Q86YS3 (RFIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Rab11 family-interacting protein 4
Short name=FIP4-Rab11
Short name=Rab11-FIP4

Alternative name(s):
Arfophilin-2

Gene names

Name:	RAB11FIP4
Synonyms:	ARFO2, KIAA1821

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	637 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. In case of infection by HCMV (human cytomegalovirus), may participate in egress of the virus out of nucleus; this function is independent of ARF6. Ref.1
Subunit structure	Homodimer. Forms a complex with Rab11 (RAB11A or RAB11B) and ARF6. Interacts with RAB11A; the interaction is direct. Forms a heterooligomeric complex with RAB11FIP2, RAB11FIP3 and RAB11FIP5. Interacts with HCMV (human cytomegalovirus) gM/UL100. Interacts with ECM29. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Midbody. Cytoplasmic vesicle. Note: Recruited to the cleavage furrow and the midbody during cytokinesis. Ref.8 Ref.9 Ref.10 Ref.12
Tissue specificity	Present at high level in testis (at protein level). Weakly expressed in other tissues. Ref.8
Domain	The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B) By similarity.
Sequence similarities	Contains 1 EF-hand domain. Contains 1 FIP-RBD domain.

Ontologies

Keywords
Biological process	Host-virus interaction Transport
Cellular component	Cytoplasmic vesicle Endosome Membrane
Coding sequence diversity	Alternative splicing
Domain	Coiled coil
Ligand	Calcium Metal-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cytokinesis Inferred from mutant phenotype Ref.9. Source: UniProtKB transport Inferred from electronic annotation. Source: UniProtKB-KW virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cleavage furrow Inferred from direct assay Ref.10Ref.9. Source: UniProtKB endocytic vesicle Inferred from direct assay Ref.12. Source: UniProtKB midbody Inferred from direct assay Ref.10Ref.9. Source: UniProtKB recycling endosome membrane Inferred from direct assay Ref.1. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro protein homodimerization activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q86YS3-1)

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: Q86YS3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-102: Missing.
     103-111: APEIPDCVE → MRTPPALGS

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 637	637	Rab11 family-interacting protein 4		PRO_0000073880
Regions
	Domain	49 – 84	36	EF-hand
	Domain	574 – 636	63	FIP-RBD
	Calcium binding	62 – 73	12	Potential
	Region	82 – 637	556	Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerization
	Coiled coil	280 – 617	338	Potential
Natural variations
	Alternative sequence	1 – 102	102	Missing in isoform 2.		VSP_013724
	Alternative sequence	103 – 111	9	APEIPDCVE → MRTPPALGS in isoform 2.		VSP_013725
Experimental info
	Mutagenesis	627	1	D → A: Abolishes Rab11-binding. Ref.9
	Sequence conflict	417	1	T → I in BAC05045. Ref.2
	Sequence conflict	518	1	E → G in BAC05045. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 8A5CDB9799383342	FASTA	637	71,928
	10 20 30 40 50 60 MAGGAGWSGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ GEEVEKLVKY 70 80 90 100 110 120 LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL PCAPEIPDCV EQGSEVTGPT 130 140 150 160 170 180 FADGELIPRE PGFFPEDEEE AMTLAPPEGP QELYTDSPME STQSLEGSVG SPAEKDGGLG 190 200 210 220 230 240 GLFLPEDKSL VHTPSMTTSD LSTHSTTSLI SNEEQFEDYG EGDDVDCAPS SPCPDDETRT 250 260 270 280 290 300 NVYSDLGSSV SSSAGQTPRK MRHVYNSELL DVYCSQCCKK INLLNDLEAR LKNLKANSPN 310 320 330 340 350 360 RKISSTAFGR QLMHSSNFSS SNGSTEDLFR DSIDSCDNDI TEKVSFLEKK VTELENDSLT 370 380 390 400 410 420 NGDLKSKLKQ ENTQLVHRVH ELEEMVKDQE TTAEQALEEE ARRHREAYGK LEREKATEVE 430 440 450 460 470 480 LLNARVQQLE EENTELRTTV TRLKSQTEKL DEERQRMSDR LEDTSLRLKD EMDLYKRMMD 490 500 510 520 530 540 KLRQNRLEFQ KEREATQELI EDLRKELEHL QMYKLDCERP GRGRSASSGL GEFNARAREV 550 560 570 580 590 600 ELEHEVKRLK QENYKLRDQN DDLNGQILSL SLYEAKNLFA AQTKAQSLAA EIDTASRDEL 610 620 630 MEALKEQEEI NFRLRQYMDK IILAILDHNP SILEIKH
	Isoform 2 [UniParc]. Checksum: 7ECB4806726B7D5D	FASTA	535	60,771
	10 20 30 40 50 60 MRTPPALGSQ GSEVTGPTFA DGELIPREPG FFPEDEEEAM TLAPPEGPQE LYTDSPMEST 70 80 90 100 110 120 QSLEGSVGSP AEKDGGLGGL FLPEDKSLVH TPSMTTSDLS THSTTSLISN EEQFEDYGEG 130 140 150 160 170 180 DDVDCAPSSP CPDDETRTNV YSDLGSSVSS SAGQTPRKMR HVYNSELLDV YCSQCCKKIN 190 200 210 220 230 240 LLNDLEARLK NLKANSPNRK ISSTAFGRQL MHSSNFSSSN GSTEDLFRDS IDSCDNDITE 250 260 270 280 290 300 KVSFLEKKVT ELENDSLTNG DLKSKLKQEN TQLVHRVHEL EEMVKDQETT AEQALEEEAR 310 320 330 340 350 360 RHREAYGKLE REKATEVELL NARVQQLEEE NTELRTTVTR LKSQTEKLDE ERQRMSDRLE 370 380 390 400 410 420 DTSLRLKDEM DLYKRMMDKL RQNRLEFQKE REATQELIED LRKELEHLQM YKLDCERPGR 430 440 450 460 470 480 GRSASSGLGE FNARAREVEL EHEVKRLKQE NYKLRDQNDD LNGQILSLSL YEAKNLFAAQ 490 500 510 520 530 TKAQSLAAEI DTASRDELME ALKEQEEINF RLRQYMDKII LAILDHNPSI LEIKH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION IN ENDOSOMAL TRAFFICKING, SUBUNIT, INTERACTION WITH RAB11A.
[2]	"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). Tissue: Testis.
[3]	"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: Brain.
[4]	"Complete physical map and gene content of the human NF1 tumor suppressor region in human and mouse." Jenne D.E., Tinschert S., Dorschner M.O., Hameister H., Stephens K., Kehrer-Sawatzki H. Genes Chromosomes Cancer 37:111-120(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 29-637 (ISOFORM 1).
[5]	"Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro." Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O. DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-637 (ISOFORM 1). Tissue: Brain.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 342-637 (ISOFORM 1). Tissue: Brain.
[7]	"The novel Rab11-FIP/Rip/RCP family of proteins displays extensive homo- and hetero-interacting abilities." Wallace D.M., Lindsay A.J., Hendrick A.G., McCaffrey M.W. Biochem. Biophys. Res. Commun. 292:909-915(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT.
[8]	"Arfophilins are dual Arf/Rab 11 binding proteins that regulate recycling endosome distribution and are related to Drosophila nuclear fallout." Hickson G.R., Matheson J., Riggs B., Maier V.H., Fielding A.B., Prekeris R., Sullivan W., Barr F.A., Gould G.W. Mol. Biol. Cell 14:2908-2920(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[9]	"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 RAB11A AND ARF6, MUTAGENESIS OF ASP-627.
[10]	"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: SUBCELLULAR LOCATION, INTERACTION WITH RAB11A.
[11]	"HCMV-encoded glycoprotein M (UL100) interacts with Rab11 effector protein FIP4." Krzyzaniak M.A., Mach M., Britt W.J. Traffic 10:1439-1457(2009) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH HCMV RAB11FIP4.
[12]	"A protein interaction network for Ecm29 links the 26 S proteasome to molecular motors and endosomal components." Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E., Rechsteiner M. J. Biol. Chem. 285:31616-31633(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH ECM29.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AY169244 mRNA. Translation: AAO21970.1. AK097424 mRNA. Translation: BAC05045.1. BC093914 mRNA. Translation: AAH93914.1. BC101517 mRNA. Translation: AAI01518.1. AJ314646 mRNA. Translation: CAC44535.1. AB058724 mRNA. Translation: BAB47450.1. AL831830 mRNA. Translation: CAD38543.1.
IPI	IPI00174771. IPI00556584.
RefSeq	NP_116321.2. NM_032932.3.
UniGene	Hs.406788.
3D structure databases
ProteinModelPortal	Q86YS3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86YS3. 1 interaction.
MINT	MINT-2877094.
STRING	9606.ENSP00000312837.
PTM databases
PhosphoSite	Q86YS3.
Polymorphism databases
DMDM	67472134.
Proteomic databases
PaxDb	Q86YS3.
PRIDE	Q86YS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000325874; ENSP00000312837; ENSG00000131242. ENST00000394744; ENSP00000378227; ENSG00000131242.
GeneID	84440.
KEGG	hsa:84440.
UCSC	uc002hgn.1. human. uc002hgo.2. human.
Organism-specific databases
CTD	84440.
GeneCards	GC17P029718.
HGNC	HGNC:30267. RAB11FIP4.
HPA	HPA021595.
MIM	611999. gene.
neXtProt	NX_Q86YS3.
PharmGKB	PA134978007.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG259959.
HOGENOM	HOG000063670.
HOVERGEN	HBG054059.
InParanoid	Q86YS3.
KO	K12485.
OMA	EFNARAR.
OrthoDB	EOG4G1MG1.
PhylomeDB	Q86YS3.
Gene expression databases
Bgee	Q86YS3.
CleanEx	HS_RAB11FIP4.
Genevestigator	Q86YS3.
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	PF09457. RBD-FIP. 1 hit. [Graphical view]
PROSITE	PS00018. EF_HAND_1. False negative. PS50222. EF_HAND_2. 1 hit. PS51511. FIP_RBD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	RAB11FIP4. human.
GenomeRNAi	84440.
NextBio	74191.
SOURCE	Search...

Entry information

Entry name

RFIP4_HUMAN

Accession

Primary (citable) accession number: Q86YS3
Secondary accession number(s): Q52LI1 , Q8N829, Q8NDT7, Q969D8

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	June 1, 2003
Last modified:	May 1, 2013
This is version 88 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.