Primary Information |
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| BoMiProt ID | Bomi340 |
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| Protein Name | Ras-related protein Rab-13 |
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| Organism | Bos taurus |
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| Uniprot ID | Q58DS5 |
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| Milk Fraction | MFGM, Exosome |
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| Ref Sequence ID | NP_001019711.1 |
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| Aminoacid Length | 203 |
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| Molecular Weight | 22970 |
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| FASTA Sequence |
Download |
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| Gene Name | RAB13 |
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| Gene ID | 514541 |
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| Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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| Protein Function | Recycling endosome-to-plasma
membrane transport, GLUT4
trafficking, epithelial junction
development; Rab proteins are GTPases that act as key regulators in
intracellular vesicular transport; belong to Ras family; switch between the inactive (GDP-bound)
and active (GTP-bound) forms; associate with membranes via their
C-terminal isoprenoid moieties; interact with motor proteins involved in transport; contribute to the structural
and functional identity of intracellular organelles; master regulators of organelle biogenesis
and cellular homeostasis; The ubiquitous Rab GTPases Rab5, Rab4,
and Rab11 function on the early endocytic
pathway, whereas Rab7 and Rab9 function on
the late endocytic pathway |
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| Biochemical Properties | Rabs are
inactivated by GTP hydrolysis catalyzed by GAPs (GTP
activating proteins), before extraction of GDP-bound
Rabs by GDB dissociation inhibitor (GDI); C-terminally lipidmodified
GTPases; high affinity for Rab escort protein and GDI; REP has high affinity for unprenylated Rabs; GDI binds unprenylated Rabs
weakly but prenylated Rabs very strongly; Rab GTPases
behave both as soluble and specifically localized,
integral-membrane proteins; kept soluble in the cytosol and in the inactive
(GDP-bound) conformation through association
with GDI; |
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| Significance in milk | important for proper mammary gland development |
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| PTMs | Prenylation—addition of one or two geranyl-
geranyl groups—on conserved carboxyterminal
cysteine residues; mammalian
Rab GTPases undergoes adenylation or
phosphocholination by bacterial enzymes that can
occur on the membrane-bound, inactive Rab
and preclude GDI rebinding |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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| Predicted Disorder Regions | NA |
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| DisProt Annotation | |
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| TM Helix Prediction | No TM helices |
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| Significance of PTMs | prenylation serves together with
upstream hypervariable regions in promoting
specific and stable membrane association; adenylation or
phosphocholination occurs in the absence of infection as an
alternative to GDI displacement and membrane
stabilization; |
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| Bibliography | 1. Wu, Y.-W. et al. (2007) ‘Interaction analysis of prenylated Rab GTPase with Rab escort protein and GDP dissociation inhibitor explains the need for both regulators’, Proceedings of the National Academy of Sciences, 104(30), pp. 12294–12299. doi: 10.1073/pnas.0701817104.
2. Hutagalung, A. H. and Novick, P. J. (2011) ‘Role of Rab GTPases in Membrane Traffic and Cell Physiology’, Physiological Reviews, 91(1), pp. 119–149. doi: 10.1152/physrev.00059.2009.
3. Ullrich, S. J. et al. (1993) ‘Phosphorylation at Ser-15 and Ser-392 in mutant p53 molecules from human tumors is altered compared to wild-type p53.’, Proceedings of the National Academy of Sciences, 90(13), pp. 5954–5958. doi: 10.1073/pnas.90.13.5954.
4. Gavriljuk, K. et al. (2013) ‘Membrane extraction of Rab proteins by GDP dissociation inhibitor characterized using attenuated total reflection infrared spectroscopy.’, Proceedings of the National Academy of Sciences of the United States of America. National Academy of Sciences, 110(33), pp. 13380–5. doi: 10.1073/pnas.1307655110.
5. Oesterlin, L. K., Goody, R. S. and Itzen, A. (2012) ‘Posttranslational modifications of Rab proteins cause effective displacement of GDP dissociation inhibitor’, Proceedings of the National Academy of Sciences, 109(15), pp. 5621–5626. doi: 10.1073/pnas.1121161109. |
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