O75154 (RFIP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab11 family-interacting protein 3
Short name=FIP3-Rab11
Short name=Rab11-FIP3

Alternative name(s):
Arfophilin-1
EF hands-containing Rab-interacting protein
Short name=Eferin
MU-MB-17.148

Gene names

Name:	RAB11FIP3
Synonyms:	ARFO1, KIAA0665

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	756 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a regulator of endocytic traffic by participating in membrane delivery. Required for the abcission step in cytokinesis, possibly by acting as an 'address tag' delivering recycling endosome membranes to the cleavage furrow during late cytokinesis. Also required for the structural integrity of the endosomal recycling compartment during interphase. May play a role in breast cancer cell motility by regulating actin cytoskeleton. Ref.12 Ref.15 Ref.17
Subunit structure	Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Interacts with RAB11B, RAB25 and RAB11FIP4. Interacts with ARF6; according to Ref.11, it specifically interacts with ARF6 but not ARF5. Interacts with ARF6; according to Ref.20 but not Ref.11. Interacts with RACGAP1/MgcRacGAP; interaction takes place during late stage of cytokinesis and is required for recruitment to the midbody. Interacts with ASAP1 and EXOC7. Ref.8 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.16 Ref.19 Ref.20
Subcellular location	Recycling endosome membrane; Peripheral membrane protein. Cytoplasm › cytoskeleton › centrosome. Cleavage furrow. Midbody. Note: In early mitosis remains diffuse and distributed through the cell. The onset of anaphase sequesters these vesicles to the centrosomes at the opposite poles of the cell. During telophase these vesicles move from the centrosomes, to the furrow, and then to the midbody to aid in abscission. Interaction with Rab11 mediates localization to endosomes. Interaction with ARF6 mediates localization to the midbody. Ref.8 Ref.10 Ref.11 Ref.12 Ref.15 Ref.16 Ref.19
Domain	The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B). Ref.20
Post-translational modification	Phosphorylated at Ser-102 by CDK1 during metaphase, and dephosphorylated as cells enter telophase. Ref.18
Sequence similarities	Contains 2 EF-hand domains. Contains 1 FIP-RBD domain.
Sequence caution	The sequence BAA31640.2 differs from that shown. Reason: Erroneous initiation. The sequence BAG57098.1 differs from that shown. Reason: Erroneous initiation. The sequence CAQ09358.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ09642.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAQ11003.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Cell cycle Cell division Transport
Cellular component	Cytoplasm Cytoskeleton Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
Ligand	Calcium Metal-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from mutant phenotype Ref.12Ref.11. Source: UniProtKB endocytic recycling Inferred from direct assay Ref.15. Source: UniProtKB
Cellular_component	centrosome Inferred from direct assay Ref.12. Source: UniProtKB cleavage furrow Inferred from direct assay Ref.12Ref.11Ref.16. Source: UniProtKB half bridge of spindle pole body Inferred from direct assay. Source: HPA midbody Inferred from direct assay Ref.12Ref.11Ref.16. Source: UniProtKB nucleus Inferred from direct assay. Source: HPA recycling endosome Inferred from direct assay Ref.15. Source: UniProtKB recycling endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Rab GTPase binding Non-traceable author statement Ref.1. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay Ref.20Ref.15. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75154-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: O75154-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-296: Missing.
     297-301: FVTYE → MPFLK

Note: No experimental confirmation available.

Isoform 3 (identifier: O75154-3)

The sequence of this isoform differs from the canonical sequence as follows:
     421-421: P → PSTDPLAAKLHSILTDEAFEFYCSQCHKQINRLEDLSARLSDLEMN

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 756

756

Rab11 family-interacting protein 3

PRO_0000073879

Regions

Domain

202 – 237

36

EF-hand 1

Domain

234 – 269

36

EF-hand 2

Domain

694 – 756

63

FIP-RBD

Calcium binding

215 – 226

12

1 Potential

Calcium binding

247 – 258

12

2 Potential

Region

484 – 588

105

ARF-binding domain (ABD)

Coiled coil

485 – 694

210

Potential

Compositional bias

5 – 197

193

Pro-rich

Compositional bias

148 – 151

4

Poly-Ser

Compositional bias

366 – 369

4

Poly-Leu

Amino acid modifications

Modified residue

102

1

Phosphoserine; by CDK1 Ref.18

Modified residue

281

1

Phosphoserine Ref.18

Modified residue

348

1

Phosphoserine Ref.18

Modified residue

488

1

Phosphoserine Ref.18

Modified residue

538

1

Phosphoserine Ref.18

Modified residue

647

1

Phosphoserine Ref.18

Modified residue

648

1

Phosphoserine Ref.18

Natural variations

Alternative sequence

1 – 296

296

Missing in isoform 2.

VSP_038664

Alternative sequence

297 – 301

5

FVTYE → MPFLK in isoform 2.

VSP_038665

Alternative sequence

421

1

P → PSTDPLAAKLHSILTDEAFE FYCSQCHKQINRLEDLSARL SDLEMN in isoform 3.

VSP_038666

Experimental info

Mutagenesis

737

1

Y → S: Abolishes Rab11-binding. Ref.20

Mutagenesis

738

1

I → E: Abolishes Rab11-binding. Ref.11 Ref.12

Mutagenesis

739

1

D → A: Abolishes Rab11-binding. Ref.20

Mutagenesis

746

1

M → S: Abolishes Rab11-binding. Ref.20

Mutagenesis

747

1

E → A: Abolishes Rab11-binding. Ref.20

Secondary structure

1

.

.

.

.

.

.

.

756

Helix Strand Turn

Details...

Helix

704 – 709

6

Helix

717 – 746

30

Helix

750 – 753

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 264CEC399F28AFB9	FASTA	756	82,440
	10 20 30 40 50 60 MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP QSPGLDEPAP 70 80 90 100 110 120 GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL ASPDAPGPGP RSEAPLPELD 130 140 150 160 170 180 PLFSWTEEPE ECGPASCPES APFRLQGSSS SHRARGEVDV FSPFPAPTAG ELALEQGPGS 190 200 210 220 230 240 PPQPSDLSQT HPLPSEPVGS QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK 250 260 270 280 290 300 DLTKYLDPSG LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY 310 320 330 340 350 360 EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV PSECLDAMEE 370 380 390 400 410 420 PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE LSPETLCNGQ LGCSDPAFLT 430 440 450 460 470 480 PSPTKRLSSK KVARYLHQSG ALTMEALEDP SPELMEGPEE DIADKVVFLE RRVLELEKDT 490 500 510 520 530 540 AATGEQHSRL RQENLQLVHR ANALEEQLKE QELRACEMVL EETRRQKELL CKMEREKSIE 550 560 570 580 590 600 IENLQTRLQQ LDEENSELRS CTPCLKANIE RLEEEKQKLL DEIESLTLRL SEEQENKRRM 610 620 630 640 650 660 GDRLSHERHQ FQRDKEATQE LIEDLRKQLE HLQLLKLEAE QRRGRSSSMG LQEYHSRARE 670 680 690 700 710 720 SELEQEVRRL KQDNRNLKEQ NEELNGQIIT LSIQGAKSLF STAFSESLAA EISSVSRDEL 730 740 750 MEAIQKQEEI NFRLQDYIDR IIVAIMETNP SILEVK
	Isoform 2 [UniParc]. Checksum: 574FC0A764FCA199	FASTA	460	52,451
	10 20 30 40 50 60 MPFLKANEVT DSAYMGSEST YSECETFTDE DTSTLVHPEL QPEGDADSAG GSAVPSECLD 70 80 90 100 110 120 AMEEPDHGAL LLLPGRPHPH GQSVITVIGG EEHFEDYGEG SEAELSPETL CNGQLGCSDP 130 140 150 160 170 180 AFLTPSPTKR LSSKKVARYL HQSGALTMEA LEDPSPELME GPEEDIADKV VFLERRVLEL 190 200 210 220 230 240 EKDTAATGEQ HSRLRQENLQ LVHRANALEE QLKEQELRAC EMVLEETRRQ KELLCKMERE 250 260 270 280 290 300 KSIEIENLQT RLQQLDEENS ELRSCTPCLK ANIERLEEEK QKLLDEIESL TLRLSEEQEN 310 320 330 340 350 360 KRRMGDRLSH ERHQFQRDKE ATQELIEDLR KQLEHLQLLK LEAEQRRGRS SSMGLQEYHS 370 380 390 400 410 420 RARESELEQE VRRLKQDNRN LKEQNEELNG QIITLSIQGA KSLFSTAFSE SLAAEISSVS 430 440 450 460 RDELMEAIQK QEEINFRLQD YIDRIIVAIM ETNPSILEVK
	Isoform 3 [UniParc]. Checksum: 4B4D2E7E868CF67B	FASTA	801	87,577
	10 20 30 40 50 60 MASAPPASPP GSEPPGPDPE PGGPDGPGAA QLAPGPAELR LGAPVGGPDP QSPGLDEPAP 70 80 90 100 110 120 GAAADGGARW SAGPAPGLEG GPRDPGPSAP PPRSGPRGQL ASPDAPGPGP RSEAPLPELD 130 140 150 160 170 180 PLFSWTEEPE ECGPASCPES APFRLQGSSS SHRARGEVDV FSPFPAPTAG ELALEQGPGS 190 200 210 220 230 240 PPQPSDLSQT HPLPSEPVGS QEDGPRLRAV FDALDGDGDG FVRIEDFIQF ATVYGAEQVK 250 260 270 280 290 300 DLTKYLDPSG LGVISFEDFY QGITAIRNGD PDGQCYGGVA SAQDEEPLAC PDEFDDFVTY 310 320 330 340 350 360 EANEVTDSAY MGSESTYSEC ETFTDEDTST LVHPELQPEG DADSAGGSAV PSECLDAMEE 370 380 390 400 410 420 PDHGALLLLP GRPHPHGQSV ITVIGGEEHF EDYGEGSEAE LSPETLCNGQ LGCSDPAFLT 430 440 450 460 470 480 PSTDPLAAKL HSILTDEAFE FYCSQCHKQI NRLEDLSARL SDLEMNSPTK RLSSKKVARY 490 500 510 520 530 540 LHQSGALTME ALEDPSPELM EGPEEDIADK VVFLERRVLE LEKDTAATGE QHSRLRQENL 550 560 570 580 590 600 QLVHRANALE EQLKEQELRA CEMVLEETRR QKELLCKMER EKSIEIENLQ TRLQQLDEEN 610 620 630 640 650 660 SELRSCTPCL KANIERLEEE KQKLLDEIES LTLRLSEEQE NKRRMGDRLS HERHQFQRDK 670 680 690 700 710 720 EATQELIEDL RKQLEHLQLL KLEAEQRRGR SSSMGLQEYH SRARESELEQ EVRRLKQDNR 730 740 750 760 770 780 NLKEQNEELN GQIITLSIQG AKSLFSTAFS ESLAAEISSV SRDELMEAIQ KQEEINFRLQ 790 800 DYIDRIIVAI METNPSILEV K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of a novel Rab11/25 binding domain present in eferin and rip proteins." Prekeris R., Davies J.M., Scheller R.H. J. Biol. Chem. 276:38966-38970(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 311-756 (ISOFORM 3). Tissue: Cerebellum and Testis.
[4]	"Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16." Daniels R.J., Peden J.F., Lloyd C., Horsley S.W., Clark K., Tufarelli C., Kearney L., Buckle V.J., Doggett N.A., Flint J., Higgs D.R. Hum. Mol. Genet. 10:339-352(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Ovary.
[7]	"Novel tumor antigens identified by autologous antibody screening of childhood medulloblastoma cDNA libraries." Behrends U., Schneider I., Roessler S., Frauenknecht H., Golbeck A., Lechner B., Eigenstetter G., Zobywalski C., Mueller-Weihrich S., Graubner U., Schmid I., Sackerer D., Spaeth M., Goetz C., Prantl F., Asmuss H.-P., Bise K., Mautner J. Int. J. Cancer 106:244-251(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 532-756.
[8]	"Identification and characterization of a family of Rab11-interacting proteins." Hales C.M., Griner R., Hobdy-Henderson K.C., Dorn M.C., Hardy D., Kumar R., Navarre J., Chan E.K.L., Lapierre L.A., Goldenring J.R. J. Biol. Chem. 276:39067-39075(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11A; RAB11B AND RAB25, SUBCELLULAR LOCATION.
[9]	"Rab11-FIP4 interacts with Rab11 in a GTP-dependent manner and its overexpression condenses the Rab11 positive compartment in HeLa cells." Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W. Biochem. Biophys. Res. Commun. 299:770-779(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11FIP4.
[10]	"Rab11-FIP3 localises to a Rab11-positive pericentrosomal compartment during interphase and to the cleavage furrow during cytokinesis." Horgan C.P., Walsh M., Zurawski T.H., McCaffrey M.W. Biochem. Biophys. Res. Commun. 319:83-94(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Rab11-FIP3 and FIP4 interact with Arf6 and the exocyst to control membrane traffic in cytokinesis." Fielding A.B., Schonteich E., Matheson J., Wilson G., Yu X., Hickson G.R., Srivastava S., Baldwin S.A., Prekeris R., Gould G.W. EMBO J. 24:3389-3399(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH EXOC7; RAB11A AND ARF6, MUTAGENESIS OF ILE-738.
[12]	"The FIP3-Rab11 protein complex regulates recycling endosome targeting to the cleavage furrow during late cytokinesis." Wilson G.M., Fielding A.B., Simon G.C., Yu X., Andrews P.D., Hames R.S., Frey A.M., Peden A.A., Gould G.W., Prekeris R. Mol. Biol. Cell 16:849-860(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RAB11A, MUTAGENESIS OF ILE-738.
[13]	"Molecular characterization of Rab11-FIP3 binding to ARF GTPases." Schonteich E., Pilli M., Simon G.C., Matern H.T., Junutula J.R., Sentz D., Holmes R.K., Prekeris R. Eur. J. Cell Biol. 86:417-431(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11A AND ARF6.
[14]	"Identification of Rab11 as a small GTPase binding protein for the Evi5 oncogene." Westlake C.J., Junutula J.R., Simon G.C., Pilli M., Prekeris R., Scheller R.H., Jackson P.K., Eldridge A.G. Proc. Natl. Acad. Sci. U.S.A. 104:1236-1241(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAB11A.
[15]	"Rab11-FIP3 is critical for the structural integrity of the endosomal recycling compartment." Horgan C.P., Oleksy A., Zhdanov A.V., Lall P.Y., White I.J., Khan A.R., Futter C.E., McCaffrey J.G., McCaffrey M.W. Traffic 8:414-430(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[16]	"Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis." Simon G.C., Schonteich E., Wu C.C., Piekny A., Ekiert D., Yu X., Gould G.W., Glotzer M., Prekeris R. EMBO J. 27:1791-1803(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH RACGAP1.
[17]	"Rab11-FIP3 is a Rab11-binding protein that regulates breast cancer cell motility by modulating the actin cytoskeleton." Jing J., Tarbutton E., Wilson G., Prekeris R. Eur. J. Cell Biol. 88:325-341(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Rab11-FIP3 is a cell cycle-regulated phosphoprotein." Collins L.L., Simon G., Matheson J., Wu C., Miller M.C., Otani T., Yu X., Hayashi S., Prekeris R., Gould G.W. BMC Cell Biol. 13:4-4(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-102; SER-281; SER-348; SER-488; SER-538; SER-647 AND SER-648.
[19]	"Structural basis for Rab11-mediated recruitment of FIP3 to recycling endosomes." Eathiraj S., Mishra A., Prekeris R., Lambright D.G. J. Mol. Biol. 364:121-135(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 695-756 IN COMPLEX WITH RAB11A, SUBCELLULAR LOCATION, HOMODIMERIZATION.
[20]	"Structural basis for Rab11-dependent membrane recruitment of a family of Rab11-interacting protein 3 (FIP3)/Arfophilin-1." Shiba T., Koga H., Shin H.-W., Kawasaki M., Kato R., Nakayama K., Wakatsuki S. Proc. Natl. Acad. Sci. U.S.A. 103:15416-15421(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 715-756 IN COMPLEX WITH RAB11A, DOMAIN RBD-FIP, HOMODIMERIZATION, INTERACTION WITH RAB11A; ARF5 AND ARF6, MUTAGENESIS OF TYR-737; ASP-739; MET-746 AND GLU-747.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF395731 mRNA. Translation: AAL12940.1.
AB014565 mRNA. Translation: BAA31640.2. Different initiation.
AK293644 mRNA. Translation: BAG57098.1. Different initiation.
AK303061 mRNA. Translation: BAG64178.1.
AE006463 Genomic DNA. Translation: AAK61232.1.
AL023881, AL049542, Z98882 Genomic DNA. Translation: CAI95593.1.
AL049542, AL023881, Z98882 Genomic DNA. Translation: CAI95788.1.
AL023881, AL049542, Z98882 Genomic DNA. Translation: CAQ11003.1. Sequence problems.
AL049542, AL023881, Z98882 Genomic DNA. Translation: CAQ09358.1. Sequence problems.
Z98882, AL023881, AL049542 Genomic DNA. Translation: CAQ09642.1. Sequence problems.
Z98882, AL023881, AL049542 Genomic DNA. Translation: CAI95591.1.
BC051360 mRNA. Translation: AAH51360.1.
AY130007 mRNA. Translation: AAN05091.1.

IPI

IPI00024426.
IPI00853085.
IPI00879102.

PIR

T00367.

RefSeq

NP_001135744.1. NM_001142272.1.
NP_055515.1. NM_014700.3.

UniGene

Hs.531642.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D7C	X-ray	1.75	C/D	715-756	[»]
2HV8	X-ray	1.86	D/E/F	695-756	[»]

ProteinModelPortal

O75154.

ModBase

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Protein-protein interaction databases

MINT

MINT-6799564.

STRING

9606.ENSP00000262305.

PTM databases

PhosphoSite

O75154.

Proteomic databases

PaxDb

O75154.

PRIDE

O75154.

Protocols and materials databases

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000262305; ENSP00000262305; ENSG00000090565.
ENST00000434585; ENSP00000399644; ENSG00000090565.
ENST00000450428; ENSP00000415919; ENSG00000090565.
ENST00000457159; ENSP00000398730; ENSG00000090565.

GeneID

9727.

KEGG

hsa:9727.

UCSC

uc002chf.3. human.
uc010uuf.2. human.
uc010uug.2. human.

Organism-specific databases

CTD

9727.

GeneCards

GC16P000475.

HGNC

HGNC:17224. RAB11FIP3.

HPA

HPA028088.
HPA028631.
HPA030086.

MIM

608738. gene.

neXtProt

NX_O75154.

PharmGKB

PA134950896.

HUGE

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GenAtlas

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Phylogenomic databases

eggNOG

NOG259959.

HOVERGEN

HBG054059.

InParanoid

O75154.

KO

K12485.

OMA

CYGGVAS.

OrthoDB

EOG4R23V0.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6downstreampathway. Arf6 downstream pathway.

Gene expression databases

ArrayExpress

O75154.

Bgee

O75154.

CleanEx

HS_RAB11FIP3.

Genevestigator

O75154.

GermOnline

ENSG00000090565. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR002048. EF_hand_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]

Pfam

PF13499. EF_hand_5. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]

SMART

SM00054. EFh. 2 hits.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. 2 hits.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

ProtoNet

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Other

ChiTaRS

RAB11FIP3. human.

EvolutionaryTrace

O75154.

GenomeRNAi

9727.

NextBio

36593.

SOURCE

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Entry information

Entry name

RFIP3_HUMAN

Accession

Primary (citable) accession number: O75154
Secondary accession number(s): B0QYI8 , B0QYT8, B1AHQ0, B4DEI7, B4DZR6, Q4VXV7, Q7Z5E9, Q9H155, Q9H1G0, Q9NUI0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 1, 1998
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.