3RAB,1ZBD,2GF9


Conserved Protein Domain Family
Rab3

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cd01865: Rab3 
Click on image for an interactive view with Cn3D
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D
The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab 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: 206657
View PSSM: cd01865
Aligned: 12 rows
Threshold Bit Score: 329.566
Threshold Setting Gi: 4557959
Created: 6-Jan-2012
Updated: 17-Jan-2013
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:
  • Comment:The active conformation of Rab is stabilized by interations between the gamma phosphate of GTP and two critically conserved residues, Thr in switch I and Gly in switch II
  • Structure:3RAB: Rattus norvegicus Rab3a binds GppNHp, a GTP analog and Mg2+, defined at 3.5 A contacts
    View structure with Cn3D
  • Structure:1ZBD: Rattus norvegicus Rab3a binds GTP and Mg2+, defined using 3.5 A contacts
    View structure with Cn3D
  • Comment:the Thr residues coordinate Mg2+

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                #######         ##  # ##                         #                     
3RAB_A        5 MFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILM 84
1ZBD_A        8 XFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGLERYRTITTAYYRGAXGFILX 87
gi 131800    21 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRHDKRVKLQIWDTAGQERYRTITTAYYRGAMGFILM 100
gi 392973    21 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRQDKRVKLQIWDTAGQERYPTITTAYYRGAMGFLLM 100
gi 420274     1 MFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLM 80
gi 14573837  36 MFKLLIIGNSSVGKTSFLFRYCDDSFTSAFVSTVGIDFKVKTVFRGDKRVKLQIWDTAGQERYRTITTAYYRGAMGFILM 115
gi 19067861  30 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFKNEKRIKLQIWDTAGQERYRTITTAYYRGAMGFILM 109
gi 27696356  51 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVYRNEKRVKLQIWDTAGQERYRTITTAYYRGAMGFLLM 130
gi 29841146  15 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTIFRQDKRVKLQIWDTAGQERYRTITTAYYRGAMGFILM 94
gi 60653473  22 MFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFRQDKRVKLQIWDTAGQERYRTITTAYYRGAMGFILM 101
gi 62955495  22 MFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILM 101
2GF9_A       22 MFKLLLIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTVYRHDKRIKLQIWDTAGQERYRTITTAYYRGAMGFLLM 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                        ## ##                         ###              
3RAB_A       85 YDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVD 164
1ZBD_A       88 YDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDXEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVD 167
gi 131800   101 YDVTNEDSFNSVQDWVTQIKTYSWDNAQVILVGNKCDMEDQRVISFERGRQLADQLGVEFFETSAKENVNVKAVFERLVD 180
gi 392973   101 YDITNEESFNAVQDWCTQIKTYSWDNAQVVLVGNKCDLEDERVVSTERGKQLADQLGLEFFETSAKENINVKAVFERLVD 180
gi 420274    81 YDIANQESFTAVQDWLRRLKPIPGTTPQVILVGNKCDLEDERVVSAEDGQRLAGDLGFEFFEASAKENINVKQVFERLVD 160
gi 14573837 116 YDITNEESFNSVQDWCTQIKTYSWENAQVVLVGNKCDMDSERVVSMDRGRQLADQLGLEFFETSAKENINVKAVFEKLVE 195
gi 19067861 110 YDITNEESFNAVQDWSTQIKTYSWDNAQVILVGNKCDMEDERVISTERGQHLGEQLGFEFFETSAKDNINVKQTFERLVD 189
gi 27696356 131 YDISNLESFNAVQDWATQIKTYSWDNAQVLLVGNKCDLEDDRVIAAEDGRKLAEELGFEFFEASAKDNINVKQVFERLVD 210
gi 29841146  95 YDITNEESFNAVQDWVTQIKTYSWDNAQVVLVGNKCDLVDDRVVSVDRGRHLAHQLGLEFFEASAKENINVKNVFERLVD 174
gi 60653473 102 YDVTNEESFNSVQDWCTQIKTYSWDNAQVILVGNKCDMEDERVISTDKGKQLADQLGLEFFETSAKENINVKQTFERLVD 181
gi 62955495 102 YDITNEESFAAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVASERGRQLSEHLGFEYFEASAKDNINVKQTFERLVD 181
2GF9_A      102 YDIANQESFAAVQDWATQIKTYSWDNAQVILVGNKCDLEDERVVPAEDGRRLADDLGFEFFEASAKENINVKQVFERLVD 181

                ....*
Feature 1            
3RAB_A      165 VICEK 169
1ZBD_A      168 VICEK 172
gi 131800   181 IICDK 185
gi 392973   181 IICDK 185
gi 420274   161 IICDK 165
gi 14573837 196 IICDK 200
gi 19067861 190 IICDK 194
gi 27696356 211 IICEK 215
gi 29841146 175 IICDK 179
gi 60653473 182 IICDK 186
gi 62955495 182 IICEK 186
2GF9_A      182 VICEK 186

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