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 03-AUG-2022, entry version 187. 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; 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 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., 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 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 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 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 [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 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 [22] 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). CC -!- FUNCTION: Acts as a regulator of endocytic traffic by participating in CC membrane delivery. Required for the abcission step in cytokinesis, CC possibly by acting as an 'address tag' delivering recycling endosome CC membranes to the cleavage furrow during late cytokinesis. Also required CC for the structural integrity of the endosomal recycling compartment CC during interphase. May play a role in breast cancer cell motility by CC regulating actin cytoskeleton. Acts as an adapter protein linking the CC dynein motor complex to various cargos and converts dynein from a non- CC processive to a highly processive motor in the presence of dynactin. CC Facilitates the interaction between dynein and dynactin and activates CC dynein processivity (the ability to move along a microtubule for a long CC distance without falling off the track) (PubMed:25035494). CC {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:17394487, CC ECO:0000269|PubMed:19327867, ECO:0000269|PubMed:25035494}. CC -!- SUBUNIT: Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and CC ARF6. Interacts with RAB11A; the interaction is direct. Interacts with CC RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6; according to CC PubMed:16148947, it specifically interacts with ARF6 but not ARF5. CC Interacts with ARF6; according to PubMed:17030804 but not CC PubMed:16148947. Interacts with RACGAP1/MgcRacGAP; interaction takes CC place during late stage of cytokinesis and is required for recruitment CC to the midbody. Interacts with ASAP1 and EXOC7. Interacts with dynein CC intermediate chain and dynactin (DCTN1) (PubMed:25035494). 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:25035494}. 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: Recycling endosome membrane CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:17007872, ECO:0000269|PubMed:17394487}; Peripheral CC membrane protein. Cytoplasm, cytoskeleton, microtubule organizing CC 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}. Midbody CC {ECO:0000269|PubMed:15601896, ECO:0000269|PubMed:16148947, CC ECO:0000269|PubMed:18511905}. Note=In early mitosis remains diffuse and CC distributed through the cell. The onset of anaphase sequesters these CC vesicles to the centrosomes at the opposite poles of the cell. During CC telophase these vesicles move from the centrosomes, to the furrow, and CC 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). CC {ECO:0000269|PubMed:11495908, ECO:0000269|PubMed:15601896, CC ECO:0000269|PubMed:16148947, 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 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 -!- 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 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; 19. 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; O75154; -. DR PeptideAtlas; O75154; -. DR PRIDE; O75154; -. DR ProteomicsDB; 49820; -. [O75154-1] DR ProteomicsDB; 49821; -. [O75154-2] DR ProteomicsDB; 49822; -. [O75154-3] DR Antibodypedia; 22705; 93 antibodies from 25 providers. DR DNASU; 9727; -. DR Ensembl; ENST00000262305.9; ENSP00000262305.4; ENSG00000090565.17. [O75154-1] 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 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; SQCHRQI; -. DR OrthoDB; 1419449at2759; -. DR PhylomeDB; O75154; -. DR TreeFam; TF327221; -. DR PathwayCommons; O75154; -. DR Reactome; R-HSA-5620916; VxPx cargo-targeting to cilium. DR SignaLink; O75154; -. DR BioGRID-ORCS; 9727; 15 hits in 1091 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 174 other tissues. DR ExpressionAtlas; O75154; baseline and differential. DR Genevisible; O75154; HS. 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: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:0030496; C:midbody; IDA:UniProtKB. DR GO; GO:0005739; C:mitochondrion; IDA:HPA. 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; IBA:GO_Central. 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:0031267; F:small GTPase binding; IPI:UniProtKB. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0032456; P:endocytic recycling; IDA:UniProtKB. DR GO; GO:0070164; P:negative regulation of adiponectin secretion; IDA:CACAO. DR GO; GO:0061512; P:protein localization to cilium; IEA:Ensembl. 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; 1. 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; Cell division; KW Coiled coil; Cytoplasm; Cytoskeleton; Endosome; Membrane; Metal-binding; KW 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 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." FT /evidence="ECO:0000269|PubMed:15601896, FT ECO:0000269|PubMed:16148947" 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 //