1C1Y,1GUA


Conserved Protein Domain Family
Rap1

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cd04175: Rap1 
Click on image for an interactive view with Cn3D
Rap1 family GTPase consists of Rap1a and Rap1b isoforms
The Rap1 subgroup is part of the Rap subfamily of the Ras family. It can be further divided into the Rap1a and Rap1b isoforms. In humans, Rap1a and Rap1b share 95% sequence homology, but are products of two different genes located on chromosomes 1 and 12, respectively. Rap1a is sometimes called smg p21 or Krev1 in the older literature. Rap1 proteins are believed to perform different cellular functions, depending on the isoform, its subcellular localization, and the effector proteins it binds. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and the microsomal membrane of pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. High expression of Rap1 has been observed in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines; interestingly, in the SCCs, the active GTP-bound form localized to the nucleus, while the inactive GDP-bound form localized to the cytoplasm. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap1a, which is stimulated by T-cell receptor (TCR) activation, is a positive regulator of T cells by directing integrin activation and augmenting lymphocyte responses. In murine hippocampal neurons, Rap1b determines which neurite will become the axon and directs the recruitment of Cdc42, which is required for formation of dendrites and axons. In murine platelets, Rap1b is required for normal homeostasis in vivo and is involved in integrin activation. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.
Statistics
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PSSM-Id: 133375
View PSSM: cd04175
Aligned: 10 rows
Threshold Bit Score: 309.062
Threshold Setting Gi: 405068
Created: 20-Mar-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 20 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1              #######         ### # ##                        #                      
1C1Y_A      3 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVY 82  human
1GUA_A      3 EYKLVVLGSGGVGKSALTVQFVQGIFVDEYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVY 82  human
P08645      3 EYKIVVLGSGGVGKSALTVQFVQCIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 82  fruit fly
BAC57522    3 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEAENQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 82  Ciona intestinalis
AAA21445    5 DYKIVVLGSGAVGKSSITVRFVQGIFLVKYDPTIEDSYRKQLDLDGQQYVLEILDTAGTEQFTAMRDLYMKTGQGFVLVY 84  Entamoeba histolytica
CAA90983    3 EYKIVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 82  nematode
AAH44988    3 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVY 82  African clawed frog
AAH44548    3 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVY 82  zebrafish
CAA38185    5 EFKIVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDSNQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVY 84  Dictyostelium disc...
AAW25200    3 EYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQIQIGDRQCMLEILDTAGTEQFTAMRDLYMKSGQGFVLCY 82  Schistosoma japonicum
Feature 1                                      ## #                           ###             
1C1Y_A     83 SITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWcnCAFLESSAKSKINVNEIFYDLV 162 human
1GUA_A     83 SITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWcnCAFLESSAKSKINVNEIFYDLV 162 human
P08645     83 SITAQSTFNDLQDLREQILRVKDTDDVPMVLVGNKCDLEEERVVGKELGKNLATQFn-CAFMETSAKAKVNVNDIFYDLV 161 fruit fly
BAC57522   83 SITSQASFNDLTDLREQILRVKDTDEVPMILVGNKCDLEEERIVTREQGELLSRQWh-CSFMETSARTKINVENIFFDLV 161 Ciona intestinalis
AAA21445   85 SIMAQSTYNDLDPIHDQIVRVRDTENVPIIVVGNKCDLESQRIVSQDDGKALADKYg-AEFLEVSAKAEIRISDIFTTLI 163 Entamoeba histolytica
CAA90983   83 SITAQSTFNDLMDLRDQILRVKDTDEVPMILVGNKCDLEDERVVGKDQGQNLARQFg-SAFLETSAKAKINVSEVFYDLV 161 nematode
AAH44988   83 SITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWnnCAFLESSAKSKINVNEIFYDLV 162 African clawed frog
AAH44548   83 SITAQSTFNDLQDLREQILRVKGTDDVPMILVGNKCDLEDERVVGKEQGQNLARQWnsCAFLESSAKSKINVNEIFYDLV 162 zebrafish
CAA38185   85 SIISNSTFNELPDLREQILRVKDCEDVPMVLVGNKCDLHDQRVISTEQGEELARKFgdCYFLEASAKNKVNVEQIFYNLI 164 Dictyostelium disc...
AAW25200   83 SVTSQSSFNDLADLYEQILRVKNVAKVPLVLVGNKCDLKQERVVDCEQGQLLSRRLd-CTFMETSAKANINVHEVFIDLV 161 Schistosoma japonicum
Feature 1          
1C1Y_A    163 RQINR 167 human
1GUA_A    163 RQINR 167 human
P08645    162 RQINK 166 fruit fly
BAC57522  162 KQINR 166 Ciona intestinalis
AAA21445  164 KRINA 168 Entamoeba histolytica
CAA90983  162 RQINR 166 nematode
AAH44988  163 RQINR 167 African clawed frog
AAH44548  163 RQINR 167 zebrafish
CAA38185  165 RQINR 169 Dictyostelium discoideum
AAW25200  162 QQIIN 166 Schistosoma japonicum

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