2RCQ,4EXZ,1EII,1KQW,1KQX,4EFG,4QYP,4ZGU


Conserved Protein Domain Family
CRBP2

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cd19463: CRBP2 
cellular retinol-binding protein 2
Cellular retinol-binding proteins (CRBPs) participate in the cellular uptake of vitamin A in the form of free retinol. Retinol achieves a higher chemical stability when bound to CRBPs, and its interaction with retinol-binding proteins allows the solubilization in the aqueous medium of the hydrophobic retinol molecule. There are four human CRBP types (CRBP1, -2, -3, -4) which differ in their tissue-specific expression pattern, as well as in their different ligand affinities. CRBP2 is also known as: "retinol-binding protein 2, cellular", CRABP-II, CRBP2, CRBPII, and RBPC2. Expression of CRBP2 is limited to the small intestine. CRBP2 binds both retinol and retinal; rat CRBP2 appears to bind both with equal affinity, human CRBP2 showed a significantly higher affinity for retinol relative to retinal. CRBP2 can bind all-trans-retinol, all trans-retinal and 13-cis-retinol, but not 9-cis-retinol. CRBPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and, besides CRBPS, include the cellular retinoic acid-binding proteins (CRABPs) and the fatty acid-binding proteins (FABPs).
Statistics
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PSSM-Id: 381238
Aligned: 8 rows
Threshold Bit Score: 236.441
Created: 13-May-2008
Updated: 17-Oct-2022
Structure
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Program:
Drawing:
Aligned Rows:
 
retinol bindingligand binding
Conserved site includes 31 residues -Click on image for an interactive view with Cn3D
Feature 1:retinol binding site [chemical binding site]
Evidence:
  • Structure:1EII; Rattus norvegicus cellular retinol-binding protein II with bound retinol, contacts 4A
    View structure with Cn3D

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1      #     #     #  ##  # #   #  ##    # # #      # # # # #### #             ##     
2RCQ_A      7 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 86  human
4EXZ_A      3 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTLVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 82  human
1EII_A      4 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKIIVQDGDNFKTKTNSTFRNYDLDFTVGVEFDEHTKGLDGRNV 83  Norway rat
1KQW_A      3 DFNGTWEMLSNDNFEDVMKALDIDFATRKIAVHLKQTKVIVQNGDKFETKTLSTFRNYEVNFVIGEEFDEQTKGLDNRTV 82  zebrafish
1KQX_A      3 DFNGTWEMLSNDNFEDVMKALDIDFATRKIAVHLKQTKVIVQNGDKFETKTLSTFRNYEVNFVIGEEFDEQTKGLDNRTV 82  zebrafish
4EFG_A      3 DQNGTWEMESNENFEGWMKALDIDFALRKIAVRLTQTLVIDQDGDNFKVKCTSTFWNYDVDFTVGVEFDEYTKSLDNRHV 82  human
4QYP_A      3 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNYDVDFTVGVEFDEYTKSLDNRHV 82  human
4ZGU_A      3 DQNGTWEMESNENFEGYMKALDIDFATRKIAVRLTQTKVIDQDGDNFKTKTTSTFRNWDVDFTVGVEFDEYTKSLDNRHV 82  human
Feature 1               #          # # #        # #          #   
2RCQ_A     87 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCgdqVCRQVFKKK 137 human
4EXZ_A     83 KALVTWEGDVLVCVQKGEKENRGWKKWIEGNKLYLELTCgdqVCRQVFKKK 133 human
1EII_A     84 KTLVTWEGNTLVCVQKGEKENRGWKQWVEGDKLYLELTCgdqVCRQVFKKK 134 Norway rat
1KQW_A     83 KTLVKWDGDKLVCVQKGEKENRGWKQWIEGDLLHLEIHCqdkVCHQVFKKK 133 zebrafish
1KQX_A     83 KTLVKWDGDKLVCVQKGEKENRGWKQWIEGDLLHLEIHCqdkVCHQVFKKK 133 zebrafish
4EFG_A     83 KALVTWEGDVLVCVQKGEKENRGWKKWIEGDKLYLELTCgdqVCRQVFKKK 133 human
4QYP_A     83 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCgdqVCRQVFKKK 133 human
4ZGU_A     83 KALVTWEGDVLVCVQKGEKENRGWKQWIEGDKLYLELTCgdqVCRQVFKKK 133 human

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