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Protein

Rab11 family-interacting protein 1

Gene

Rab11fip1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

A Rab11 effector protein involved in the endosomal recycling process. Also involved in controlling membrane trafficking along the phagocytic pathway and phagocytosis (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Rab11 family-interacting protein 1
Short name:
Rab11-FIP1
Alternative name(s):
Rab-coupling protein
Gene namesi
Name:Rab11fip1
Synonyms:Rcp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1923017. Rab11fip1.

Subcellular locationi

  • Recycling endosome By similarity
  • Cytoplasmic vesiclephagosome membrane By similarity

  • Note: Membrane-bound. RAB11A rather than RAB4A mediates RAB11FIP1 localization in the endocytic recycling compartment (ERC). Colocalizes with RAB11A at phagosomes (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasmic vesicle, Endosome, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 645645Rab11 family-interacting protein 1PRO_0000097305Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei204 – 2041PhosphoserineBy similarity
Modified residuei301 – 3011PhosphoserineBy similarity
Modified residuei340 – 3401Phosphoserine1 Publication
Modified residuei344 – 3441Phosphoserine1 Publication
Modified residuei346 – 3461Phosphoserine1 Publication
Modified residuei358 – 3581Phosphoserine1 Publication
Modified residuei434 – 4341PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9D620.
PaxDbiQ9D620.
PRIDEiQ9D620.

PTM databases

PhosphoSiteiQ9D620.

Expressioni

Gene expression databases

BgeeiQ9D620.
CleanExiMM_RAB11FIP1.
ExpressionAtlasiQ9D620. baseline and differential.
GenevisibleiQ9D620. MM.

Interactioni

Subunit structurei

Homooligomer. Interacts with RAB4A, RAB11A, RAB11B and RAB25 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ9D620. 1 interaction.
MINTiMINT-4127168.
STRINGi10090.ENSMUSP00000058042.

Structurei

3D structure databases

ProteinModelPortaliQ9D620.
SMRiQ9D620. Positions 605-637.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 110106C2PROSITE-ProRule annotationAdd
BLAST
Domaini573 – 63563FIP-RBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni581 – 64565Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recyclingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi211 – 22010Poly-Lys

Sequence similaritiesi

Contains 1 C2 domain.PROSITE-ProRule annotation
Contains 1 FIP-RBD domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG85521.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG079127.
InParanoidiQ9D620.
OrthoDBiEOG7WQ7SB.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9D620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE
60 70 80 90 100
KYATSVSERS LGAPVWREEA TFELPPLLSS GAAPAAAATL QLTVLHRALL
110 120 130 140 150
GLDKFLGRAE VDLRELHRDQ GRRKKQWYTL KSKPGKKDKE RGEIEVDIQF
160 170 180 190 200
MRNNMTASMF DLSMKDKSRN PFGKLKDKIK GKNKDSASDT ASAIVPSVTP
210 220 230 240 250
SVDSDDESFS KDKKKKSKIK TLFSKSSLQK TPLSQSMSVL PTSKSDKVLL
260 270 280 290 300
RAGDFQSQWD DDAHEDESSS ASDVMSHKRT SSTDQQPNQS NFSLPKKEGL
310 320 330 340 350
SFLGGLRSKN DSLSRSTVCI NGNHVYMEQP EARSEIRESS PSNSPSPQGF
360 370 380 390 400
RRKHLFSSTE NLAARSPKEP GEGGGTSSDR RLSDSSTKDS MKSMSLPSYR
410 420 430 440 450
PLTSGDNRES MSPANVEAAR ETKDSKKQES KKSSLLSLVT GKRDAAAKGS
460 470 480 490 500
ESEPLPTVSE KEKERKGALV EAQLREEDLM RRPEKDALPV ASQWGSSLNP
510 520 530 540 550
FEDVQISDPG ATTESRSEPK PPVPAARVPQ TKAVKPRPHP VKPMNTTATK
560 570 580 590 600
IANSSLGTAT IITENLISEA LMKKYQPSDP AFAYAQLTHD ELIQLVLKQK
610 620 630 640
ETISKKEFQV RELEDYIDNL LVRVMEETPN ILRVPAQMGK KAGKM
Length:645
Mass (Da):70,684
Last modified:July 27, 2011 - v2
Checksum:i667E0D12EC5FBD3B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601S → T in BAB29507 (PubMed:16141072).Curated
Sequence conflicti207 – 2071E → K in BAE30042 (PubMed:16141072).Curated
Sequence conflicti256 – 2561Q → H in BAE30042 (PubMed:16141072).Curated
Sequence conflicti283 – 2831T → A in BAE30042 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014696 mRNA. Translation: BAB29507.1.
AK151024 mRNA. Translation: BAE30042.1.
CH466580 Genomic DNA. Translation: EDL32793.1.
BC125400 mRNA. Translation: AAI25401.1.
BC132094 mRNA. Translation: AAI32095.1.
CCDSiCCDS52534.1.
RefSeqiNP_083699.2. NM_029423.2.
UniGeneiMm.205335.

Genome annotation databases

EnsembliENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
GeneIDi75767.
UCSCiuc009lia.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK014696 mRNA. Translation: BAB29507.1.
AK151024 mRNA. Translation: BAE30042.1.
CH466580 Genomic DNA. Translation: EDL32793.1.
BC125400 mRNA. Translation: AAI25401.1.
BC132094 mRNA. Translation: AAI32095.1.
CCDSiCCDS52534.1.
RefSeqiNP_083699.2. NM_029423.2.
UniGeneiMm.205335.

3D structure databases

ProteinModelPortaliQ9D620.
SMRiQ9D620. Positions 605-637.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9D620. 1 interaction.
MINTiMINT-4127168.
STRINGi10090.ENSMUSP00000058042.

PTM databases

PhosphoSiteiQ9D620.

Proteomic databases

MaxQBiQ9D620.
PaxDbiQ9D620.
PRIDEiQ9D620.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
GeneIDi75767.
UCSCiuc009lia.2. mouse.

Organism-specific databases

CTDi80223.
MGIiMGI:1923017. Rab11fip1.

Phylogenomic databases

eggNOGiNOG85521.
GeneTreeiENSGT00530000063203.
HOGENOMiHOG000234700.
HOVERGENiHBG079127.
InParanoidiQ9D620.
OrthoDBiEOG7WQ7SB.

Miscellaneous databases

NextBioi343894.
PROiQ9D620.
SOURCEiSearch...

Gene expression databases

BgeeiQ9D620.
CleanExiMM_RAB11FIP1.
ExpressionAtlasiQ9D620. baseline and differential.
GenevisibleiQ9D620. MM.

Family and domain databases

Gene3Di2.60.40.150. 1 hit.
InterProiIPR000008. C2_dom.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamiPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTiSM00239. C2. 1 hit.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 1 hit.
PROSITEiPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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: Bone marrow and Head.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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].
    Tissue: Brain.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-340; SER-344 AND SER-346, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiRFIP1_MOUSE
AccessioniPrimary (citable) accession number: Q9D620
Secondary accession number(s): Q05A58, Q3UBC2, Q8BN24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 107 of the entry and version 2 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

External Data

Dasty 3

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 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.