446, CC PubMed:15601896, PubMed:18511905). Interaction with Rab11 mediates CC localization to endosomes (PubMed:11495908). Interaction with ARF6 CC mediates localization to the midbody (PubMed:16148947). Localized to CC the Golgi and TGN when interacting with RHO in photoreceptors CC (PubMed:25673879). Localized to rhodopsin transport carriers when CC interacting with RAB11A and ASAP1 in photoreceptors (PubMed:25673879). CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17394487, CC ECO:0000269|PubMed:18511905, ECO:0000269|PubMed:20026645, CC ECO:0000269|PubMed:25673879}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O75154-1; Sequence=Displayed; CC Name=2; CC IsoId=O75154-2; Sequence=VSP_038664, VSP_038665; CC Name=3; CC IsoId=O75154-3; Sequence=VSP_038666; CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 (RAB11A CC or RAB11B). {ECO:0000269|PubMed:17030804}. CC -!- PTM: Phosphorylated at Ser-102 by CDK1 during metaphase, and CC dephosphorylated as cells enter telophase. CC {ECO:0000269|PubMed:22401586}. CC -!- CAUTION: Was initially shown not to interact with ARF5 CC (PubMed:16148947). Another study later demonstrated the interaction CC (PubMed:17030804). {ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:17030804}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA31640.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG57098.1; Type=Erroneous initiation; Evidence={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; AF395731; AAL12940.1; -; mRNA. DR EMBL; AB014565; BAA31640.2; ALT_INIT; mRNA. DR EMBL; AK293644; BAG57098.1; ALT_INIT; mRNA. DR EMBL; AK303061; BAG64178.1; -; mRNA. DR EMBL; AE006463; AAK61232.1; -; Genomic_DNA. DR EMBL; AL023881; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL049542; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z98882; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC051360; AAH51360.1; -; mRNA. DR EMBL; AY130007; AAN05091.1; -; mRNA. DR CCDS; CCDS32351.1; -. [O75154-1] DR CCDS; CCDS92071.1; -. [O75154-3] DR PIR; T00367; T00367. DR RefSeq; NP_001135744.1; NM_001142272.1. DR RefSeq; NP_055515.1; NM_014700.3. [O75154-1] DR RefSeq; XP_005255770.1; XM_005255713.3. DR RefSeq; XP_005255772.1; XM_005255715.4. DR RefSeq; XP_011521066.1; XM_011522764.2. DR PDB; 2D7C; X-ray; 1.75 A; C/D=715-756. DR PDB; 2HV8; X-ray; 1.86 A; D/E/F=695-756. DR PDB; 4D0M; X-ray; 6.00 A; E/F/K/L/U/V/a/b/e/f/i/j=713-756. DR PDB; 4UJ3; X-ray; 3.00 A; C/F/I/L/O/R/U/X=695-756. DR PDB; 4UJ4; X-ray; 4.20 A; C/F/I/L=695-756. DR PDBsum; 2D7C; -. DR PDBsum; 2HV8; -. DR PDBsum; 4D0M; -. DR PDBsum; 4UJ3; -. DR PDBsum; 4UJ4; -. DR AlphaFoldDB; O75154; -. DR SMR; O75154; -. DR BioGRID; 115076; 22. DR DIP; DIP-47494N; -. DR IntAct; O75154; 11. DR MINT; O75154; -. DR STRING; 9606.ENSP00000262305; -. DR iPTMnet; O75154; -. DR PhosphoSitePlus; O75154; -. DR BioMuta; RAB11FIP3; -. DR EPD; O75154; -. DR jPOST; O75154; -. DR MassIVE; O75154; -. DR MaxQB; O75154; -. DR PaxDb; 9606-ENSP00000262305; -. DR PeptideAtlas; O75154; -. DR ProteomicsDB; 49820; -. [O75154-1] DR ProteomicsDB; 49821; -. [O75154-2] DR ProteomicsDB; 49822; -. [O75154-3] DR Antibodypedia; 22705; 108 antibodies from 25 providers. DR DNASU; 9727; -. DR Ensembl; ENST00000262305.9; ENSP00000262305.4; ENSG00000090565.17. [O75154-1] DR Ensembl; ENST00000434585.6; ENSP00000399644.2; ENSG00000090565.17. [O75154-3] DR Ensembl; ENST00000450428.5; ENSP00000415919.1; ENSG00000090565.17. [O75154-2] DR Ensembl; ENST00000610934.1; ENSP00000484620.1; ENSG00000275338.4. [O75154-2] DR Ensembl; ENST00000611004.4; ENSP00000482156.1; ENSG00000275338.4. [O75154-1] DR GeneID; 9727; -. DR KEGG; hsa:9727; -. DR MANE-Select; ENST00000262305.9; ENSP00000262305.4; NM_014700.4; NP_055515.1. DR UCSC; uc002chf.4; human. [O75154-1] DR AGR; HGNC:17224; -. DR CTD; 9727; -. DR DisGeNET; 9727; -. DR GeneCards; RAB11FIP3; -. DR HGNC; HGNC:17224; RAB11FIP3. DR HPA; ENSG00000090565; Tissue enhanced (kidney). DR MIM; 608738; gene. DR neXtProt; NX_O75154; -. DR OpenTargets; ENSG00000090565; -. DR PharmGKB; PA134950896; -. DR VEuPathDB; HostDB:ENSG00000090565; -. DR eggNOG; KOG0982; Eukaryota. DR GeneTree; ENSGT00440000033742; -. DR HOGENOM; CLU_018925_2_0_1; -. DR InParanoid; O75154; -. DR OMA; XVTDSAY; -. DR OrthoDB; 5312348at2759; -. DR PhylomeDB; O75154; -. DR TreeFam; TF327221; -. DR PathwayCommons; O75154; -. DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium. DR SignaLink; O75154; -. DR SIGNOR; O75154; -. DR BioGRID-ORCS; 9727; 31 hits in 1171 CRISPR screens. DR ChiTaRS; RAB11FIP3; human. DR EvolutionaryTrace; O75154; -. DR GeneWiki; RAB11FIP3; -. DR GenomeRNAi; 9727; -. DR Pharos; O75154; Tbio. DR PRO; PR:O75154; -. DR Proteomes; UP000005640; Chromosome 16. DR RNAct; O75154; Protein. DR Bgee; ENSG00000090565; Expressed in kidney epithelium and 176 other cell types or tissues. DR ExpressionAtlas; O75154; baseline and differential. DR GO; GO:0034451; C:centriolar satellite; IDA:HPA. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0032154; C:cleavage furrow; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030139; C:endocytic vesicle; IBA:GO_Central. DR GO; GO:0030666; C:endocytic vesicle membrane; IDA:UniProtKB. DR GO; GO:0005768; C:endosome; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB. DR GO; GO:0045171; C:intercellular bridge; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0098944; C:postsynaptic recycling endosome membrane; IEA:Ensembl. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central. DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051959; F:dynein light intermediate chain binding; IMP:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB. DR GO; GO:0060090; F:molecular adaptor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl. DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:UniProt. DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0061502; P:early endosome to recycling endosome transport; IMP:UniProt. DR GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB. DR GO; GO:0043001; P:Golgi to plasma membrane protein transport; IMP:UniProt. DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:CACAO. DR GO; GO:0045724; P:positive regulation of cilium assembly; IDA:UniProt. DR GO; GO:1903438; P:positive regulation of mitotic cytokinetic process; IDA:UniProt. DR GO; GO:0061512; P:protein localization to cilium; IMP:UniProtKB. DR GO; GO:1905345; P:protein localization to cleavage furrow; IDA:UniProt. DR GO; GO:1902017; P:regulation of cilium assembly; IDA:UniProtKB. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:1902954; P:regulation of early endosome to recycling endosome transport; IMP:UniProtKB. DR GO; GO:2001135; P:regulation of endocytic recycling; IMP:UniProtKB. DR GO; GO:1904779; P:regulation of protein localization to centrosome; IMP:UniProtKB. DR GO; GO:0060627; P:regulation of vesicle-mediated transport; IMP:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IMP:UniProt. DR Gene3D; 1.20.5.2440; -; 1. DR Gene3D; 1.10.238.10; EF-hand; 1. DR InterPro; IPR011992; EF-hand-dom_pair. DR InterPro; IPR002048; EF_hand_dom. DR InterPro; IPR037245; FIP-RBD_C_sf. DR InterPro; IPR019018; Rab-bd_FIP-RBD. DR PANTHER; PTHR15726:SF6; RAB11 FAMILY-INTERACTING PROTEIN 3; 1. DR PANTHER; PTHR15726; RAB11-FAMILY INTERACTING PROTEIN; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF09457; RBD-FIP; 1. DR SUPFAM; SSF47473; EF-hand; 1. DR SUPFAM; SSF144270; Eferin C-derminal domain-like; 1. DR PROSITE; PS50222; EF_HAND_2; 2. DR PROSITE; PS51511; FIP_RBD; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Calcium; Cell cycle; Cell division; KW Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Golgi apparatus; Membrane; KW Metal-binding; Phosphoprotein; Reference proteome; Repeat; Transport. FT CHAIN 1..756 FT /note="Rab11 family-interacting protein 3" FT /id="PRO_0000073879" FT DOMAIN 202..237 FT /note="EF-hand 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 234..269 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 694..756 FT /note="FIP-RBD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00844" FT REGION 1..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2..435 FT /note="Important for binding to DYNC1LI1" FT /evidence="ECO:0000269|PubMed:20026645" FT REGION 484..588 FT /note="ARF-binding domain (ABD)" FT REGION 645..664 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 485..694 FT /evidence="ECO:0000255" FT COMPBIAS 1..24 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 80..97 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 181..196 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 215 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 217 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 219 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 226 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000305" FT BINDING 247 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 249 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT BINDING 258 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000305" FT MOD_RES 52 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 102 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:22401586, FT ECO:0007744|PubMed:23186163" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT MOD_RES 348 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT MOD_RES 488 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT MOD_RES 538 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT MOD_RES 647 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT MOD_RES 648 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:22401586" FT VAR_SEQ 1..296 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038664" FT VAR_SEQ 297..301 FT /note="FVTYE -> MPFLK (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038665" FT VAR_SEQ 421 FT /note="P -> PSTDPLAAKLHSILTDEAFEFYCSQCHKQINRLEDLSARLSDLEMN FT (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_038666" FT MUTAGEN 737 FT /note="Y->S: Abolishes Rab11-binding." FT /evidence="ECO:0000269|PubMed:17030804" FT MUTAGEN 738 FT /note="I->E: Abolishes Rab11-binding. Capable of binding to FT DYNC1LI1. Impaired trafficking towards the pericentrosomal FT endosomal recycling compartment (ERC)." FT /evidence="ECO:0000269|PubMed:15601896, FT ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:20026645" FT MUTAGEN 739 FT /note="D->A: Abolishes Rab11-binding." FT /evidence="ECO:0000269|PubMed:17030804" FT MUTAGEN 746 FT /note="M->S: Abolishes Rab11-binding." FT /evidence="ECO:0000269|PubMed:17030804" FT MUTAGEN 747 FT /note="E->A: Abolishes Rab11-binding." FT /evidence="ECO:0000269|PubMed:17030804" FT HELIX 704..709 FT /evidence="ECO:0007829|PDB:2HV8" FT HELIX 717..746 FT /evidence="ECO:0007829|PDB:2D7C" FT HELIX 750..753 FT /evidence="ECO:0007829|PDB:2D7C" SQ SEQUENCE 756 AA; 82440 MW; 264CEC399F28AFB9 CRC64; MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP QSPGLDEPAP GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL ASPDAPGPGP RSEAPLPELD PLFSWTEEPE ECGPASCPES APFRLQGSSS SHRARGEVDV FSPFPAPTAG ELALEQGPGS PPQPSDLSQT HPLPSEPVGS QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK DLTKYLDPSG LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV PSECLDAMEE PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE LSPETLCNGQ LGCSDPAFLT PSPTKRLSSK KVARYLHQSG ALTMEALEDP SPELMEGPEE DIADKVVFLE RRVLELEKDT AATGEQHSRL RQENLQLVHR ANALEEQLKE QELRACEMVL EETRRQKELL CKMEREKSIE IENLQTRLQQ LDEENSELRS CTPCLKANIE RLEEEKQKLL DEIESLTLRL SEEQENKRRM GDRLSHERHQ FQRDKEATQE LIEDLRKQLE HLQLLKLEAE QRRGRSSSMG LQEYHSRARE SELEQEVRRL KQDNRNLKEQ NEELNGQIIT LSIQGAKSLF STAFSESLAA EISSVSRDEL MEAIQKQEEI NFRLQDYIDR IIVAIMETNP SILEVK //