RFIP3_HUMAN
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};
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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
