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Q9ERI2 (RB27A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 121. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ras-related protein Rab-27A
Gene names
Name:Rab27a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length221 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in cytotoxic granule exocytosis in lymphocytes. Required for both granule maturation and granule docking and priming at the immunologic synapse By similarity.

Subunit structure

Binds SYTL1, SYTL2, SLAC2B, MYRIP, SYTL3, SYTL4, SYTL5 and MLPH. Interacts with UNC13D. Interacts with RPH3A and RPH3A. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Membrane; Lipid-anchor. Melanosome By similarity. Late endosome By similarity. Lysosome By similarity. Note: Localizes to endosomal exocytic vesicles By similarity.

Tissue specificity

Detected in melanocytes. Expressed abundantly in the stomach and is predominantly localized at the apical region of gastric-surface mucus cells. Also expressed in the thymus and lung. Ref.9

Sequence similarities

Belongs to the small GTPase superfamily. Rab family.

Ontologies

Keywords
   Biological processExocytosis
   Cellular componentEndosome
Lysosome
Membrane
   LigandGTP-binding
Nucleotide-binding
   PTMAcetylation
Disulfide bond
Lipoprotein
Methylation
Prenylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.12. Source: GOC

blood coagulation

Inferred from mutant phenotype Ref.1. Source: MGI

cytotoxic T cell degranulation

Inferred from mutant phenotype PubMed 11266473. Source: MGI

melanocyte differentiation

Inferred from mutant phenotype PubMed 2379821. Source: MGI

melanosome localization

Inferred from mutant phenotype PubMed 11266470. Source: MGI

melanosome transport

Inferred from mutant phenotype PubMed 11266473. Source: MGI

natural killer cell degranulation

Inferred from mutant phenotype PubMed 11266473. Source: MGI

pigment granule localization

Inferred from mutant phenotype PubMed 14978221PubMed 15572405. Source: MGI

pigment granule transport

Inferred from mutant phenotype PubMed 15572405. Source: MGI

pigmentation

Inferred from mutant phenotype PubMed 2379821. Source: MGI

protein targeting

Inferred from mutant phenotype PubMed 11266470Ref.7. Source: MGI

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

vesicle-mediated transport

Inferred from mutant phenotype Ref.1. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from direct assay PubMed 14724135. Source: MGI

cytosol

Traceable author statement. Source: Reactome

intracellular

Inferred from sequence or structural similarity Ref.1. Source: MGI

late endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

melanosome

Inferred from direct assay PubMed 11964381. Source: UniProtKB

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

photoreceptor outer segment

Inferred from direct assay PubMed 11964381. Source: UniProtKB

secretory granule

Inferred from mutant phenotype PubMed 11266473. Source: MGI

   Molecular_functionGDP binding

Inferred from sequence or structural similarity. Source: UniProtKB

GTP binding

Inferred from direct assay Ref.12. Source: UniProtKB

GTPase activity

Inferred from direct assay Ref.12. Source: UniProtKB

myosin V binding

Inferred from physical interaction PubMed 11266470. Source: MGI

protein binding

Inferred from physical interaction Ref.6PubMed 11964381Ref.11Ref.10Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Rph3aP477082EBI-398172,EBI-398376
SYTL5Q8TDW52EBI-398172,EBI-2939487From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 221220Ras-related protein Rab-27A
PRO_0000121222

Regions

Nucleotide binding16 – 249GTP
Nucleotide binding74 – 785GTP
Nucleotide binding133 – 1364GTP
Nucleotide binding163 – 1653GTP
Motif38 – 469Effector region By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2211Cysteine methyl ester By similarity
Lipidation2191S-geranylgeranyl cysteine By similarity
Lipidation2211S-geranylgeranyl cysteine By similarity
Disulfide bond123 ↔ 188 By similarity

Experimental info

Mutagenesis781Q → L: Loss of GTPase activity. Ref.12

Secondary structure

................................ 221
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9ERI2 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C6857EBDD7F38137

FASTA22125,017
        10         20         30         40         50         60 
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR VVYRANGPDG 

        70         80         90        100        110        120 
AVGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD LTNEQSFLNV RNWISQLQMH 

       130        140        150        160        170        180 
AYCENPDIVL CGNKSDLEDQ RAVKEEEARE LAEKYGIPYF ETSAANGTNI SHAIEMLLDL 

       190        200        210        220 
IMKRMERCVD KSWIPEGVVR SNGHTSADQL SEEKEKGLCG C 

« Hide

References

« Hide 'large scale' references
[1]"A mutation in Rab27a causes the vesicle transport defects observed in ashen mice."
Wilson S.M., Yip R., Swing D.A., O'Sullivan T.N., Zhang Y., Novak E.K., Swank R.T., Russell L.B., Copeland N.G., Jenkins N.A.
Proc. Natl. Acad. Sci. U.S.A. 97:7933-7938(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C3H/HeSn.
[2]Izumi T.
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Embryonic stem cell.
[4]"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].
[5]"Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains."
Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.
Biochem. Biophys. Res. Commun. 293:899-906(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYTL5.
[6]"The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain."
Kuroda T.S., Fukuda M., Ariga H., Mikoshiba K.
J. Biol. Chem. 277:9212-9218(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYTL1; SYTL2; SYTL3; SYTL4; SLAC2B AND MYRIP.
[7]"Identification of an organelle receptor for myosin-Va."
Wu X.S., Rao K., Zhang H., Wang F., Sellers J.R., Matesic L.E., Copeland N.G., Jenkins N.A., Hammer J.A. III
Nat. Cell Biol. 4:271-278(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MLPH.
[8]"Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2."
Fukuda M.
J. Biol. Chem. 278:15373-15380(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RPH3A AND RPH3AL.
[9]"Decreased basal mucus secretion by Slp2-a-deficient gastric surface mucous cells."
Saegusa C., Tanaka T., Tani S., Itohara S., Mikoshiba K., Fukuda M.
Genes Cells 11:623-631(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INTERACTION WITH SYTL2.
[10]"Doc2 alpha and Munc13-4 regulate Ca(2+) -dependent secretory lysosome exocytosis in mast cells."
Higashio H., Nishimura N., Ishizaki H., Miyoshi J., Orita S., Sakane A., Sasaki T.
J. Immunol. 180:4774-4784(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UNC13D.
[11]"Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to secretion from the immunological synapse."
Holt O., Kanno E., Bossi G., Booth S., Daniele T., Santoro A., Arico M., Saegusa C., Fukuda M., Griffiths G.M.
Traffic 9:446-457(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SYTL1 AND SYTL2.
[12]"Elucidation of Rab27 recruitment by its effectors: structure of Rab27a bound to Exophilin4/Slp2-a."
Chavas L.M., Ihara K., Kawasaki M., Torii S., Uejima T., Kato R., Izumi T., Wakatsuki S.
Structure 16:1468-1477(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-193 IN COMPLEX WITH GTP ANALOG, INTERACTION WITH SYTL2, MUTAGENESIS OF GLN-78.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF304376 mRNA. Translation: AAG24638.1.
AB046693 mRNA. Translation: BAB62313.1.
AK010373 mRNA. Translation: BAB26891.1.
BC008173 mRNA. Translation: AAH08173.1.
BC009656 mRNA. Translation: AAH09656.1.
CCDSCCDS23335.1.
RefSeqNP_076124.1. NM_023635.5.
XP_006510843.1. XM_006510780.1.
XP_006510844.1. XM_006510781.1.
XP_006510845.1. XM_006510782.1.
UniGeneMm.34867.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80A/E1-193[»]
ProteinModelPortalQ9ERI2.
SMRQ9ERI2. Positions 4-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198222. 4 interactions.
DIPDIP-31054N.
IntActQ9ERI2. 11 interactions.

PTM databases

PhosphoSiteQ9ERI2.

Proteomic databases

MaxQBQ9ERI2.
PaxDbQ9ERI2.
PRIDEQ9ERI2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034722; ENSMUSP00000034722; ENSMUSG00000032202.
ENSMUST00000184146; ENSMUSP00000139310; ENSMUSG00000032202.
GeneID11891.
KEGGmmu:11891.
UCSCuc009qqv.1. mouse.

Organism-specific databases

CTD5873.
MGIMGI:1861441. Rab27a.

Phylogenomic databases

eggNOGCOG1100.
GeneTreeENSGT00740000114962.
HOGENOMHOG000233968.
HOVERGENHBG009351.
InParanoidQ9ERI2.
KOK07885.
OMADQRAVKE.
OrthoDBEOG7FFMSC.
PhylomeDBQ9ERI2.
TreeFamTF312895.

Gene expression databases

ArrayExpressQ9ERI2.
BgeeQ9ERI2.
CleanExMM_RAB27A.
GenevestigatorQ9ERI2.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SMARTSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAB27A. mouse.
EvolutionaryTraceQ9ERI2.
NextBio279933.
PROQ9ERI2.
SOURCESearch...

Entry information

Entry nameRB27A_MOUSE
AccessionPrimary (citable) accession number: Q9ERI2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 121 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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