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Q9D620 (RFIP1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Rab11 family-interacting protein 1
Short name=Rab11-FIP1
Alternative name(s):
Rab-coupling protein
Gene names
Name:Rab11fip1
Synonyms:Rcp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length645 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

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

Subcellular location

Recycling endosome By similarity. Cytoplasmic vesicle › phagosome 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.

Sequence similarities

Contains 1 C2 domain.

Contains 1 FIP-RBD domain.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCytoplasmic vesicle
Endosome
Membrane
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein transport

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentphagocytic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

recycling endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 645645Rab11 family-interacting protein 1
PRO_0000097305

Regions

Domain5 – 110106C2
Domain573 – 63563FIP-RBD
Region581 – 64565Necessary for interaction with RAB4A and RAB11A, subcellular location and endosomal recycling By similarity
Compositional bias211 – 22010Poly-Lys

Amino acid modifications

Modified residue2041Phosphoserine By similarity
Modified residue3011Phosphoserine By similarity
Modified residue3401Phosphoserine By similarity
Modified residue3441Phosphoserine Ref.6
Modified residue3461Phosphoserine Ref.6
Modified residue3571Phosphoserine Ref.4
Modified residue3581Phosphoserine Ref.5 Ref.7
Modified residue3831Phosphoserine Ref.5
Modified residue4341Phosphoserine By similarity

Experimental info

Sequence conflict601S → T in BAB29507. Ref.1
Sequence conflict2071E → K in BAE30042. Ref.1
Sequence conflict2561Q → H in BAE30042. Ref.1
Sequence conflict2831T → A in BAE30042. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9D620 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 667E0D12EC5FBD3B

FASTA64570,684
        10         20         30         40         50         60 
MSLAASAGRG PGTMWSPTHV QVTVLQARGL RAKGPGGTSD AYAVIQVGKE KYATSVSERS 

        70         80         90        100        110        120 
LGAPVWREEA TFELPPLLSS GAAPAAAATL QLTVLHRALL GLDKFLGRAE VDLRELHRDQ 

       130        140        150        160        170        180 
GRRKKQWYTL KSKPGKKDKE RGEIEVDIQF MRNNMTASMF DLSMKDKSRN PFGKLKDKIK 

       190        200        210        220        230        240 
GKNKDSASDT ASAIVPSVTP SVDSDDESFS KDKKKKSKIK TLFSKSSLQK TPLSQSMSVL 

       250        260        270        280        290        300 
PTSKSDKVLL RAGDFQSQWD DDAHEDESSS ASDVMSHKRT SSTDQQPNQS NFSLPKKEGL 

       310        320        330        340        350        360 
SFLGGLRSKN DSLSRSTVCI NGNHVYMEQP EARSEIRESS PSNSPSPQGF RRKHLFSSTE 

       370        380        390        400        410        420 
NLAARSPKEP GEGGGTSSDR RLSDSSTKDS MKSMSLPSYR PLTSGDNRES MSPANVEAAR 

       430        440        450        460        470        480 
ETKDSKKQES KKSSLLSLVT GKRDAAAKGS ESEPLPTVSE KEKERKGALV EAQLREEDLM 

       490        500        510        520        530        540 
RRPEKDALPV ASQWGSSLNP FEDVQISDPG ATTESRSEPK PPVPAARVPQ TKAVKPRPHP 

       550        560        570        580        590        600 
VKPMNTTATK IANSSLGTAT IITENLISEA LMKKYQPSDP AFAYAQLTHD ELIQLVLKQK 

       610        620        630        640 
ETISKKEFQV RELEDYIDNL LVRVMEETPN ILRVPAQMGK KAGKM

« Hide

References

[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-357, MASS SPECTROMETRY.
Tissue: Liver.
[5]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-358 AND SER-383, MASS SPECTROMETRY.
Tissue: Melanoma.
[6]"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-344 AND SER-346, MASS SPECTROMETRY.
Tissue: Macrophage.
[7]"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, MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
IPIIPI00317548.
RefSeqNP_083699.2. NM_029423.2.
UniGeneMm.205335.

3D structure databases

ProteinModelPortalQ9D620.
SMRQ9D620. Positions 605-637.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000058042.

PTM databases

PhosphoSiteQ9D620.

Proteomic databases

PaxDbQ9D620.
PRIDEQ9D620.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000033878; ENSMUSP00000033878; ENSMUSG00000031488.
GeneID75767.
KEGGmmu:75767.

Organism-specific databases

CTD80223.
MGIMGI:1923017. Rab11fip1.

Phylogenomic databases

eggNOGNOG85521.
GeneTreeENSGT00530000063203.
HOGENOMHOG000234700.
HOVERGENHBG079127.
KOK12484.
OrthoDBEOG42JNQP.

Gene expression databases

ArrayExpressQ9D620.
BgeeQ9D620.
CleanExMM_RAB11FIP1.
GenevestigatorQ9D620.
GermOnlineENSMUSG00000031488. Mus musculus.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR008973. C2_Ca/lipid-bd_dom_CaLB.
IPR018029. C2_membr_targeting.
IPR019018. Rab-bd_FIP-RBD.
[Graphical view]
PfamPF00168. C2. 1 hit.
PF09457. RBD-FIP. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
[Graphical view]
SUPFAMSSF49562. C2_CaLB. 1 hit.
PROSITEPS50004. C2. 1 hit.
PS51511. FIP_RBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio343894.
SOURCESearch...

Entry information

Entry nameRFIP1_MOUSE
AccessionPrimary (citable) accession number: Q9D620
Secondary accession number(s): Q05A58, Q3UBC2, Q8BN24
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 87 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents