Conserved Protein Domain Family
alpha_CA_IX

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cd03150: alpha_CA_IX 
Carbonic anhydrase alpha, isozyme IX. Carbonic anhydrases (CAs) are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism: a nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Alpha CAs are strictly monomeric enzymes. The zinc ion is complexed by three histidine residues. This sub-family comprises the membrane protein CA IX. CA IX is functionally implicated in tumor growth and survival. CA IX is mainly present in solid tumors and its expression in normal tissues is limited to the mucosa of alimentary tract. CA IX is a transmembrane protein with two extracellular domains: carbonic anhydrase and, a proteoglycan-like segment mediating cell-cell adhesion. There is evidence for an involvement of the MAPK pathway in the regulation of CA9 expression.
Statistics
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PSSM-Id: 239403
View PSSM: cd03150
Aligned: 3 rows
Threshold Bit Score: 473.289
Threshold Setting Gi: 68437327
Created: 4-Nov-2005
Updated: 17-Jan-2013
Structure
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Aligned Rows:
 
active sitezinc binding
Feature 1:active site [active site]
Evidence:
  • Comment:zinc binding histidines and other residues found to be important for enzymatic activity

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                                              #                       #
gi 76624532 133 GAPPWPQVSPACAGRFQSPVDIRPELTAFCPALRPLEFLGFELPpqpkLRLCNNGHTVQLSLPSGLKMALGPgqEYRALQ 212
gi 9955948  145 GDPPWPRVSPACAGRFQSPVDIRPQLAAFCPALRPLELLGFQLPplpeLRLRNNGHSVQLTLPPGLEMALGPgrEYRALQ 224
gi 68437327  89 DQDAWLSAFEHCGGKSQSPINIDTHKVLHEPRLPPIQLDGYDLTgshsLTLLNNGHTLQLSLPSSMRIRRGFdqVYVAAQ 168
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1        # #         #            #                                                     
gi 76624532 213 LHLHWGAagrPGSEHTVDGHRFPAEIHVVHLSTAFEEFDEALGRPGGLAVLAAFLqeaqkkNSAYEQLLSRLGEITEKDS 292
gi 9955948  225 LHLHWGAagrPGSEHTVEGHRFPAEIHVVHLSTAFARVDEALGRPGGLAVLAAFLeegpeeNSAYEQLLSRLEEIAEEGS 304
gi 68437327 169 LHFHWGTtevPGSEHTIDNIHYPAEIHVVHYNSKYANLTEAASKADGLAVLGGFIaiglheNDNYEKILSALSDVSTEES 248
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
Feature 1                                  #                                                    
gi 76624532 293 ETWVPGLDVSALLPSDLSRYFRYEGSLTTPPCAQGVIWTVFNQTVKLSAKQLHTLSDSLWgpddsrLQLNFRATQPLNGR 372
gi 9955948  305 ETQVPGLDISALLPSDFSRYFQYEGSLTTPPCAQGVIWTVFNQTVMLSAKQLHTLSDTLWgpgdsrLQLNFRATQPLNGR 384
gi 68437327 249 LTVIPGFNVRHLLPNSLERFYRYSGSLTTPPCLQTVSWTLFNDSIRVSRRQLAALEESLKtehnklLSKNFRAPQLLHGR 328

                ....*..
Feature 1              
gi 76624532 373 IIEASFP 379
gi 9955948  385 VIEASFP 391
gi 68437327 329 KIQSSFH 335

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