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Protein

Rab11 family-interacting protein 4

Gene

Rab11fip4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 (By similarity). May play a role in differentiation during retinal development, in a Rab11-independent manner.By similarity1 Publication

Regions

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

GO - Molecular functioni

GO - Biological processi

  • cytokinesis Source: UniProtKB
  • neural retina development Source: MGI
  • positive regulation of G1 to G0 transition Source: MGI
  • transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, 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
Short name:
mRab11-FIP4A
Gene namesi
Name:Rab11fip4
Synonyms:Kiaa1821
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2442920. Rab11fip4.

Subcellular locationi

GO - Cellular componenti

  • cleavage furrow Source: UniProtKB
  • endocytic vesicle Source: UniProtKB
  • endosome Source: UniProtKB
  • extracellular space Source: MGI
  • midbody Source: UniProtKB
  • perinuclear region of cytoplasm Source: MGI
  • recycling endosome membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL2176809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Rab11 family-interacting protein 4PRO_0000073881Add
BLAST

Proteomic databases

MaxQBiQ8BQP8.
PaxDbiQ8BQP8.
PRIDEiQ8BQP8.

PTM databases

iPTMnetiQ8BQP8.
PhosphoSiteiQ8BQP8.

Expressioni

Tissue specificityi

Strongly expressed in the developing retina. Expressed predominantly in neural tissues.1 Publication

Gene expression databases

BgeeiQ8BQP8.
CleanExiMM_RAB11FIP4.
ExpressionAtlasiQ8BQP8. baseline and differential.
GenevisibleiQ8BQP8. MM.

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 (By similarity). Interacts with ECM29 (By similarity).By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000017783.

Structurei

3D structure databases

ProteinModelPortaliQ8BQP8.
SMRiQ8BQP8. Positions 17-81, 594-634.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini49 – 8436EF-handPROSITE-ProRule annotationAdd
BLAST
Domaini572 – 63463FIP-RBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 635554Necessary for interaction with RAB11A, subcellular location, homo- or heterooligomerizationBy similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili279 – 615337Sequence 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

eggNOGiKOG0982. Eukaryota.
ENOG4111K32. LUCA.
GeneTreeiENSGT00440000033742.
HOGENOMiHOG000063670.
HOVERGENiHBG054059.
InParanoidiQ8BQP8.
KOiK12485.
OMAiGRQLMHS.
OrthoDBiEOG793B75.
PhylomeDBiQ8BQP8.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8BQP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGGAGWAGA PAALLRSVRR LREVFEVCGR DPDGFLRVER VAALGLRFGQ
60 70 80 90 100
GEEVEKLVKC LDPNDLGRIN FKDFCRGVFA MKGCEELLKD VLSVESAGTL
110 120 130 140 150
PCSPDIPDCV EQGSDFSGST DGEQLPREPD FFQEDEEEAM TLALPEGPQE
160 170 180 190 200
LDMDSPMESS QGPEGSVKGC GEEKEPELGG LFLPEDKCLV LTPSVTTSDL
210 220 230 240 250
STHSTASLIS NEEQFEDYGE GDDVDCAPSS PCPDDETRTN VYSDLGSSVS
260 270 280 290 300
SSAGQTPRKM RHAYNSELLD VYCSQCCKKI NLLNDLEARL KNLKANSPNR
310 320 330 340 350
KISSTAFGRQ LMHNSNFSSS NGSTEDLFRD SIDSCDNDIT EKVSFLEKKV
360 370 380 390 400
TELENDSLTS GGLKSKLKQE NMQLVHRVHE LEEMVKDQET TAEQALEEEA
410 420 430 440 450
RRHREVYCKL EREKSTELEL LNTRVQQLEE ENTDLRTTVA RLKSQTEKLD
460 470 480 490 500
EERQRMSDRL EDTSLRLKDE MDLYKRMMDK LRQNRLEFQK EREATQELIE
510 520 530 540 550
DLRRELEHLQ MYKLDCERPG RGRSSSGLGE FNARAREVEL EHEVKRLKQE
560 570 580 590 600
NHKLRDQNDD LNGQILSLSL YEAKNLFATQ TKAQSLAAEI DTASRDELME
610 620 630
ALKEQEEINF RLRQYMDKII LAILDHNPSI LEIKH
Length:635
Mass (Da):71,901
Last modified:March 1, 2003 - v1
Checksum:i85F3C779A2963AAD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti368 – 37710KQENMQLVHR → WGTVAPGSAE in BAC65841 (PubMed:12693553).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046734 mRNA. Translation: BAC32850.1.
AL591174 Genomic DNA. Translation: CAI24836.1.
AK122559 mRNA. Translation: BAC65841.1.
CCDSiCCDS25123.1.
RefSeqiNP_780752.1. NM_175543.3.
UniGeneiMm.130656.
Mm.491175.

Genome annotation databases

EnsembliENSMUST00000017783; ENSMUSP00000017783; ENSMUSG00000017639.
GeneIDi268451.
KEGGimmu:268451.
UCSCiuc007kku.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK046734 mRNA. Translation: BAC32850.1.
AL591174 Genomic DNA. Translation: CAI24836.1.
AK122559 mRNA. Translation: BAC65841.1.
CCDSiCCDS25123.1.
RefSeqiNP_780752.1. NM_175543.3.
UniGeneiMm.130656.
Mm.491175.

3D structure databases

ProteinModelPortaliQ8BQP8.
SMRiQ8BQP8. Positions 17-81, 594-634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000017783.

Chemistry

ChEMBLiCHEMBL2176809.

PTM databases

iPTMnetiQ8BQP8.
PhosphoSiteiQ8BQP8.

Proteomic databases

MaxQBiQ8BQP8.
PaxDbiQ8BQP8.
PRIDEiQ8BQP8.

Protocols and materials databases

DNASUi268451.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000017783; ENSMUSP00000017783; ENSMUSG00000017639.
GeneIDi268451.
KEGGimmu:268451.
UCSCiuc007kku.1. mouse.

Organism-specific databases

CTDi84440.
MGIiMGI:2442920. Rab11fip4.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0982. Eukaryota.
ENOG4111K32. LUCA.
GeneTreeiENSGT00440000033742.
HOGENOMiHOG000063670.
HOVERGENiHBG054059.
InParanoidiQ8BQP8.
KOiK12485.
OMAiGRQLMHS.
OrthoDBiEOG793B75.
PhylomeDBiQ8BQP8.
TreeFamiTF327221.

Miscellaneous databases

PROiQ8BQP8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8BQP8.
CleanExiMM_RAB11FIP4.
ExpressionAtlasiQ8BQP8. baseline and differential.
GenevisibleiQ8BQP8. MM.

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]
SUPFAMiSSF47473. SSF47473. 1 hit.
PROSITEiPS50222. EF_HAND_2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Brain cortex.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
    Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
    DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 368-635.
    Tissue: Brain.
  4. "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: INTERACTION WITH RAB11A.
  5. "Mouse Rab11-FIP4 regulates proliferation and differentiation of retinal progenitors in a Rab11-independent manner."
    Muto A., Aoki Y., Watanabe S.
    Dev. Dyn. 236:214-225(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney.

Entry informationi

Entry nameiRFIP4_MOUSE
AccessioniPrimary (citable) accession number: Q8BQP8
Secondary accession number(s): Q80T87
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: March 1, 2003
Last modified: June 8, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.