Search by BoMiProt ID - Bomi79

Primary Information

BoMiProt ID Bomi79
Protein Name Ras-related protein Rap-1A
Organism Bos taurus
Uniprot IDP62833
Milk FractionExosome
Ref Sequence ID NP_776873.1
Aminoacid Length 184
Molecular Weight 20987
FASTA Sequence Download
Gene Name RAP1A
Gene ID 282031
Protein Existence Status Reviewed: xperimental evidence at protein level

Secondary Information

Presence in other biological fluids/tissue/cells localised to plasma membrane and specific granules of neutrophils
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
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.
Significance in milk important for proper mammary gland development
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;
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Linking IDs
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.