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Conserved domains on  [gi|1953360272|ref|XP_038517604|]
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alpha-2-macroglobulin receptor-associated protein [Canis lupus familiaris]

Protein Classification

Alpha-2-MRAP_N and RAP_D3 domain-containing protein( domain architecture ID 12070242)

Alpha-2-MRAP_N and RAP_D3 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Alpha-2-MRAP_C pfam06401
Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 153-364 3.09e-89

Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. Two different studies have provided conflicted domain boundaries.


:

Pssm-ID: 461899 [Multi-domain]  Cd Length: 211  Bit Score: 267.22  E-value: 3.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGkFSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHS------ 226
Cdd:pfam06401   1 FKDKKLNKLWEKAETSG-FTEEELDKLKEEFQHHQEKIDEYYSLLEDLERTEEIHENSISPEELDRFNEIELAEkrdney 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 227 --KHAELKDRLRGINQGYDRLRRVSHRGYGTQaEFEEPRVIDLWDLAKSANFTEKELESFREELKHFEAKIEKHNHYQKQ 304
Cdd:pfam06401  80 leKHNLLKEKHRELRDGYDRLRRIAAKGPKSK-EFIEPKVQGLWKLALAANFTPDELESLKEELLHYETRLLKLRHYQAQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 305 LEISHQKLKHVesfgdrEHVSRNKEKYAMLEEKTKELGYKVKKHLQDLSGRISRaRHNEL 364
Cdd:pfam06401 159 LALSAEKLKHE------EHIGDKVEKHSTLEEKIKKLGRKVKKLHQDLESRISQ-RHNEL 211
Alpha-2-MRAP_N pfam06400
Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 29-137 2.28e-44

Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. The N-terminal domain is predominately alpha helical. Two different studies have provided conflicted domain boundaries.


:

Pssm-ID: 461898  Cd Length: 123  Bit Score: 149.00  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272  29 VGPRTAAGHGGKYSREKNEPE-----LPPKRESGGEFRMEKLNQLWEKAQRlQLSPVKLSELHADLKMQERDEFAWKKLK 103
Cdd:pfam06400   7 LGPSAAEAHAGKYSREANEPKpvdpyPPSKRELDKPFRMAKLNLVWEKAQR-RLTEVKLKSLHSDLKIHDKEELAWKKLK 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1953360272 104 AEGLDEDGEKQAKLTRNLSVILAKYGL----DGRKDAR 137
Cdd:pfam06400  86 AEGLDKDGEKEAELRKKLNGIMSTYGLlehfDDTKDPE 123
 
Name Accession Description Interval E-value
Alpha-2-MRAP_C pfam06401
Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 153-364 3.09e-89

Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. Two different studies have provided conflicted domain boundaries.


Pssm-ID: 461899 [Multi-domain]  Cd Length: 211  Bit Score: 267.22  E-value: 3.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGkFSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHS------ 226
Cdd:pfam06401   1 FKDKKLNKLWEKAETSG-FTEEELDKLKEEFQHHQEKIDEYYSLLEDLERTEEIHENSISPEELDRFNEIELAEkrdney 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 227 --KHAELKDRLRGINQGYDRLRRVSHRGYGTQaEFEEPRVIDLWDLAKSANFTEKELESFREELKHFEAKIEKHNHYQKQ 304
Cdd:pfam06401  80 leKHNLLKEKHRELRDGYDRLRRIAAKGPKSK-EFIEPKVQGLWKLALAANFTPDELESLKEELLHYETRLLKLRHYQAQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 305 LEISHQKLKHVesfgdrEHVSRNKEKYAMLEEKTKELGYKVKKHLQDLSGRISRaRHNEL 364
Cdd:pfam06401 159 LALSAEKLKHE------EHIGDKVEKHSTLEEKIKKLGRKVKKLHQDLESRISQ-RHNEL 211
Alpha-2-MRAP_N pfam06400
Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 29-137 2.28e-44

Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. The N-terminal domain is predominately alpha helical. Two different studies have provided conflicted domain boundaries.


Pssm-ID: 461898  Cd Length: 123  Bit Score: 149.00  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272  29 VGPRTAAGHGGKYSREKNEPE-----LPPKRESGGEFRMEKLNQLWEKAQRlQLSPVKLSELHADLKMQERDEFAWKKLK 103
Cdd:pfam06400   7 LGPSAAEAHAGKYSREANEPKpvdpyPPSKRELDKPFRMAKLNLVWEKAQR-RLTEVKLKSLHSDLKIHDKEELAWKKLK 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1953360272 104 AEGLDEDGEKQAKLTRNLSVILAKYGL----DGRKDAR 137
Cdd:pfam06400  86 AEGLDKDGEKEAELRKKLNGIMSTYGLlehfDDTKDPE 123
RAP_D2 cd14807
Domain 2 of receptor-associated protein (RAP); This subfamily is the N-terminal domain (D2) of ...
 153-250 1.32e-41

Domain 2 of receptor-associated protein (RAP); This subfamily is the N-terminal domain (D2) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.


Pssm-ID: 269814  Cd Length: 98  Bit Score: 141.15  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGKFSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHSKHAELK 232
Cdd:cd14807     1 FDDPRLEKLWNKAKTSGKFSDEELQKLHREFQHHKEKIHEYNILLETVSRTEEIHKNVISPSLEEDIKESVLHNKHTDLK 80

                          90
                  ....*....|....*...
gi 1953360272 233 DRLRGINQGYDRLRRVSH 250
Cdd:cd14807    81 ERLRSINQGFERLRKVSH 98
RAP_D1 cd14806
Receptor-associated protein (RAP), Domain 1; This subfamily is the N-terminal domain (D1) of ...
 60-130 2.17e-32

Receptor-associated protein (RAP), Domain 1; This subfamily is the N-terminal domain (D1) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D1 as well as domain 2 (D2) are essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as activated forms of alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly, suggesting the avidity effects arising from amino acid residues contributed from each domain. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.


Pssm-ID: 269813  Cd Length: 71  Bit Score: 115.94  E-value: 2.17e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953360272  60 FRMEKLNQLWEKAQRLQLSPVKLSELHADLKMQERDEFAWKKLKAEGLDEDGEKQAKLTRNLSVILAKYGL 130
Cdd:cd14806     1 FRMAKLNQLWEKAQRLLLSPVKLAELYADLKIQEKDELAWKKLKAEGLDEDGEKEAKLRRNLNVILAKYGL 71
 
Name Accession Description Interval E-value
Alpha-2-MRAP_C pfam06401
Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 153-364 3.09e-89

Alpha-2-macroglobulin RAP, C-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. Two different studies have provided conflicted domain boundaries.


Pssm-ID: 461899 [Multi-domain]  Cd Length: 211  Bit Score: 267.22  E-value: 3.09e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGkFSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHS------ 226
Cdd:pfam06401   1 FKDKKLNKLWEKAETSG-FTEEELDKLKEEFQHHQEKIDEYYSLLEDLERTEEIHENSISPEELDRFNEIELAEkrdney 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 227 --KHAELKDRLRGINQGYDRLRRVSHRGYGTQaEFEEPRVIDLWDLAKSANFTEKELESFREELKHFEAKIEKHNHYQKQ 304
Cdd:pfam06401  80 leKHNLLKEKHRELRDGYDRLRRIAAKGPKSK-EFIEPKVQGLWKLALAANFTPDELESLKEELLHYETRLLKLRHYQAQ 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 305 LEISHQKLKHVesfgdrEHVSRNKEKYAMLEEKTKELGYKVKKHLQDLSGRISRaRHNEL 364
Cdd:pfam06401 159 LALSAEKLKHE------EHIGDKVEKHSTLEEKIKKLGRKVKKLHQDLESRISQ-RHNEL 211
Alpha-2-MRAP_N pfam06400
Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated ...
 29-137 2.28e-44

Alpha-2-macroglobulin RAP, N-terminal domain; The alpha-2-macroglobulin receptor-associated protein (RAP) is a intracellular glycoprotein that binds to the 2-macroglobulin receptor and other members of the low density lipoprotein receptor family. The protein inhibits binding of all currently known ligands of these receptors. The N-terminal domain is predominately alpha helical. Two different studies have provided conflicted domain boundaries.


Pssm-ID: 461898  Cd Length: 123  Bit Score: 149.00  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272  29 VGPRTAAGHGGKYSREKNEPE-----LPPKRESGGEFRMEKLNQLWEKAQRlQLSPVKLSELHADLKMQERDEFAWKKLK 103
Cdd:pfam06400   7 LGPSAAEAHAGKYSREANEPKpvdpyPPSKRELDKPFRMAKLNLVWEKAQR-RLTEVKLKSLHSDLKIHDKEELAWKKLK 85

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1953360272 104 AEGLDEDGEKQAKLTRNLSVILAKYGL----DGRKDAR 137
Cdd:pfam06400  86 AEGLDKDGEKEAELRKKLNGIMSTYGLlehfDDTKDPE 123
RAP_D2 cd14807
Domain 2 of receptor-associated protein (RAP); This subfamily is the N-terminal domain (D2) of ...
 153-250 1.32e-41

Domain 2 of receptor-associated protein (RAP); This subfamily is the N-terminal domain (D2) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D2, along with RAP domain 1 (D1), is essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly to the second and the fourth ligand-binding clusters present on LRP, suggesting the avidity effects arising from amino acid residues contributed from each domain. Also, RAP has regions that interact weakly with heparin, one located in D2 and two located in D3. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.


Pssm-ID: 269814  Cd Length: 98  Bit Score: 141.15  E-value: 1.32e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGKFSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHSKHAELK 232
Cdd:cd14807     1 FDDPRLEKLWNKAKTSGKFSDEELQKLHREFQHHKEKIHEYNILLETVSRTEEIHKNVISPSLEEDIKESVLHNKHTDLK 80

                          90
                  ....*....|....*...
gi 1953360272 233 DRLRGINQGYDRLRRVSH 250
Cdd:cd14807    81 ERLRSINQGFERLRKVSH 98
RAP_D3 cd14808
C-terminal receptor-associated protein (RAP), Domain 3; This subfamily is the C-terminal ...
 259-364 5.68e-41

C-terminal receptor-associated protein (RAP), Domain 3; This subfamily is the C-terminal domain (D3) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D3 is required for folding and trafficking of low-density lipoprotein receptor-related protein (LRP). In the mildly acidic pH of the Golgi, unfolding of RAP-D3 helical bundle facilitates dissociation of RAP from the LDL receptor type A (LA) repeats of LDLR family proteins. Also, RAP has 3 regions that interact weakly with heparin, two regions located in D3 and one in RAP domain 2 (D2). The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.


Pssm-ID: 269815  Cd Length: 100  Bit Score: 139.34  E-value: 5.68e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 259 FEEPRVIDLWDLAKSANFTEKELESFREELKHFEAKIEKHNHYQKQLEISHQKLKHVESFGdrehvsRNKEKYAMLEEKT 338
Cdd:cd14808     1 FEEPRVQDLWKLAQKANFTPEELESFKEELKHFEKRLEKHRHYQKELELSHEKLEHKEKVG------RKPEKHAELEEKT 74

                          90       100
                  ....*....|....*....|....*.
gi 1953360272 339 KELGYKVKKHLQDLSGRISRARHNEL 364
Cdd:cd14808    75 KKLGRKVKKLHQDLESRISKARHTEL 100
RAP_D1 cd14806
Receptor-associated protein (RAP), Domain 1; This subfamily is the N-terminal domain (D1) of ...
 60-130 2.17e-32

Receptor-associated protein (RAP), Domain 1; This subfamily is the N-terminal domain (D1) of receptor-associated protein, RAP, an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. D1 as well as domain 2 (D2) are essential for blocking low-density lipoprotein receptor-related protein (LRP) from binding of certain ligands, such as activated forms of alpha2-macroglobulin; D1 and D2 each bind LRP weakly but the tandem D1D2 binds much more tightly, suggesting the avidity effects arising from amino acid residues contributed from each domain. The double module of complement type repeats, CR56, of LRP binds many ligands including alpha2-macroglobulin, which promotes the catabolism of the Abeta-peptide implicated in Alzheimer's disease.


Pssm-ID: 269813  Cd Length: 71  Bit Score: 115.94  E-value: 2.17e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953360272  60 FRMEKLNQLWEKAQRLQLSPVKLSELHADLKMQERDEFAWKKLKAEGLDEDGEKQAKLTRNLSVILAKYGL 130
Cdd:cd14806     1 FRMAKLNQLWEKAQRLLLSPVKLAELYADLKIQEKDELAWKKLKAEGLDEDGEKEAKLRRNLNVILAKYGL 71
RAP cd14803
Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a ...
 259-357 1.32e-21

Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. RAP associates with (LDL) receptor-related protein (LRP) early in the secretory pathway, reducing its ligand binding capacity, and then dissociates from LRP in the low-pH environment of the Golgi; studies have shown that histidine residues in RAP D3 serve as a switch that facilitates its uncoupling from the receptor. RAP is a modular protein identified as having an internal triplication, with domains, D1, D2, and D3, each thought to have distinct functions; these domains are independent and do not interact. The carboxyl-terminal domain (D3) of RAP is required for folding and trafficking of LRP, while the amino-terminal tandem D1D2 domains of RAP are essential for blocking LRP from binding of certain ligands, such as activated forms of alpha2-macroglobulin.


Pssm-ID: 269812  Cd Length: 97  Bit Score: 88.26  E-value: 1.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 259 FEEPRVIDLWDLAKSANFTEKELESFREELKHFEAKIEKHNHYQKQLEISHQKLKHVESFGDRehVSRNKEKYAMLEEKT 338
Cdd:cd14803     1 FRMPRLNQLWEKAQRLHLPPVELAELHAELKHQERKELAWNKLKLDLEIAEEIHEHAESPGDL--SDIKGEKHALGLDED 78

                          90
                  ....*....|....*....
gi 1953360272 339 KELGYKVKKHLQDLSGRIS 357
Cdd:cd14803    79 KEKEARLIRNLNVLLAKYG 97
RAP cd14803
Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a ...
 153-250 1.64e-19

Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. RAP associates with (LDL) receptor-related protein (LRP) early in the secretory pathway, reducing its ligand binding capacity, and then dissociates from LRP in the low-pH environment of the Golgi; studies have shown that histidine residues in RAP D3 serve as a switch that facilitates its uncoupling from the receptor. RAP is a modular protein identified as having an internal triplication, with domains, D1, D2, and D3, each thought to have distinct functions; these domains are independent and do not interact. The carboxyl-terminal domain (D3) of RAP is required for folding and trafficking of LRP, while the amino-terminal tandem D1D2 domains of RAP are essential for blocking LRP from binding of certain ligands, such as activated forms of alpha2-macroglobulin.


Pssm-ID: 269812  Cd Length: 97  Bit Score: 82.48  E-value: 1.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272 153 LEDPRLEKLWHKAKTSGKfSSEELDKLWREFQHHQEKVREYHVLLETLSRTEEIQENVISPFDTSRIKEDVLHSKHAELK 232
Cdd:cd14803     1 FRMPRLNQLWEKAQRLHL-PPVELAELHAELKHQERKELAWNKLKLDLEIAEEIHEHAESPGDLSDIKGEKHALGLDEDK 79

                          90
                  ....*....|....*...
gi 1953360272 233 DRLRGINQGYDRLRRVSH 250
Cdd:cd14803    80 EKEARLIRNLNVLLAKYG 97
RAP cd14803
Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a ...
 60-129 2.89e-09

Receptor-associated protein (RAP); Receptor-associated protein, RAP, is an antagonist and a specialized chaperone in the endoplasmic reticulum that binds tightly to members of the low-density lipoprotein (LDL) receptor family and prevents them from associating with other ligands. RAP associates with (LDL) receptor-related protein (LRP) early in the secretory pathway, reducing its ligand binding capacity, and then dissociates from LRP in the low-pH environment of the Golgi; studies have shown that histidine residues in RAP D3 serve as a switch that facilitates its uncoupling from the receptor. RAP is a modular protein identified as having an internal triplication, with domains, D1, D2, and D3, each thought to have distinct functions; these domains are independent and do not interact. The carboxyl-terminal domain (D3) of RAP is required for folding and trafficking of LRP, while the amino-terminal tandem D1D2 domains of RAP are essential for blocking LRP from binding of certain ligands, such as activated forms of alpha2-macroglobulin.


Pssm-ID: 269812  Cd Length: 97  Bit Score: 53.97  E-value: 2.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953360272  60 FRMEKLNQLWEKAQRLQLSPVKLSELHADLKMQERDEFAWKKLK---------------------------AEGLDEDGE 112
Cdd:cd14803     1 FRMPRLNQLWEKAQRLHLPPVELAELHAELKHQERKELAWNKLKldleiaeeihehaespgdlsdikgekhALGLDEDKE 80

                          90
                  ....*....|....*..
gi 1953360272 113 KQAKLTRNLSVILAKYG 129
Cdd:cd14803    81 KEARLIRNLNVLLAKYG 97
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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