Q9ERI2 (RB27A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ras-related protein Rab-27A

Gene names

Name:

Rab27a

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	221 AA.
Sequence status	Complete.
Protein existence	Evidence 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.12 Ref.13
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 process	Exocytosis
Cellular component	Endosome Lysosome Membrane
Ligand	GTP-binding Nucleotide-binding
PTM	Disulfide bond Lipoprotein Methylation Phosphoprotein Prenylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 transport Inferred from mutant phenotype PubMed 11266473. Source: MGI multivesicular body sorting pathway Inferred from electronic annotation. Source: Compara natural killer cell degranulation Inferred from mutant phenotype PubMed 11266473. Source: MGI positive regulation of exocytosis Inferred from electronic annotation. Source: Compara protein targeting Inferred from mutant phenotype PubMed 11266470Ref.7. Source: MGI small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 14724135. Source: MGI apical plasma membrane Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome dendrite Inferred from electronic annotation. Source: Compara exocytic vesicle Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from direct assay PubMed 11964381. Source: UniProtKB multivesicular body membrane Inferred from electronic annotation. Source: Compara photoreceptor outer segment Inferred from direct assay PubMed 11964381. Source: UniProtKB secretory granule Inferred from mutant phenotype PubMed 11266473. Source: MGI secretory granule membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GDP binding Inferred from sequence or structural similarity. Source: UniProtKB GTP binding Inferred from direct assay Ref.13. Source: UniProtKB GTPase activity Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rph3a	P47708	2	EBI-398172,EBI-398376
SYTL5	Q8TDW5	2	EBI-398172,EBI-2939487	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 221

221

Ras-related protein Rab-27A

PRO_0000121222

Regions

Nucleotide binding

16 – 24

9

GTP

Nucleotide binding

74 – 78

5

GTP

Nucleotide binding

133 – 136

4

GTP

Nucleotide binding

163 – 165

3

GTP

Motif

38 – 46

9

Effector region By similarity

Amino acid modifications

Modified residue

211

1

Phosphoserine Ref.11

Modified residue

221

1

Cysteine methyl ester By similarity

Lipidation

219

1

S-geranylgeranyl cysteine By similarity

Lipidation

221

1

S-geranylgeranyl cysteine By similarity

Disulfide bond

123 ↔ 188

By similarity

Experimental info

Mutagenesis

78

1

Q → L: Loss of GTPase activity. Ref.13

Secondary structure

1

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221

Helix Strand Turn

Details...

Beta strand

7 – 15

9

Helix

22 – 31

10

Beta strand

43 – 53

11

Beta strand

66 – 75

10

Helix

79 – 81

3

Helix

82 – 87

6

Turn

88 – 91

4

Beta strand

93 – 100

8

Helix

104 – 108

5

Helix

110 – 120

11

Beta strand

121 – 125

5

Beta strand

128 – 133

6

Helix

138 – 140

3

Helix

145 – 155

11

Beta strand

159 – 161

3

Turn

164 – 166

3

Helix

170 – 187

18

Sequences

	Sequence		Length	Mass (Da)
	Q9ERI2 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: C6857EBDD7F38137	FASTA	221	25,017
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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-211, MASS SPECTROMETRY. Tissue: Melanoma.
[12]	"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.
[13]	"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.

IPI

IPI00112374.

RefSeq

NP_076124.1. NM_023635.5.

UniGene

Mm.34867.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BC1	X-ray	1.80	A/E	1-193	[»]

ProteinModelPortal

Q9ERI2.

SMR

Q9ERI2. Positions 4-187.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31054N.

IntAct

Q9ERI2. 11 interactions.

PTM databases

PhosphoSite

Q9ERI2.

Proteomic databases

PaxDb

Q9ERI2.

PRIDE

Q9ERI2.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000034722; ENSMUSP00000034722; ENSMUSG00000032202.

GeneID

11891.

KEGG

mmu:11891.

Organism-specific databases

CTD

5873.

MGI

MGI:1861441. Rab27a.

Phylogenomic databases

eggNOG

COG1100.

GeneTree

ENSGT00700000104288.

HOGENOM

HOG000233968.

HOVERGEN

HBG009351.

InParanoid

Q9ERI2.

KO

K07885.

OMA

DQRAVKE.

OrthoDB

EOG4PRSRM.

Enzyme and pathway databases

Reactome

REACT_118324. Disease.

Gene expression databases

ArrayExpress

Q9ERI2.

Bgee

Q9ERI2.

CleanEx

MM_RAB27A.

Genevestigator

Q9ERI2.

GermOnline

ENSMUSG00000032202. 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

ChiTaRS

RAB27A. mouse.

EvolutionaryTrace

Q9ERI2.

NextBio

279933.

SOURCE

Search...

Entry information

Entry name

RB27A_MOUSE

Accession

Primary (citable) accession number: Q9ERI2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 16, 2002
Last sequence update:	March 1, 2001
Last modified:	April 3, 2013
This is version 109 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program