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Q86YS3

- RFIP4_HUMAN

UniProt

Q86YS3 - RFIP4_HUMAN

Protein

Rab11 family-interacting protein 4

Gene

RAB11FIP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 1 (01 Jun 2003)
      Previous versions | rss
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    Functioni

    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 ARF6.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi62 – 7312PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. ADP-ribosylation factor binding Source: UniProtKB
    2. calcium ion binding Source: InterPro
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB
    5. Rab GTPase binding Source: UniProtKB

    GO - Biological processi

    1. cytokinesis Source: UniProtKB
    2. transport Source: UniProtKB-KW
    3. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Transport

    Keywords - Ligandi

    Calcium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Rab11 family-interacting protein 4
    Short name:
    FIP4-Rab11
    Short name:
    Rab11-FIP4
    Alternative name(s):
    Arfophilin-2
    Gene namesi
    Name:RAB11FIP4
    Synonyms:ARFO2, KIAA1821
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:30267. RAB11FIP4.

    Subcellular locationi

    Recycling endosome membrane; Peripheral membrane protein. Cleavage furrow. Midbody. Cytoplasmic vesicle
    Note: Recruited to the cleavage furrow and the midbody during cytokinesis.

    GO - Cellular componenti

    1. cleavage furrow Source: UniProtKB
    2. endocytic vesicle Source: UniProtKB
    3. endosome Source: UniProtKB
    4. extracellular space Source: UniProt
    5. midbody Source: UniProtKB
    6. recycling endosome membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi627 – 6271D → A: Abolishes Rab11-binding. 1 Publication

    Organism-specific databases

    PharmGKBiPA134978007.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 637637Rab11 family-interacting protein 4PRO_0000073880Add
    BLAST

    Proteomic databases

    MaxQBiQ86YS3.
    PaxDbiQ86YS3.
    PRIDEiQ86YS3.

    PTM databases

    PhosphoSiteiQ86YS3.

    Expressioni

    Tissue specificityi

    Present at high level in testis (at protein level). Weakly expressed in other tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ86YS3.
    BgeeiQ86YS3.
    CleanExiHS_RAB11FIP4.
    GenevestigatoriQ86YS3.

    Organism-specific databases

    HPAiHPA021595.

    Interactioni

    Subunit structurei

    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 ECM29.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Arf6P623312EBI-949727,EBI-988682From a different organism.

    Protein-protein interaction databases

    BioGridi124079. 10 interactions.
    IntActiQ86YS3. 3 interactions.
    MINTiMINT-2877094.
    STRINGi9606.ENSP00000312837.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86YS3.
    SMRiQ86YS3. Positions 17-81, 596-636.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini49 – 8436EF-handPROSITE-ProRule annotationAdd
    BLAST
    Domaini574 – 63663FIP-RBDPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni82 – 637556Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerizationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili280 – 617338Sequence AnalysisAdd
    BLAST

    Domaini

    The RBD-FIP domain mediates the interaction with Rab11 (RAB11A or RAB11B).By similarity

    Sequence similaritiesi

    Contains 1 EF-hand domain.PROSITE-ProRule annotation
    Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG259959.
    HOGENOMiHOG000063670.
    HOVERGENiHBG054059.
    InParanoidiQ86YS3.
    KOiK12485.
    OMAiGRQLMHS.
    OrthoDBiEOG793B75.
    PhylomeDBiQ86YS3.
    TreeFamiTF327221.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view]
    PfamiPF09457. RBD-FIP. 1 hit.
    [Graphical view]
    PROSITEiPS50222. EF_HAND_2. 1 hit.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86YS3-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAGGAGWSGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ    50
    GEEVEKLVKY LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL 100
    PCAPEIPDCV EQGSEVTGPT FADGELIPRE PGFFPEDEEE AMTLAPPEGP 150
    QELYTDSPME STQSLEGSVG SPAEKDGGLG GLFLPEDKSL VHTPSMTTSD 200
    LSTHSTTSLI SNEEQFEDYG EGDDVDCAPS SPCPDDETRT NVYSDLGSSV 250
    SSSAGQTPRK MRHVYNSELL DVYCSQCCKK INLLNDLEAR LKNLKANSPN 300
    RKISSTAFGR QLMHSSNFSS SNGSTEDLFR DSIDSCDNDI TEKVSFLEKK 350
    VTELENDSLT NGDLKSKLKQ ENTQLVHRVH ELEEMVKDQE TTAEQALEEE 400
    ARRHREAYGK LEREKATEVE LLNARVQQLE EENTELRTTV TRLKSQTEKL 450
    DEERQRMSDR LEDTSLRLKD EMDLYKRMMD KLRQNRLEFQ KEREATQELI 500
    EDLRKELEHL QMYKLDCERP GRGRSASSGL GEFNARAREV ELEHEVKRLK 550
    QENYKLRDQN DDLNGQILSL SLYEAKNLFA AQTKAQSLAA EIDTASRDEL 600
    MEALKEQEEI NFRLRQYMDK IILAILDHNP SILEIKH 637
    Length:637
    Mass (Da):71,928
    Last modified:June 1, 2003 - v1
    Checksum:i8A5CDB9799383342
    GO
    Isoform 2 (identifier: Q86YS3-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:535
    Mass (Da):60,771
    Checksum:i7ECB4806726B7D5D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti417 – 4171T → I in BAC05045. (PubMed:14702039)Curated
    Sequence conflicti518 – 5181E → G in BAC05045. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 102102Missing in isoform 2. 1 PublicationVSP_013724Add
    BLAST
    Alternative sequencei103 – 1119APEIPDCVE → MRTPPALGS in isoform 2. 1 PublicationVSP_013725

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11267.1. [Q86YS3-1]
    RefSeqiNP_116321.2. NM_032932.3. [Q86YS3-1]
    UniGeneiHs.406788.

    Genome annotation databases

    EnsembliENST00000394744; ENSP00000378227; ENSG00000131242. [Q86YS3-2]
    GeneIDi84440.
    KEGGihsa:84440.
    UCSCiuc002hgn.1. human. [Q86YS3-1]
    uc002hgo.2. human. [Q86YS3-2]

    Polymorphism databases

    DMDMi67472134.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11267.1. [Q86YS3-1 ]
    RefSeqi NP_116321.2. NM_032932.3. [Q86YS3-1 ]
    UniGenei Hs.406788.

    3D structure databases

    ProteinModelPortali Q86YS3.
    SMRi Q86YS3. Positions 17-81, 596-636.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 124079. 10 interactions.
    IntActi Q86YS3. 3 interactions.
    MINTi MINT-2877094.
    STRINGi 9606.ENSP00000312837.

    PTM databases

    PhosphoSitei Q86YS3.

    Polymorphism databases

    DMDMi 67472134.

    Proteomic databases

    MaxQBi Q86YS3.
    PaxDbi Q86YS3.
    PRIDEi Q86YS3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000394744 ; ENSP00000378227 ; ENSG00000131242 . [Q86YS3-2 ]
    GeneIDi 84440.
    KEGGi hsa:84440.
    UCSCi uc002hgn.1. human. [Q86YS3-1 ]
    uc002hgo.2. human. [Q86YS3-2 ]

    Organism-specific databases

    CTDi 84440.
    GeneCardsi GC17P029718.
    HGNCi HGNC:30267. RAB11FIP4.
    HPAi HPA021595.
    MIMi 611999. gene.
    neXtProti NX_Q86YS3.
    PharmGKBi PA134978007.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259959.
    HOGENOMi HOG000063670.
    HOVERGENi HBG054059.
    InParanoidi Q86YS3.
    KOi K12485.
    OMAi GRQLMHS.
    OrthoDBi EOG793B75.
    PhylomeDBi Q86YS3.
    TreeFami TF327221.

    Miscellaneous databases

    ChiTaRSi RAB11FIP4. human.
    GeneWikii RAB11FIP4.
    GenomeRNAii 84440.
    NextBioi 74191.
    PROi Q86YS3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86YS3.
    Bgeei Q86YS3.
    CleanExi HS_RAB11FIP4.
    Genevestigatori Q86YS3.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR002048. EF_hand_dom.
    IPR019018. Rab-bd_FIP-RBD.
    [Graphical view ]
    Pfami PF09457. RBD-FIP. 1 hit.
    [Graphical view ]
    PROSITEi PS50222. EF_HAND_2. 1 hit.
    PS51511. FIP_RBD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiRFIP4_HUMAN
    AccessioniPrimary (citable) accession number: Q86YS3
    Secondary accession number(s): Q52LI1
    , Q8N829, Q8NDT7, Q969D8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: June 1, 2003
    Last modified: October 1, 2014
    This is version 100 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3