Ras-related protein Rab-35 (RAB35)

The protein contains 201 amino acids for an estimated molecular weight of 23025 Da.

 

The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion. That Rab is involved in the process of endocytosis and is an essential rate-limiting regulator of the fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge. May indirectly regulate neurite outgrowth. Together with TBC1D13 may be involved in regulation of insulin-induced glucose transporter SLC2A4/GLUT4 translocation to the plasma membrane in adipocytes. (updated: Dec. 20, 2017)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  7. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 100
No model available.

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The reference OMIM entry for this protein is 604199

Ras-associated protein rab35; rab35

CLONING

The Ras superfamily of small GTP-binding proteins, which includes the Ras, Ral, Rho, Rap, and Rab families, is involved in controlling a diverse set of essential cellular functions. The Rab family appears to play a critical role in regulating exocytotic and endocytotic pathways. By PCR using degenerate oligonucleotides based on the RAB3D (604350) amino acid sequence, followed by screening of a human fetal skeletal muscle cDNA library with the PCR product, Zhu et al. (1994) isolated cDNAs encoding RAB11B (604198) and RAB35, which they named RAY. The deduced 201-amino acid RAB35 protein contains the 4 conserved domains important for GTP binding. RAB35 is similar to human RAB1A (RAB1; 179508), rat Rab1b (612565), and yeast YPT1 in the N-terminal region, but is different from these Rab family members in the C-terminal region. However, like these other Rab proteins, RAB35 has 2 consecutive cysteine residues at its C terminus; in Rab proteins, this region is thought to be involved in membrane association. Recombinant RAB35 expressed in bacteria had GTP-binding activity. Northern blot analysis detected a 3.6-kb RAB35 transcript in all human tissues examined.

GENE FUNCTION

Zhang et al. (2009) found that RAB35 regulates the assembly of actin filaments during bristle development in Drosophila and filopodia formation in cultured cells. These effects were mediated by the actin-bundling protein fascin (602689), which directly associated with active Rab35. Targeting Rab35 to the outer mitochondrial membrane triggered actin recruitment, demonstrating a role for an intracellular trafficking protein in localized actin assembly. Using mouse 3T3-L1 cells, Davey et al. (2012) found that Tbc1d13 (616218) inhibited insulin (INS; 176730)-stimulated Glut4 (SLC2A4; 138190) translocation to the plasma membrane by acting as a GTPase-activating protein for Rab35.

MAPPING

Hartz (2015) mapped the RAB35 gene to chromosome 12q24.23 based on an alignment of the RAB35 sequence (GenBank GENBANK AF498960) with the genomic sequence (GRCh38). ... More on the omim web site

Subscribe to this protein entry history

Feb. 10, 2018: Protein entry updated
Automatic update: Entry updated from uniprot information.

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 604199 was added.