1MR3,1Z6X,1R8Q,1J2J,2KSQ,3AQ4,3LRP


Conserved Protein Domain Family
Arf1_5_like

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cd04150: Arf1_5_like 
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ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5)
The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).
Statistics
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PSSM-Id: 206717
Aligned: 27 rows
Threshold Bit Score: 285.84
Created: 1-Sep-2005
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
  next features
Conserved site includes 13 residues -Click on image for an interactive view with Cn3D
Feature 1:GTP/Mg2+ binding site [chemical binding site]
Evidence:
  • Structure:1MR3: Saccharomyces cerevisiae Arf2 complexed with GDP3'P, a GTP analog and Mg2+, defined at 3.5A contacts
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1             #######                                                                 
1MR3_F     18 MRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVETVQYKNISFTVWDVGGQDRIRSLWRHYYRNTEGVIFVIDSNDR 97  baker's yeast
AAF35891   18 MRILMVGLDAAGKTTILYKLKLGEVVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFSNTHGLIFVIDSNDR 97  Toxoplasma gondii
P40945     18 MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 97  fruit fly
O00909     18 MRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDR 97  Dictyostelium disc...
Q94650     18 VRILMVGLDAAGKTTILYKVKLGEVVTTIPTIGFNVETVEFRNISFTVWDVGGQDKIRPLWRHYYSNTDGLIFVVDSNDR 97  malaria parasite P...
P26991     18 VRILMVGLDAAGKTTILYKLMLGEVVTTVPTIGFNVETVEYKNINFTVWDVGGQDSIRPLWRHYYQNTDALIYVIDSADL 97  Giardia intestinalis
XP_827588  18 VRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNLKFTMWDVGGQDVLRPLWRHYYQNTNGIIFVVDSNDK 97  Trypanosoma brucei
XP_656677  14 MRILMVGLDAAGKTSILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYYQNTQAIIFVVDSNDR 93  Entamoeba histolyt...
CAI44530   18 MRILMVGLDAAGKTTILYKLKLGEVVSSVPTIGFNVEKVQYKNISFTVWDIGGQDKLRLLWRHYFNGTQGIIFVVDSSDK 97  Paramecium tetraur...
2KSQ_A     18 MRILMVGLDGAGKTTVLYKLKLGEVITTIPTIGFNVECVQYCNISFTVWDVGGQDRIRSLWRHYYCNTEGVIFVVDSNDR 97  baker's yeast
Feature 1                                   ## #                             ###              
1MR3_F     98 S--RIGEAREVMQRMLNEDELRNAVWLVFANKQDLPEAMsaaEITEKLGLHSIRnRPWFIQSTCATSGEGLYEGLEWLSN 175 baker's yeast
AAF35891   98 D--RIEDAREELHRMLNEDELRDAVLLIFANKQDLPNTMtaaEVTDKLHLHSIRhRNWFIQSTCATTGDGLYEGLDWLSR 175 Toxoplasma gondii
P40945     98 D--RITEAERELQNMLQEDELRDAVLLVFANKQDLPNAMtaaELTDKLRLNQLRnRHWFIQSTCATQGHGLYEGLDWLSA 175 fruit fly
O00909     98 E--RIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMsvaEVTDKLNLHSLRsRKWYIQSTCATSGDGLYEGLDWLSN 175 Dictyostelium disc...
Q94650     98 E--RIDDAREELHRMINEEELKDAIILVFANKQDLPNAMsaaEVTEKLHLNTIReRNWFIQSTCATRGDGLYEGFDWLTT 175 malaria parasite P...
P26991     98 EpkRIEDAKNELHTLLGEDELRDAALLVFANKQDLPKAMsttDLTERLGLQELKkRDWYIQPTCARSGDGLYQGLDWLSD 177 Giardia intestinalis
XP_827588  98 E--RVGKARQELEKMLSEDELRNAVLLVFANKQDLPNAMsttEVTEKLGLQSVRqRNWYIQGCCATTAQGLYEGLDWLSA 175 Trypanosoma brucei
XP_656677  94 D--RIGEAREELMKMLNEDEMRNAILLVFANKHDLPQAMsisEVTEKLGLQTIKnRKWYCQTSCATNGDGLYEGLDWLAD 171 Entamoeba histolyt...
CAI44530   98 E--RINVAKQELMRLMSEEELKDAAILILANKFDISQVTv-dQLISQFDLQNCR-RDWYVQTTCAITGDGLYQGLDWLSK 173 Paramecium tetraur...
2KSQ_A     98 S--RIGEAREVMQRMLNEDELCNAAWLVFANKQDLPEAMsaaEITEKLGLHSIRnRPWFIQATCATSGEGLYEGLEWLSN 175 baker's yeast
Feature 1      
1MR3_F    176 N 176 baker's yeast
AAF35891  176 T 176 Toxoplasma gondii
P40945    176 E 176 fruit fly
O00909    176 T 176 Dictyostelium discoideum
Q94650    176 H 176 malaria parasite P. falciparum
P26991    178 Y 178 Giardia intestinalis
XP_827588 176 N 176 Trypanosoma brucei
XP_656677 172 N 172 Entamoeba histolytica HM-1:IMSS
CAI44530  174 Q 174 Paramecium tetraurelia
2KSQ_A    176 C 176 baker's yeast

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