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Protein

Ras-related protein Rab-27B

Gene

Rab27b

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

Functioni

May be involved in targeting uroplakins to urothelial apical membranes.By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi16 – 249GTP1 Publication
Nucleotide bindingi74 – 785GTP1 Publication
Nucleotide bindingi133 – 1364GTP1 Publication
Nucleotide bindingi163 – 1653GTP1 Publication

GO - Molecular functioni

  • GDP binding Source: UniProtKB
  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB
  • myosin V binding Source: MGI
  • protein domain specific binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Ras-related protein Rab-27B
Gene namesi
Name:Rab27b
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:1931295. Rab27b.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi6 – 61Y → F: Abolishes the interaction with MLPH. 1 Publication
Mutagenesisi78 – 781Q → L: Loss of GTPase activity. 1 Publication
Mutagenesisi91 – 911D → G: Strongly reduces the interaction with MLPH. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 218217Ras-related protein Rab-27BPRO_0000121225Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Disulfide bondi123 ↔ 1881 Publication
Lipidationi216 – 2161S-geranylgeranyl cysteineBy similarity
Modified residuei218 – 2181Cysteine methyl esterBy similarity
Lipidationi218 – 2181S-geranylgeranyl cysteineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Lipoprotein, Methylation, Prenylation

Proteomic databases

EPDiQ99P58.
MaxQBiQ99P58.
PaxDbiQ99P58.
PRIDEiQ99P58.

PTM databases

PhosphoSiteiQ99P58.

Expressioni

Tissue specificityi

Expressed abundantly in the stomach and is predominantly localized at the apical region of gastric-surface mucus cells. Also expressed in the brain and spleen.1 Publication

Gene expression databases

BgeeiQ99P58.
CleanExiMM_RAB27B.
ExpressionAtlasiQ99P58. baseline and differential.
GenevisibleiQ99P58. MM.

Interactioni

Subunit structurei

Interacts with SYTL2, SYTL4, MYRIP and MLPH. Interacts with RPH3A and RPH3A.5 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi219798. 2 interactions.
DIPiDIP-46237N.
IntActiQ99P58. 4 interactions.
STRINGi10090.ENSMUSP00000068349.

Structurei

Secondary structure

1
218
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 179Combined sources
Helixi22 – 309Combined sources
Beta strandi37 – 5317Combined sources
Beta strandi66 – 7712Combined sources
Helixi80 – 8910Combined sources
Beta strandi94 – 1007Combined sources
Helixi105 – 11511Combined sources
Turni122 – 1243Combined sources
Beta strandi127 – 1337Combined sources
Helixi138 – 1403Combined sources
Helixi146 – 1538Combined sources
Turni154 – 1563Combined sources
Beta strandi159 – 1613Combined sources
Turni164 – 1674Combined sources
Helixi170 – 18718Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IEYX-ray3.18A/B1-193[»]
2IEZX-ray2.80A/B/H/I1-218[»]
2IF0X-ray2.80A/B1-198[»]
2ZETX-ray3.00A/B1-201[»]
ProteinModelPortaliQ99P58.
SMRiQ99P58. Positions 5-188.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ99P58.

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

eggNOGiKOG0081. Eukaryota.
ENOG410XQ3T. LUCA.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ99P58.
KOiK07886.
OMAiQNVEKSV.
OrthoDBiEOG7FFMSC.
PhylomeDBiQ99P58.
TreeFamiTF312895.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 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.

Q99P58-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTDGDYDYLI KLLALGDSGV GKTTFLYRYT DNKFNPKFIT TVGIDFREKR
60 70 80 90 100
VVYDTQGADG ASGKAFKVHL QLWDTAGQER FRSLTTAFFR DAMGFLLMFD
110 120 130 140 150
LTSQQSFLNV RNWMSQLQAN AYCENPDIVL IGNKADLPDQ REVNERQARE
160 170 180 190 200
LAEKYGIPYF ETSAATGQNV EKSVETLLDL IMKRMEKCVE KTQVPDTVNG
210
GNSGKLDGEK PAEKKCAC
Length:218
Mass (Da):24,560
Last modified:January 23, 2007 - v3
Checksum:i01DBC47275B4B955
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti57 – 571G → R in AAG45502 (Ref. 2) Curated
Sequence conflicti77 – 771G → E in AAG45502 (Ref. 2) Curated
Sequence conflicti100 – 1001D → V in AAG45502 (Ref. 2) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328893 mRNA. Translation: AAK11242.1.
AY010898 mRNA. Translation: AAG45502.1.
BC032928 mRNA. Translation: AAH32928.1.
CCDSiCCDS29331.1.
RefSeqiNP_001076022.1. NM_001082553.2.
NP_001289727.1. NM_001302798.1.
NP_085031.3. NM_030554.4.
UniGeneiMm.246753.

Genome annotation databases

EnsembliENSMUST00000069749; ENSMUSP00000068349; ENSMUSG00000024511.
ENSMUST00000117692; ENSMUSP00000112807; ENSMUSG00000024511.
ENSMUST00000121693; ENSMUSP00000114094; ENSMUSG00000024511.
GeneIDi80718.
KEGGimmu:80718.
UCSCiuc008fnz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF328893 mRNA. Translation: AAK11242.1.
AY010898 mRNA. Translation: AAG45502.1.
BC032928 mRNA. Translation: AAH32928.1.
CCDSiCCDS29331.1.
RefSeqiNP_001076022.1. NM_001082553.2.
NP_001289727.1. NM_001302798.1.
NP_085031.3. NM_030554.4.
UniGeneiMm.246753.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IEYX-ray3.18A/B1-193[»]
2IEZX-ray2.80A/B/H/I1-218[»]
2IF0X-ray2.80A/B1-198[»]
2ZETX-ray3.00A/B1-201[»]
ProteinModelPortaliQ99P58.
SMRiQ99P58. Positions 5-188.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi219798. 2 interactions.
DIPiDIP-46237N.
IntActiQ99P58. 4 interactions.
STRINGi10090.ENSMUSP00000068349.

PTM databases

PhosphoSiteiQ99P58.

Proteomic databases

EPDiQ99P58.
MaxQBiQ99P58.
PaxDbiQ99P58.
PRIDEiQ99P58.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000069749; ENSMUSP00000068349; ENSMUSG00000024511.
ENSMUST00000117692; ENSMUSP00000112807; ENSMUSG00000024511.
ENSMUST00000121693; ENSMUSP00000114094; ENSMUSG00000024511.
GeneIDi80718.
KEGGimmu:80718.
UCSCiuc008fnz.2. mouse.

Organism-specific databases

CTDi5874.
MGIiMGI:1931295. Rab27b.

Phylogenomic databases

eggNOGiKOG0081. Eukaryota.
ENOG410XQ3T. LUCA.
GeneTreeiENSGT00760000118937.
HOGENOMiHOG000233968.
HOVERGENiHBG009351.
InParanoidiQ99P58.
KOiK07886.
OMAiQNVEKSV.
OrthoDBiEOG7FFMSC.
PhylomeDBiQ99P58.
TreeFamiTF312895.

Miscellaneous databases

ChiTaRSiRab27b. mouse.
EvolutionaryTraceiQ99P58.
NextBioi350069.
PROiQ99P58.
SOURCEiSearch...

Gene expression databases

BgeeiQ99P58.
CleanExiMM_RAB27B.
ExpressionAtlasiQ99P58. baseline and differential.
GenevisibleiQ99P58. MM.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 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. "Chromosomal mapping, gene structure and characterization of the human and murine RAB27B gene."
    Ramalho J.S., Tolmachova T., Hume A.N., McGuigan A., Gregory-Evans C.Y., Huxley C., Seabra M.C.
    BMC Genet. 2:2-2(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mouse Rab27b."
    Chen Y., Deng F.-M., Sun T.-T., Kreibich G.
    Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: CH3/HeSn.
  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: Czech II.
    Tissue: Lung.
  4. "Involvement of Rab27b in the regulated secretion of pituitary hormones."
    Zhao S., Torii S., Yokota-Hashimoto H., Takeuchi T., Izumi T.
    Endocrinology 143:1817-1824(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SYTL4.
  5. "Slac2-c (synaptotagmin-like protein homologue lacking C2 domains-c), a novel linker protein that interacts with Rab27, myosin Va/VIIa, and actin."
    Fukuda M., Kuroda T.S.
    J. Biol. Chem. 277:43096-43103(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MYRIP.
  6. "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.
  7. "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.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Lung, Pancreas and Spleen.
  9. "Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases."
    Kukimoto-Niino M., Sakamoto A., Kanno E., Hanawa-Suetsugu K., Terada T., Shirouzu M., Fukuda M., Yokoyama S.
    Structure 16:1478-1490(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-201 IN COMPLEX WITH GTP AND MLPH, DISULFIDE BOND, MUTAGENESIS OF TYR-6; GLN-78 AND ASP-91.

Entry informationi

Entry nameiRB27B_MOUSE
AccessioniPrimary (citable) accession number: Q99P58
Secondary accession number(s): Q8CIX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2002
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 141 of the entry and version 3 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

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 one 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.