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Q9ERI2

- RB27A_MOUSE

UniProt

Q9ERI2 - RB27A_MOUSE

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Protein
Ras-related protein Rab-27A
Gene
Rab27a
Organism
Mus musculus (Mouse)
Status
Reviewed - 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.

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. GTP binding Source: UniProtKB
  3. GTPase activity Source: UniProtKB
  4. myosin V binding Source: MGI
  5. protein binding Source: UniProtKB

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. blood coagulation Source: MGI
  3. cytotoxic T cell degranulation Source: MGI
  4. melanocyte differentiation Source: MGI
  5. melanosome localization Source: MGI
  6. melanosome transport Source: MGI
  7. natural killer cell degranulation Source: MGI
  8. pigment granule localization Source: MGI
  9. pigment granule transport Source: MGI
  10. pigmentation Source: MGI
  11. protein targeting Source: MGI
  12. small GTPase mediated signal transduction Source: InterPro
  13. vesicle-mediated transport Source: MGI
Complete GO annotation...

Keywords - Biological processi

Exocytosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_207837. 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: Chromosome 9

Organism-specific databases

MGIiMGI:1861441. Rab27a.

Subcellular locationi

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

GO - Cellular componenti

  1. Golgi apparatus Source: MGI
  2. cytosol Source: Reactome
  3. intracellular Source: MGI
  4. late endosome Source: UniProtKB-SubCell
  5. lysosome Source: UniProtKB-SubCell
  6. melanosome Source: UniProtKB
  7. membrane Source: UniProtKB-SubCell
  8. photoreceptor outer segment Source: UniProtKB
  9. secretory granule Source: MGI
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 – 11Removed By similarity
Chaini2 – 221220Ras-related protein Rab-27A
PRO_0000121222Add
BLAST

Amino acid modifications

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

ArrayExpressiQ9ERI2.
BgeeiQ9ERI2.
CleanExiMM_RAB27A.
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

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BC1X-ray1.80A/E1-193[»]
ProteinModelPortaliQ9ERI2.
SMRiQ9ERI2. Positions 4-187.

Miscellaneous databases

EvolutionaryTraceiQ9ERI2.

Family & Domainsi

Motif

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1100.
GeneTreeiENSGT00740000114962.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ9ERI2.
KOiK07885.
OMAiDQRAVKE.
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

MSDGDYDYLI KFLALGDSGV GKTSVLYQYT DGKFNSKFIT TVGIDFREKR    50
VVYRANGPDG AVGRGQRIHL QLWDTAGQER FRSLTTAFFR DAMGFLLLFD 100
LTNEQSFLNV RNWISQLQMH AYCENPDIVL CGNKSDLEDQ RAVKEEEARE 150
LAEKYGIPYF ETSAANGTNI SHAIEMLLDL IMKRMERCVD KSWIPEGVVR 200
SNGHTSADQL SEEKEKGLCG C 221
Length:221
Mass (Da):25,017
Last modified:March 1, 2001 - v1
Checksum:iC6857EBDD7F38137
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_076124.1. NM_023635.5.
XP_006510843.1. XM_006510780.1.
XP_006510844.1. XM_006510781.1.
XP_006510845.1. XM_006510782.1.
UniGeneiMm.34867.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS23335.1.
RefSeqi NP_076124.1. NM_023635.5.
XP_006510843.1. XM_006510780.1.
XP_006510844.1. XM_006510781.1.
XP_006510845.1. XM_006510782.1.
UniGenei Mm.34867.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3BC1 X-ray 1.80 A/E 1-193 [» ]
ProteinModelPortali Q9ERI2.
SMRi Q9ERI2. Positions 4-187.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198222. 4 interactions.
DIPi DIP-31054N.
IntActi Q9ERI2. 11 interactions.

PTM databases

PhosphoSitei Q9ERI2.

Proteomic databases

MaxQBi Q9ERI2.
PaxDbi Q9ERI2.
PRIDEi Q9ERI2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000034722 ; ENSMUSP00000034722 ; ENSMUSG00000032202 .
ENSMUST00000184146 ; ENSMUSP00000139310 ; ENSMUSG00000032202 .
GeneIDi 11891.
KEGGi mmu:11891.
UCSCi uc009qqv.1. mouse.

Organism-specific databases

CTDi 5873.
MGIi MGI:1861441. Rab27a.

Phylogenomic databases

eggNOGi COG1100.
GeneTreei ENSGT00740000114962.
HOGENOMi HOG000233968.
HOVERGENi HBG009351.
InParanoidi Q9ERI2.
KOi K07885.
OMAi DQRAVKE.
OrthoDBi EOG7FFMSC.
PhylomeDBi Q9ERI2.
TreeFami TF312895.

Enzyme and pathway databases

Reactomei REACT_207837. Insulin processing.

Miscellaneous databases

ChiTaRSi RAB27A. mouse.
EvolutionaryTracei Q9ERI2.
NextBioi 279933.
PROi Q9ERI2.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9ERI2.
Bgeei Q9ERI2.
CleanExi MM_RAB27A.
Genevestigatori Q9ERI2.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR003579. Small_GTPase_Rab_type.
[Graphical view ]
Pfami PF00071. Ras. 1 hit.
[Graphical view ]
PRINTSi PR00449. RASTRNSFRMNG.
SMARTi SM00175. RAB. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00231. small_GTP. 1 hit.
PROSITEi PS51419. RAB. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 122 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

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