ID RFIP3_HUMAN Reviewed; 756 AA. AC O75154; B0QYI8; B0QYT8; B1AHQ0; B4DEI7; B4DZR6; Q4VXV7; Q7Z5E9; AC Q9H155; Q9H1G0; Q9NUI0; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 18-JUL-2018, entry version 164. DE RecName: Full=Rab11 family-interacting protein 3; DE Short=FIP3-Rab11; DE Short=Rab11-FIP3; DE AltName: Full=Arfophilin-1; DE AltName: Full=EF hands-containing Rab-interacting protein; DE Short=Eferin; DE AltName: Full=MU-MB-17.148; GN Name=RAB11FIP3; Synonyms=ARFO1, KIAA0665; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT and 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. RT The complete sequences of 100 new cDNA clones from brain which can RT code for large proteins in vitro."; RL DNA Res. 5:169-176(1998). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE RP SEQUENCE [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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., RA Higgs D.R.; RT "Sequence, structure and pathology of the fully annotated terminal 2 RT Mb of 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., RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., RA 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., RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., RA 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 RT project: 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., RA Kumar R., 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 RT 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 SUBCELLULAR LOCATION, INTERACTION WITH EXOC7; RAB11A AND ARF6, AND RP MUTAGENESIS OF ILE-738. RX PubMed=16148947; DOI=10.1038/sj.emboj.7600803; RA Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., RA Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W.; RT "Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control RT membrane traffic in cytokinesis."; RL EMBO J. 24:3389-3399(2005). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11A, AND RP MUTAGENESIS OF 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., RA Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R.; RT "The FIP3-Rab11 protein complex regulates recycling endosome targeting RT to the cleavage furrow during late cytokinesis."; RL Mol. Biol. Cell 16:849-860(2005). RN [13] RP 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., RA Sentz D., 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 RT Evi5 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., RA Khan A.R., 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 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 RT cell motility by modulating the actin cytoskeleton."; RL Eur. J. Cell Biol. 88:325-341(2009). RN [18] RP PHOSPHORYLATION AT SER-102; SER-281; SER-348; SER-488; SER-538; RP SER-647 AND 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., RA Yu X., 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 [19] 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 [20] 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 [21] RP X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 695-756 IN COMPLEX WITH RP RAB11A, 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 [22] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 715-756 IN COMPLEX WITH RP RAB11A, DOMAIN RBD-FIP, HOMODIMERIZATION, INTERACTION WITH RAB11A; RP ARF5 AND ARF6, AND MUTAGENESIS OF TYR-737; ASP-739; MET-746 AND RP 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 RT of Rab11-interacting protein 3 (FIP3)/Arfophilin-1."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006). CC -!- FUNCTION: Acts as a regulator of endocytic traffic by CC participating in membrane delivery. Required for the abcission CC step in cytokinesis, possibly by acting as an 'address tag' CC delivering recycling endosome membranes to the cleavage furrow CC during late cytokinesis. Also required for the structural CC integrity of the endosomal recycling compartment during CC interphase. May play a role in breast cancer cell motility by CC regulating actin cytoskeleton. Acts as an adapter protein linking CC the dynein motor complex to various cargos and converts dynein CC from a non-processive to a highly processive motor in the presence CC of dynactin. Facilitates the interaction between dynein and CC dynactin and activates dynein processivity (the ability to move CC along a microtubule for a long distance without falling off the CC track) (PubMed:25035494). {ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:17394487, ECO:0000269|PubMed:19327867, CC ECO:0000269|PubMed:25035494}. CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) CC and ARF6. Interacts with RAB11A; the interaction is direct. CC Interacts with RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6; CC according to PubMed:16148947, it specifically interacts with ARF6 CC but not ARF5. Interacts with ARF6; according to PubMed:17030804 CC but not PubMed:16148947. Interacts with RACGAP1/MgcRacGAP; CC interaction takes place during late stage of cytokinesis and is CC required for recruitment to the midbody. Interacts with ASAP1 and CC EXOC7. Interacts with dynein intermediate chain and dynactin CC (DCTN1) (PubMed:25035494). {ECO:0000269|PubMed:11495908, CC ECO:0000269|PubMed:12470645, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:16148947, ECO:0000269|PubMed:17007872, CC ECO:0000269|PubMed:17030804, ECO:0000269|PubMed:17229837, CC ECO:0000269|PubMed:17628206, ECO:0000269|PubMed:18511905, CC ECO:0000269|PubMed:25035494}. CC -!- INTERACTION: CC P18085:ARF4; NbExp=2; IntAct=EBI-15605207, EBI-1237085; CC P62491:RAB11A; NbExp=16; IntAct=EBI-15605207, EBI-745098; CC Q96QF0-2:RAB3IP; NbExp=6; IntAct=EBI-15605207, EBI-747865; CC Q9H0H5:RACGAP1; NbExp=7; IntAct=EBI-7942186, EBI-717233; CC -!- SUBCELLULAR LOCATION: Recycling endosome membrane CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17394487}; CC Peripheral membrane protein. Cytoplasm, cytoskeleton, microtubule CC organizing center, centrosome {ECO:0000269|PubMed:15158446, CC ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:17394487, CC ECO:0000269|PubMed:18511905}. Cleavage furrow CC {ECO:0000269|PubMed:15158446, ECO:0000269|PubMed:15601896}. CC Midbody {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:18511905}. Note=In early mitosis remains CC diffuse and distributed through the cell. The onset of anaphase CC sequesters these vesicles to the centrosomes at the opposite poles CC of the cell. During telophase these vesicles move from the CC centrosomes, to the furrow, and then to the midbody to aid in CC abscission (PubMed:15158446, PubMed:15601896, PubMed:18511905). CC Interaction with Rab11 mediates localization to endosomes CC (PubMed:11495908). Interaction with ARF6 mediates localization to CC the midbody (PubMed:16148947). {ECO:0000269|PubMed:11495908, CC ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:18511905}. 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 Note=No experimental confirmation available.; CC Name=3; CC IsoId=O75154-3; Sequence=VSP_038666; CC Note=No experimental confirmation available.; CC -!- DOMAIN: The RBD-FIP domain mediates the interaction with Rab11 CC (RAB11A 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 -!- SEQUENCE CAUTION: CC Sequence=BAA31640.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=BAG57098.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAQ09358.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAQ09642.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305}; CC Sequence=CAQ11003.1; Type=Erroneous gene model prediction; 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; CAI95593.1; -; Genomic_DNA. DR EMBL; AL049542; CAI95593.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAI95593.1; JOINED; Genomic_DNA. DR EMBL; AL049542; CAI95788.1; -; Genomic_DNA. DR EMBL; AL023881; CAI95788.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAI95788.1; JOINED; Genomic_DNA. DR EMBL; AL023881; CAQ11003.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL049542; CAQ11003.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAQ11003.1; JOINED; Genomic_DNA. DR EMBL; AL049542; CAQ09358.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL023881; CAQ09358.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAQ09358.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAQ09642.1; ALT_SEQ; Genomic_DNA. DR EMBL; AL023881; CAQ09642.1; JOINED; Genomic_DNA. DR EMBL; AL049542; CAQ09642.1; JOINED; Genomic_DNA. DR EMBL; Z98882; CAI95591.1; -; Genomic_DNA. DR EMBL; AL023881; CAI95591.1; JOINED; Genomic_DNA. DR EMBL; AL049542; CAI95591.1; JOINED; Genomic_DNA. DR EMBL; BC051360; AAH51360.1; -; mRNA. DR EMBL; AY130007; AAN05091.1; -; mRNA. DR CCDS; CCDS32351.1; -. [O75154-1] DR CCDS; CCDS45364.1; -. [O75154-2] DR PIR; T00367; T00367. DR RefSeq; NP_001135744.1; NM_001142272.1. [O75154-2] DR RefSeq; NP_055515.1; NM_014700.3. [O75154-1] DR RefSeq; XP_005255770.1; XM_005255713.3. [O75154-3] DR RefSeq; XP_005255772.1; XM_005255715.4. DR RefSeq; XP_011521066.1; XM_011522764.2. DR UniGene; Hs.531642; -. 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 ProteinModelPortal; O75154; -. DR SMR; O75154; -. DR BioGrid; 115076; 15. DR DIP; DIP-47494N; -. DR IntAct; O75154; 10. DR MINT; O75154; -. DR STRING; 9606.ENSP00000262305; -. DR iPTMnet; O75154; -. DR PhosphoSitePlus; O75154; -. DR BioMuta; RAB11FIP3; -. DR EPD; O75154; -. DR MaxQB; O75154; -. DR PaxDb; O75154; -. DR PeptideAtlas; O75154; -. DR PRIDE; O75154; -. DR ProteomicsDB; 49820; -. DR ProteomicsDB; 49821; -. [O75154-2] DR ProteomicsDB; 49822; -. [O75154-3] DR Ensembl; ENST00000262305; ENSP00000262305; ENSG00000090565. [O75154-1] DR Ensembl; ENST00000450428; ENSP00000415919; ENSG00000090565. [O75154-2] DR Ensembl; ENST00000610934; ENSP00000484620; ENSG00000275338. [O75154-2] DR Ensembl; ENST00000611004; ENSP00000482156; ENSG00000275338. [O75154-1] DR GeneID; 9727; -. DR KEGG; hsa:9727; -. DR UCSC; uc002chf.4; human. [O75154-1] DR CTD; 9727; -. DR DisGeNET; 9727; -. DR EuPathDB; HostDB:ENSG00000090565.15; -. DR GeneCards; RAB11FIP3; -. DR HGNC; HGNC:17224; RAB11FIP3. DR HPA; HPA028088; -. DR HPA; HPA028631; -. DR HPA; HPA030086; -. DR MIM; 608738; gene. DR neXtProt; NX_O75154; -. DR OpenTargets; ENSG00000090565; -. DR PharmGKB; PA134950896; -. DR eggNOG; KOG0982; Eukaryota. DR eggNOG; ENOG4111K32; LUCA. DR GeneTree; ENSGT00440000033742; -. DR HOVERGEN; HBG054059; -. DR InParanoid; O75154; -. DR KO; K12485; -. DR OMA; VQFATVY; -. DR OrthoDB; EOG091G0421; -. DR PhylomeDB; O75154; -. DR TreeFam; TF327221; -. DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium. DR ChiTaRS; RAB11FIP3; human. DR EvolutionaryTrace; O75154; -. DR GeneWiki; RAB11FIP3; -. DR GenomeRNAi; 9727; -. DR PRO; PR:O75154; -. DR Proteomes; UP000005640; Chromosome 16. DR Bgee; ENSG00000090565; -. DR CleanEx; HS_RAB11FIP3; -. DR ExpressionAtlas; O75154; baseline and differential. DR Genevisible; O75154; HS. 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:0005768; C:endosome; 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:0005815; C:microtubule organizing center; IDA:HPA. DR GO; GO:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB. DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030306; F:ADP-ribosylation factor binding; IPI:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0051959; F:dynein light intermediate chain binding; IPI:FlyBase. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0017137; F:Rab GTPase binding; IPI:UniProtKB. DR GO; GO:0000910; P:cytokinesis; IEA:InterPro. DR GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB. DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:CACAO. DR GO; GO:0032465; P:regulation of cytokinesis; IMP:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; TAS:UniProtKB. 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 InterPro; IPR032920; Rab11-FIP3. DR PANTHER; PTHR15726:SF6; PTHR15726:SF6; 2. DR Pfam; PF09457; RBD-FIP; 1. DR SUPFAM; SSF144270; SSF144270; 1. DR SUPFAM; SSF47473; SSF47473; 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; KW Cell division; Coiled coil; Complete proteome; Cytoplasm; KW Cytoskeleton; Endosome; Membrane; Metal-binding; Phosphoprotein; KW Reference proteome; Repeat; Transport. FT CHAIN 1 756 Rab11 family-interacting protein 3. FT /FTId=PRO_0000073879. FT DOMAIN 202 237 EF-hand 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 234 269 EF-hand 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT DOMAIN 694 756 FIP-RBD. {ECO:0000255|PROSITE- FT ProRule:PRU00844}. FT CA_BIND 215 226 1. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT CA_BIND 247 258 2. {ECO:0000255|PROSITE- FT ProRule:PRU00448}. FT REGION 484 588 ARF-binding domain (ABD). FT COILED 485 694 {ECO:0000255}. FT COMPBIAS 5 197 Pro-rich. FT COMPBIAS 148 151 Poly-Ser. FT COMPBIAS 366 369 Poly-Leu. FT MOD_RES 52 52 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 102 102 Phosphoserine; by CDK1. FT {ECO:0000244|PubMed:23186163, FT ECO:0000269|PubMed:22401586}. FT MOD_RES 281 281 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT MOD_RES 348 348 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT MOD_RES 488 488 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT MOD_RES 538 538 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT MOD_RES 647 647 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT MOD_RES 648 648 Phosphoserine. FT {ECO:0000269|PubMed:22401586}. FT VAR_SEQ 1 296 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038664. FT VAR_SEQ 297 301 FVTYE -> MPFLK (in isoform 2). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038665. FT VAR_SEQ 421 421 P -> PSTDPLAAKLHSILTDEAFEFYCSQCHKQINRLEDL FT SARLSDLEMN (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_038666. FT MUTAGEN 737 737 Y->S: Abolishes Rab11-binding. FT {ECO:0000269|PubMed:17030804}. FT MUTAGEN 738 738 I->E: Abolishes Rab11-binding. FT {ECO:0000269|PubMed:15601896, FT ECO:0000269|PubMed:16148947}. FT MUTAGEN 739 739 D->A: Abolishes Rab11-binding. FT {ECO:0000269|PubMed:17030804}. FT MUTAGEN 746 746 M->S: Abolishes Rab11-binding. FT {ECO:0000269|PubMed:17030804}. FT MUTAGEN 747 747 E->A: Abolishes Rab11-binding. FT {ECO:0000269|PubMed:17030804}. FT HELIX 704 709 {ECO:0000244|PDB:2HV8}. FT HELIX 717 746 {ECO:0000244|PDB:2D7C}. FT HELIX 750 753 {ECO:0000244|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 //