P62492 (RB11A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-11A
Short name=Rab-11

Gene names

Name:	Rab11a
Synonyms:	Rab11

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab regulates endocytic recycling. Acts as a major regulator of membrane delivery during cytokinesis. Together with MYO5B and RAB8A participates in epithelial cell polarization. Together with RAB3IP, RAB8A, the exocyst complex, PARD3, PRKCI, ANXA2, CDC42 and DNMBP promotes transcytosis of PODXL to the apical membrane initiation sites (AMIS), apical surface formation and lumenogenesis. Together with MYO5B participates in CFTR trafficking to the plasma membrane and TF (Transferrin) recycling in nonpolarized cells. Required in a complex with MYO5B and RAB11FIP2 for the transport of NPC1L1 to the plasma membrane. Participates in the sorting and basolateral transport of CDH1 from the Golgi apparatus to the plasma membrane. Regulates the recycling of FCGRT (receptor of Fc region of monomeric Ig G) to basolateral membranes By similarity. May also play a role in melanosome transport and release from melanocytes. Ref.8
Subunit structure	Interacts with RAB11FIP1, RAB11FIP2, RAB11FIP3 (via its C-terminus) and RAB11FIP4. Interacts with EVI5; EVI5 and RAB11FIP3 may be mutually exclusive and compete for binding RAB11A. Interacts with RIP11 and STXBP6. Interacts (GDP-bound form) with ZFYVE27 By similarity. Interacts with SGSM1, SGSM2, SGSM3 and VIPAS39. Interacts with EXOC6 in a GTP-dependent manner. Interacts with BIRC6/bruce By similarity. May interact with TBC1D14 By similarity. Ref.5 Ref.6 Ref.7
Subcellular location	Cell membrane; Peripheral membrane protein By similarity. Recycling endosome membrane; Peripheral membrane protein By similarity. Cytoplasmic vesicle › phagosome membrane; Lipid-anchor; Cytoplasmic side By similarity. Note: Translocates with RAB11FIP2 from the vesicles of the endocytic recycling compartment (ERC) to the plasma membrane. Colocalizes with PARD3, PRKCI, EXOC5, OCLN, PODXL and RAB8A in apical membrane initiation sites (AMIS) during the generation of apical surface and lumenogenesis By similarity. Recruited to phagosomes containing S.aureus or Mycobacterium By similarity.
Sequence similarities	Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
Biological process	Cell cycle Protein transport Transport
Cellular component	Cell membrane Cytoplasmic vesicle Endosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Acetylation Lipoprotein Methylation Prenylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell cycle Inferred from electronic annotation. Source: UniProtKB-KW cytokinesis Inferred from electronic annotation. Source: Compara melanosome transport Inferred from mutant phenotype Ref.8. Source: UniProtKB neuron projection development Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of axon extension Inferred from mutant phenotype PubMed 22573681. Source: MGI protein localization to plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB protein transport Inferred from electronic annotation. Source: UniProtKB-KW regulation of long-term neuronal synaptic plasticity Inferred from electronic annotation. Source: Compara regulation of protein transport Inferred from electronic annotation. Source: Compara small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro vesicle-mediated transport Inferred from electronic annotation. Source: Compara
Cellular_component	axon Inferred from direct assay PubMed 22573681. Source: MGI cleavage furrow Inferred from sequence or structural similarity. Source: UniProtKB mitochondrion Inferred from direct assay PubMed 18614015. Source: MGI perinuclear region of cytoplasm Inferred from direct assay PubMed 22573681. Source: MGI phagocytic vesicle Inferred from sequence or structural similarity. Source: UniProtKB phagocytic vesicle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell protein complex Inferred from electronic annotation. Source: Compara recycling endosome Inferred from direct assay Ref.8. Source: UniProtKB recycling endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell trans-Golgi network Inferred from sequence orthology PubMed 15229288. Source: MGI transport vesicle Inferred from electronic annotation. Source: Compara
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Vps33b	P59016	3	EBI-770256,EBI-2656383

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 213	212	Ras-related protein Rab-11A		PRO_0000121152
	Propeptide	214 – 216	3	Removed in mature form Potential		PRO_0000370808
Regions
	Nucleotide binding	18 – 26	9	GTP By similarity
	Nucleotide binding	66 – 70	5	GTP By similarity
	Nucleotide binding	124 – 127	4	GTP By similarity
	Nucleotide binding	154 – 156	3	GTP By similarity
	Motif	40 – 48	9	Effector region By similarity
Amino acid modifications
	Modified residue	2	1	N-acetylglycine By similarity
	Modified residue	213	1	Cysteine methyl ester Potential
	Lipidation	212	1	S-geranylgeranyl cysteine By similarity
	Lipidation	213	1	S-geranylgeranyl cysteine By similarity
Experimental info
	Sequence conflict	180	1	Q → H in AAF36458. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P62492 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 76FC1E113A29B269	FASTA	216	24,394
	10 20 30 40 50 60 MGTRDDEYDY LFKVVLIGDS GVGKSNLLSR FTRNEFNLES KSTIGVEFAT RSIQVDGKTI 70 80 90 100 110 120 KAQIWDTAGQ ERYRAITSAY YRGAVGALLV YDIAKHLTYE NVERWLKELR DHADSNIVIM 130 140 150 160 170 180 LVGNKSDLRH LRAVPTDEAR AFAEKNGLSF IETSALDSTN VEAAFQTILT EIYRIVSQKQ 190 200 210 MSDRRENDMS PSNNVVPIHV PPTTENKPKV QCCQNI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic structure of murine rab11 family members." Bhartur S.G., Calhoun B.C., Woodrum J., Kurkjian J., Iyer S., Lai F., Goldenring J.R. Biochem. Biophys. Res. Commun. 269:611-617(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"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: Amnion and Head.
[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]. Strain: C57BL/6J.
[4]	Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 14-24; 42-51 AND 83-95, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Sec15 is an effector for the Rab11 GTPase in mammalian cells." Zhang X.-M., Ellis S., Sriratana A., Mitchell C.A., Rowe T. J. Biol. Chem. 279:43027-43034(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EXOC6.
[6]	"Identification of three novel proteins (SGSM1, 2, 3) which modulate small G protein (RAP and RAB)-mediated signaling pathway." Yang H., Sasaki T., Minoshima S., Shimizu N. Genomics 90:249-260(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SGSM1; SGSM2 AND SGSM3.
[7]	"Mutations in VIPAR cause an arthrogryposis, renal dysfunction and cholestasis syndrome phenotype with defects in epithelial polarization." Cullinane A.R., Straatman-Iwanowska A., Zaucker A., Wakabayashi Y., Bruce C.K., Luo G., Rahman F., Gurakan F., Utine E., Ozkan T.B., Denecke J., Vukovic J., Di Rocco M., Mandel H., Cangul H., Matthews R.P., Thomas S.G., Rappoport J.Z. , Arias I.M., Wolburg H., Knisely A.S., Kelly D.A., Muller F., Maher E.R., Gissen P. Nat. Genet. 42:303-312(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH VIPAS39.
[8]	"The recycling endosome protein Rab17 regulates melanocytic filopodia formation and melanosome trafficking." Beaumont K.A., Hamilton N.A., Moores M.T., Brown D.L., Ohbayashi N., Cairncross O., Cook A.L., Smith A.G., Misaki R., Fukuda M., Taguchi T., Sturm R.A., Stow J.L. Traffic 12:627-643(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN MELANOSOME TRANSPORT.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF127669 Genomic DNA. Translation: AAF36458.1. AK014268 mRNA. Translation: BAB29233.1. AK132072 mRNA. Translation: BAE20971.1. AK132159 mRNA. Translation: BAE21003.1. AK147122 mRNA. Translation: BAE27693.1. BC010722 mRNA. Translation: AAH10722.1.
IPI	IPI00323897.
RefSeq	NP_059078.2. NM_017382.5.
UniGene	Mm.1387.
3D structure databases
ProteinModelPortal	P62492.
ModBase	Search...
Protein-protein interaction databases
IntAct	P62492. 11 interactions.
PTM databases
PhosphoSite	P62492.
Proteomic databases
PaxDb	P62492.
PRIDE	P62492.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000172298; ENSMUSP00000129163; ENSMUSG00000004771.
GeneID	53869.
KEGG	mmu:53869.
Organism-specific databases
CTD	8766.
MGI	MGI:1858202. Rab11a.
Phylogenomic databases
eggNOG	COG1100.
HOGENOM	HOG000233968.
HOVERGEN	HBG009351.
InParanoid	P62492.
KO	K07904.
OMA	AMGTRDD.
OrthoDB	EOG4RR6J7.
Gene expression databases
ArrayExpress	P62492.
Bgee	P62492.
CleanEx	MM_RAB11A.
Genevestigator	P62492.
GermOnline	ENSMUSG00000004771. Mus musculus.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR003579. Small_GTPase_Rab_type. [Graphical view]
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
SMART	SM00175. RAB. 1 hit. [Graphical view]
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	310717.
SOURCE	Search...

Entry information

Entry name

RB11A_MOUSE

Accession

Primary (citable) accession number: P62492
Secondary accession number(s): P24410, Q3V1Z6, Q9JLX1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program