Primary Information |
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| BoMiProt ID | Bomi79 |
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| Protein Name | Ras-related protein Rap-1A |
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| Organism | Bos taurus |
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| Uniprot ID | P62833 |
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| Milk Fraction | Exosome |
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| Ref Sequence ID | NP_776873.1 |
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| Aminoacid Length | 184 |
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| Molecular Weight | 20987 |
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| FASTA Sequence |
Download |
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| Gene Name | RAP1A |
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| Gene ID | 282031 |
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| Protein Existence Status | Reviewed: xperimental evidence at protein level |
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Secondary Information |
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| Presence in other biological fluids/tissue/cells | localised to plasma membrane and specific granules of neutrophils |
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| Protein Function | Two rap families, designated rapl and rap2, identified with each family having two members denoted
as A and B, i.e. rap lA and rap lB; Rap proteins have roles in cellular function;
exert biological activities in cellular growth and differentiation
control, in a phagocyte-specific enzyme system
responsible for the generation of microbicidal oxygen radicals; role of rap1 in NADPH oxidase system of phagocytic cells |
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| Biochemical Properties | share highly conserved structural motifs with the ras
transforming proteins; regulated by a cycle of GTP binding and hydrolysis; The rate of GTP binding to Rap is limited at physiological conc of Mg2+ by dissociation of GDP; Hydrolysis of GTP to GDP occurs at a
very low rate on the Rap proteins; Rap-GDS interacts with
Rap 1A and lB as a 1: 1 stoichiometric complex ; A number of anionic phospholipids
antagonize the GDP/GTP exchange activity of Rap-GDS, and
reduce markedly the ability of GDS to stimulate Rap1 B GTP
binding;
RaplB may bind to anionic lipids in the plasma membrane
through the polycationic C-terminal domain, suppressing GDS
action. |
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| Significance in milk | important for proper mammary gland development |
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| PTMs | covalent addition of an isoprenoid group; addition of isoprenyl group to the cysteine residue of the
CAAX motif via a thioether linkage; RaplA, ending in CLLL, modified by a
geranylgeranyl group at Cys-181; Carboxylmethylation of RaplB
and RaplA is stimulated by guanosine 5'-[ɣthio]
triphosphate (GTPɣS); substrates for phosphorylation by
cyclic AMP-dependent protein kinase; as shown in HL60 which has been differentiated into neutrophil like ceel, rap1A phosphorylation site
is Ser-180; |
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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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| Linking IDs | |
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| Bibliography | 1. Orlando, R. A., & Farquhar, M. G. (1994). Functional domains of the receptor-associated protein (RAP). Proceedings of the National Academy of Sciences of the United States of America, 91(8), 3161–3165. https://doi.org/10.1073/pnas.91.8.3161 |
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