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Protein

Ras-related protein Rab-27A

Gene

Rab27a

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

Functioni

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).By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 249GTP
Nucleotide bindingi74 – 785GTP
Nucleotide bindingi133 – 1364GTP
Nucleotide bindingi163 – 1653GTP

GO - Molecular functioni

  1. GDP binding Source: UniProtKB
  2. GTPase activity Source: UniProtKB
  3. GTP binding Source: UniProtKB
  4. myosin V binding Source: MGI

GO - Biological processi

  1. antigen processing and presentation Source: MGI
  2. blood coagulation Source: MGI
  3. complement-dependent cytotoxicity Source: MGI
  4. cytotoxic T cell degranulation Source: MGI
  5. exocytosis Source: MGI
  6. exosomal secretion Source: MGI
  7. melanocyte differentiation Source: MGI
  8. melanosome localization Source: MGI
  9. melanosome transport Source: MGI
  10. metabolic process Source: GOC
  11. multivesicular body organization Source: MGI
  12. multivesicular body sorting pathway Source: MGI
  13. natural killer cell degranulation Source: MGI
  14. pigmentation Source: MGI
  15. pigment granule localization Source: MGI
  16. pigment granule transport Source: MGI
  17. positive regulation of constitutive secretory pathway Source: MGI
  18. positive regulation of exocytosis Source: MGI
  19. positive regulation of gene expression Source: MGI
  20. positive regulation of phagocytosis Source: MGI
  21. positive regulation of reactive oxygen species biosynthetic process Source: MGI
  22. positive regulation of regulated secretory pathway Source: MGI
  23. protein secretion Source: GO_Central
  24. protein targeting Source: MGI
  25. Rab protein signal transduction Source: GO_Central
  26. vesicle docking involved in exocytosis Source: GO_Central
  27. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_298481. Insulin processing.

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-27A
Gene namesi
Name:Rab27a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1861441. Rab27a.

Subcellular locationi

  1. Membrane; Lipid-anchor
  2. Melanosome By similarity
  3. Late endosome By similarity
  4. Lysosome By similarity

  5. Note: Localizes to endosomal exocytic vesicles.By similarity

GO - Cellular componenti

  1. apical plasma membrane Source: Ensembl
  2. cytosol Source: Reactome
  3. dendrite Source: MGI
  4. exocytic vesicle Source: MGI
  5. extracellular vesicular exosome Source: MGI
  6. Golgi apparatus Source: MGI
  7. intracellular Source: MGI
  8. late endosome Source: MGI
  9. lysosome Source: MGI
  10. melanosome Source: UniProtKB
  11. multivesicular body membrane Source: MGI
  12. photoreceptor outer segment Source: UniProtKB
  13. secretory granule Source: MGI
  14. secretory granule membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Endosome, Lysosome, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi78 – 781Q → L: Loss of GTPase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 221220Ras-related protein Rab-27APRO_0000121222Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Disulfide bondi123 ↔ 188By similarity
Lipidationi219 – 2191S-geranylgeranyl cysteineBy similarity
Modified residuei221 – 2211Cysteine methyl esterBy similarity
Lipidationi221 – 2211S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

MaxQBiQ9ERI2.
PaxDbiQ9ERI2.
PRIDEiQ9ERI2.

PTM databases

PhosphoSiteiQ9ERI2.

Expressioni

Tissue specificityi

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.1 Publication

Gene expression databases

BgeeiQ9ERI2.
CleanExiMM_RAB27A.
ExpressionAtlasiQ9ERI2. baseline and differential.
GenevestigatoriQ9ERI2.

Interactioni

Subunit structurei

Binds SYTL1, SYTL2, SLAC2B, MYRIP, SYTL3, SYTL4, SYTL5 and MLPH. Interacts with UNC13D. Interacts with RPH3A and RPH3A.8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rph3aP477082EBI-398172,EBI-398376
SYTL5Q8TDW52EBI-398172,EBI-2939487From a different organism.

Protein-protein interaction databases

BioGridi198222. 4 interactions.
DIPiDIP-31054N.
IntActiQ9ERI2. 11 interactions.

Structurei

Secondary structure

1
221
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 159Combined sources
Helixi22 – 3110Combined sources
Beta strandi43 – 5311Combined sources
Beta strandi66 – 7510Combined sources
Helixi79 – 813Combined sources
Helixi82 – 876Combined sources
Turni88 – 914Combined sources
Beta strandi93 – 1008Combined sources
Helixi104 – 1085Combined sources
Helixi110 – 12011Combined sources
Beta strandi121 – 1255Combined sources
Beta strandi128 – 1336Combined sources
Helixi138 – 1403Combined sources
Helixi145 – 15511Combined sources
Beta strandi159 – 1613Combined sources
Turni164 – 1663Combined sources
Helixi170 – 18718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80A/E1-193[»]
ProteinModelPortaliQ9ERI2.
SMRiQ9ERI2. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9ERI2.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi38 – 469Effector regionBy similarity

Sequence similaritiesi

Belongs to the small GTPase superfamily. Rab family.Curated

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00770000120510.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9ERI2.
KOiK07885.
OMAiKEKGACG.
OrthoDBiEOG7FFMSC.
PhylomeDBiQ9ERI2.
TreeFamiTF312895.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9ERI2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR
60 70 80 90 100
VVYRANGPDG AVGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD
110 120 130 140 150
LTNEQSFLNV RNWISQLQMH AYCENPDIVL CGNKSDLEDQ RAVKEEEARE
160 170 180 190 200
LAEKYGIPYF ETSAANGTNI SHAIEMLLDL IMKRMERCVD KSWIPEGVVR
210 220
SNGHTSADQL SEEKEKGLCG C
Length:221
Mass (Da):25,017
Last modified:March 1, 2001 - v1
Checksum:iC6857EBDD7F38137
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23335.1.
RefSeqiNP_001288159.1. NM_001301230.1.
NP_001288161.1. NM_001301232.1.
NP_076124.1. NM_023635.6.
XP_006510843.1. XM_006510780.2.
UniGeneiMm.34867.
Mm.490032.

Genome annotation databases

EnsembliENSMUST00000034722; ENSMUSP00000034722; ENSMUSG00000032202.
ENSMUST00000184146; ENSMUSP00000139310; ENSMUSG00000032202.
GeneIDi11891.
KEGGimmu:11891.
UCSCiuc009qqv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS23335.1.
RefSeqiNP_001288159.1. NM_001301230.1.
NP_001288161.1. NM_001301232.1.
NP_076124.1. NM_023635.6.
XP_006510843.1. XM_006510780.2.
UniGeneiMm.34867.
Mm.490032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80A/E1-193[»]
ProteinModelPortaliQ9ERI2.
SMRiQ9ERI2. Positions 4-187.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198222. 4 interactions.
DIPiDIP-31054N.
IntActiQ9ERI2. 11 interactions.

PTM databases

PhosphoSiteiQ9ERI2.

Proteomic databases

MaxQBiQ9ERI2.
PaxDbiQ9ERI2.
PRIDEiQ9ERI2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000034722; ENSMUSP00000034722; ENSMUSG00000032202.
ENSMUST00000184146; ENSMUSP00000139310; ENSMUSG00000032202.
GeneIDi11891.
KEGGimmu:11891.
UCSCiuc009qqv.1. mouse.

Organism-specific databases

CTDi5873.
MGIiMGI:1861441. Rab27a.

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00770000120510.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9ERI2.
KOiK07885.
OMAiKEKGACG.
OrthoDBiEOG7FFMSC.
PhylomeDBiQ9ERI2.
TreeFamiTF312895.

Enzyme and pathway databases

ReactomeiREACT_298481. Insulin processing.

Miscellaneous databases

ChiTaRSiRab27a. mouse.
EvolutionaryTraceiQ9ERI2.
NextBioi279933.
PROiQ9ERI2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9ERI2.
CleanExiMM_RAB27A.
ExpressionAtlasiQ9ERI2. baseline and differential.
GenevestigatoriQ9ERI2.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SMARTiSM00175. RAB. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. 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.
    , 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. 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.

Entry informationi

Entry nameiRB27A_MOUSE
AccessioniPrimary (citable) accession number: Q9ERI2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: March 1, 2001
Last modified: April 1, 2015
This is version 129 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.