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Q86YS3 (RFIP4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length637 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Arf6P623312EBI-949727,EBI-988682From a different organism.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 637637Rab11 family-interacting protein 4
PRO_0000073880

Regions

Domain49 – 8436EF-hand
Domain574 – 63663FIP-RBD
Calcium binding62 – 7312 Potential
Region82 – 637556Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerization
Coiled coil280 – 617338 Potential

Natural variations

Alternative sequence1 – 102102Missing in isoform 2.
VSP_013724
Alternative sequence103 – 1119APEIPDCVE → MRTPPALGS in isoform 2.
VSP_013725

Experimental info

Mutagenesis6271D → A: Abolishes Rab11-binding. Ref.9
Sequence conflict4171T → I in BAC05045. Ref.2
Sequence conflict5181E → G in BAC05045. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8A5CDB9799383342

FASTA63771,928
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7ECB4806726B7D5D
Show »

FASTA53560,771

References

« Hide '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. expand/collapse author list , 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.
RefSeqNP_116321.2. NM_032932.3.
UniGeneHs.406788.

3D structure databases

ProteinModelPortalQ86YS3.
SMRQ86YS3. Positions 19-77, 596-636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124079. 10 interactions.
IntActQ86YS3. 3 interactions.
MINTMINT-2877094.
STRING9606.ENSP00000312837.

PTM databases

PhosphoSiteQ86YS3.

Polymorphism databases

DMDM67472134.

Proteomic databases

PaxDbQ86YS3.
PRIDEQ86YS3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000325874; ENSP00000312837; ENSG00000131242. [Q86YS3-1]
ENST00000394744; ENSP00000378227; ENSG00000131242. [Q86YS3-2]
GeneID84440.
KEGGhsa:84440.
UCSCuc002hgn.1. human. [Q86YS3-1]
uc002hgo.2. human. [Q86YS3-2]

Organism-specific databases

CTD84440.
GeneCardsGC17P029718.
HGNCHGNC:30267. RAB11FIP4.
HPAHPA021595.
MIM611999. gene.
neXtProtNX_Q86YS3.
PharmGKBPA134978007.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259959.
HOGENOMHOG000063670.
HOVERGENHBG054059.
InParanoidQ86YS3.
KOK12485.
OMAGRQLMHS.
OrthoDBEOG793B75.
PhylomeDBQ86YS3.
TreeFamTF327221.

Gene expression databases

ArrayExpressQ86YS3.
BgeeQ86YS3.
CleanExHS_RAB11FIP4.
GenevestigatorQ86YS3.

Family and domain databases

Gene3D1.10.238.10. 1 hit.
InterProIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamPF09457. RBD-FIP. 1 hit.
[Graphical view]
PROSITEPS50222. EF_HAND_2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB11FIP4. human.
GeneWikiRAB11FIP4.
GenomeRNAi84440.
NextBio74191.
PROQ86YS3.
SOURCESearch...

Entry information

Entry nameRFIP4_HUMAN
AccessionPrimary (citable) accession number: Q86YS3
Secondary accession number(s): Q52LI1 expand/collapse secondary AC list , Q8N829, Q8NDT7, Q969D8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: June 1, 2003
Last modified: April 16, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM