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Conserved domains on  [gi|19526463|ref|NP_080405|]
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endoplasmic reticulum resident protein 29 precursor [Mus musculus]

Protein Classification

endoplasmic reticulum resident protein 29( domain architecture ID 10222096)

endoplasmic reticulum resident protein 29 plays an important role in the processing of secretory proteins within the endoplasmic reticulum (ER), possibly by participating in the folding of proteins in the ER

CATH:  3.40.30.10
Gene Symbol:  ERP29
Gene Ontology:  GO:0005783|GO:0051087|GO:0042803
PubMed:  11435111|16677078|15558583
SCOP:  3000031

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 35-157 3.83e-66

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member pfam07912:

Pssm-ID: 469754  Cd Length: 126  Bit Score: 201.62  E-value: 3.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463    35 LHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLA-ENSASSEELLVAEVGISDYGDKLNMELSEKYKLD 113
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAkENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19526463   114 KESYPVFYLFRdGDLENPVLY--NGAVKVGAIQRWLKGQ-GVYLGMP 157
Cdd:pfam07912  81 KESYPVIYLFR-GDLENPVLYpsNGAVTVDALQRFLKGQtGLYIGMP 126
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 158-252 1.89e-28

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


:

Pssm-ID: 462253  Cd Length: 95  Bit Score: 103.81  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463   158 GCLPAYDALAGEFIKASSiEARQAILKQGQDGLLSVKETEKKWASQYLKIMGKILDQGEDFPASEMARIGKLIE-NKMSD 236
Cdd:pfam07749   1 GRIEELDALAAEFVAAAK-DERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAkGKLSP 79

                          90
                  ....*....|....*.
gi 19526463   237 SKKEELQKSLNILTAF 252
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
 
Name Accession Description Interval E-value
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 35-157 3.83e-66

ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains.


Pssm-ID: 400320  Cd Length: 126  Bit Score: 201.62  E-value: 3.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463    35 LHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLA-ENSASSEELLVAEVGISDYGDKLNMELSEKYKLD 113
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAkENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19526463   114 KESYPVFYLFRdGDLENPVLY--NGAVKVGAIQRWLKGQ-GVYLGMP 157
Cdd:pfam07912  81 KESYPVIYLFR-GDLENPVLYpsNGAVTVDALQRFLKGQtGLYIGMP 126
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 38-151 2.15e-62

PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ER-resident protein expressed in high levels in secretory cells. It forms homodimers and higher oligomers in vitro and in vivo. It contains a redox inactive TRX-like domain at the N-terminus, which is homologous to the redox active TRX (a) domains of PDI, and a C-terminal helical domain similar to the C-terminal domain of P5. The expression profile of ERp29 suggests a role in secretory protein production distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase.


Pssm-ID: 239305  Cd Length: 116  Bit Score: 191.60  E-value: 2.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463  38 KGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSAS-SEELLVAEVGISDYGDKLNMELSEKYKLDKES 116
Cdd:cd03007   1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASaTDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19526463 117 YPVFYLFRDGDLENPVLYNGA-VKVGAIQRWLKGQG 151
Cdd:cd03007  81 YPVIYLFHGGDFENPVPYSGAdVTVDALQRFLKGNT 116
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 158-252 1.89e-28

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


Pssm-ID: 462253  Cd Length: 95  Bit Score: 103.81  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463   158 GCLPAYDALAGEFIKASSiEARQAILKQGQDGLLSVKETEKKWASQYLKIMGKILDQGEDFPASEMARIGKLIE-NKMSD 236
Cdd:pfam07749   1 GRIEELDALAAEFVAAAK-DERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAkGKLSP 79

                          90
                  ....*....|....*.
gi 19526463   237 SKKEELQKSLNILTAF 252
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 160-252 1.75e-25

ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like proteins ERp29 and ERp38. ERp29 (also called ERp28) is a ubiquitous endoplasmic reticulum (ER)-resident protein expressed in high levels in secretory cells. It contains a redox inactive TRX-like domain at the N-terminus. The expression profile of ERp29 suggests a role in secretory protein production, distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex and is essential in regulating the secretion of thyroglobulin. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. ERp38 is a P5-like protein, first isolated from alfalfa (the cDNA clone was named G1), which contains two redox active TRX domains at the N-terminus, like human P5. However, unlike human P5, ERp38 also contains a C-terminal domain with homology to the C-terminal domain of ERp29. It may be a glucose-regulated protein. The function of the all-helical C-terminal domain of ERp29 and ERp38 remains unclear. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe.


Pssm-ID: 238146  Cd Length: 93  Bit Score: 96.22  E-value: 1.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463 160 LPAYDALAGEFIKASSiEARQAILKQGQDGLLSVKETEKKWASQYLKIMGKILDQGEDFPASEMARIGKLIENK-MSDSK 238
Cdd:cd00238   1 IEELDELAKEFVDASD-EERKELLEKVKEAVEKLKEAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKgLAPEK 79

                        90
                ....*....|....
gi 19526463 239 KEELQKSLNILTAF 252
Cdd:cd00238  80 ADELTRRLNILRSF 93
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 47-148 6.63e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 40.50  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463   47 TFYKVIPKSKFVLVKFdtqypYGEKQDEFKRLA-ENSASSEEL--LVAEVGISDYGDKLNMELSEKYKLdkESYPVFYLF 123
Cdd:PTZ00102  41 TFDKFITENEIVLVKF-----YAPWCGHCKRLApEYKKAAKMLkeKKSEIVLASVDATEEMELAQEFGV--RGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*
gi 19526463  124 RDGdleNPVLYNGAVKVGAIQRWLK 148
Cdd:PTZ00102 114 NKG---NPVNYSGGRTADGIVSWIK 135
 
Name Accession Description Interval E-value
ERp29_N pfam07912
ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and ...
 35-157 3.83e-66

ERp29, N-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein, and is involved in the processes of protein maturation and protein secretion in this organelle. The protein exists as a homodimer, with each monomer being composed of two domains. The N-terminal domain featured in this family is organized into a thioredoxin-like fold that resembles the a domain of human protein disulphide isomerase (PDI). However, this domain lacks the C-X-X-C motif required for the redox function of PDI; it is therefore thought that ERp29's function is similar to the chaperone function of PDI. The N-terminal domain is exclusively responsible for the homodimerization of the protein, without covalent linkages or additional contacts with other domains.


Pssm-ID: 400320  Cd Length: 126  Bit Score: 201.62  E-value: 3.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463    35 LHTKGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLA-ENSASSEELLVAEVGISDYGDKLNMELSEKYKLD 113
Cdd:pfam07912   1 LTTKGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAkENSASTEELLVAEVGIKDYGEKLNMELGERYKLD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 19526463   114 KESYPVFYLFRdGDLENPVLY--NGAVKVGAIQRWLKGQ-GVYLGMP 157
Cdd:pfam07912  81 KESYPVIYLFR-GDLENPVLYpsNGAVTVDALQRFLKGQtGLYIGMP 126
PDI_a_ERp29_N cd03007
PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ...
 38-151 2.15e-62

PDIa family, endoplasmic reticulum protein 29 (ERp29) subfamily; ERp29 is a ubiquitous ER-resident protein expressed in high levels in secretory cells. It forms homodimers and higher oligomers in vitro and in vivo. It contains a redox inactive TRX-like domain at the N-terminus, which is homologous to the redox active TRX (a) domains of PDI, and a C-terminal helical domain similar to the C-terminal domain of P5. The expression profile of ERp29 suggests a role in secretory protein production distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase.


Pssm-ID: 239305  Cd Length: 116  Bit Score: 191.60  E-value: 2.15e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463  38 KGALPLDTVTFYKVIPKSKFVLVKFDTQYPYGEKQDEFKRLAENSAS-SEELLVAEVGISDYGDKLNMELSEKYKLDKES 116
Cdd:cd03007   1 KGCVDLDTVTFYKVIPKFKYSLVKFDTAYPYGEKHEAFTRLAESSASaTDDLLVAEVGIKDYGEKLNMELGERYKLDKES 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 19526463 117 YPVFYLFRDGDLENPVLYNGA-VKVGAIQRWLKGQG 151
Cdd:cd03007  81 YPVIYLFHGGDFENPVPYSGAdVTVDALQRFLKGNT 116
ERp29 pfam07749
Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed ...
 158-252 1.89e-28

Endoplasmic reticulum protein ERp29, C-terminal domain; ERp29 is a ubiquitously expressed endoplasmic reticulum protein found in mammals. ERp29 is comprised of two domains. This domain, the C-terminal domain, has an all helical fold. ERp29 is thought to form part of the thyroglobulin folding complex.


Pssm-ID: 462253  Cd Length: 95  Bit Score: 103.81  E-value: 1.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463   158 GCLPAYDALAGEFIKASSiEARQAILKQGQDGLLSVKETEKKWASQYLKIMGKILDQGEDFPASEMARIGKLIE-NKMSD 236
Cdd:pfam07749   1 GRIEELDALAAEFVAAAK-DERKELLEEAKKAAEKLKEAEKKYAKYYVKVMEKILEKGEEYVEKELARLEKLLAkGKLSP 79

                          90
                  ....*....|....*.
gi 19526463   237 SKKEELQKSLNILTAF 252
Cdd:pfam07749  80 EKKDELQIRLNILRSF 95
ERp29c cd00238
ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like ...
 160-252 1.75e-25

ERp29 and ERp38, C-terminal domain; composed of the protein disulfide isomerase (PDI)-like proteins ERp29 and ERp38. ERp29 (also called ERp28) is a ubiquitous endoplasmic reticulum (ER)-resident protein expressed in high levels in secretory cells. It contains a redox inactive TRX-like domain at the N-terminus. The expression profile of ERp29 suggests a role in secretory protein production, distinct from that of PDI. It has also been identified as a member of the thyroglobulin folding complex and is essential in regulating the secretion of thyroglobulin. The Drosophila homolog, Wind, is the product of windbeutel, an essential gene in the development of dorsal-ventral patterning. Wind is required for correct targeting of Pipe, a Golgi-resident type II transmembrane protein with homology to 2-O-sulfotransferase. ERp38 is a P5-like protein, first isolated from alfalfa (the cDNA clone was named G1), which contains two redox active TRX domains at the N-terminus, like human P5. However, unlike human P5, ERp38 also contains a C-terminal domain with homology to the C-terminal domain of ERp29. It may be a glucose-regulated protein. The function of the all-helical C-terminal domain of ERp29 and ERp38 remains unclear. The C-terminal domain of Wind is thought to provide a distinct site required for interaction with its substrate, Pipe.


Pssm-ID: 238146  Cd Length: 93  Bit Score: 96.22  E-value: 1.75e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463 160 LPAYDALAGEFIKASSiEARQAILKQGQDGLLSVKETEKKWASQYLKIMGKILDQGEDFPASEMARIGKLIENK-MSDSK 238
Cdd:cd00238   1 IEELDELAKEFVDASD-EERKELLEKVKEAVEKLKEAEAKYAKYYVKVMEKILEKGEDYVEKELARLERLLEKKgLAPEK 79

                        90
                ....*....|....
gi 19526463 239 KEELQKSLNILTAF 252
Cdd:cd00238  80 ADELTRRLNILRSF 93
PDI_a_family cd02961
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ...
 41-147 3.12e-11

Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29.


Pssm-ID: 239259 [Multi-domain]  Cd Length: 101  Bit Score: 58.78  E-value: 3.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463  41 LPLDTVTFYKVIPKSKFVLVKFDTQY--PYGEKQDEFKRLAENSASSEELLVAEVGISDygdklNMELSEKYKLdkESYP 118
Cdd:cd02961   1 VELTDDNFDELVKDSKDVLVEFYAPWcgHCKALAPEYEKLAKELKGDGKVVVAKVDCTA-----NNDLCSEYGV--RGYP 73

                        90       100
                ....*....|....*....|....*....
gi 19526463 119 VFYLFRDGDlENPVLYNGAVKVGAIQRWL 147
Cdd:cd02961  74 TIKLFPNGS-KEPVKYEGPRTLESLVEFI 101
PTZ00102 PTZ00102
disulphide isomerase; Provisional
 47-148 6.63e-04

disulphide isomerase; Provisional


Pssm-ID: 240266 [Multi-domain]  Cd Length: 477  Bit Score: 40.50  E-value: 6.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526463   47 TFYKVIPKSKFVLVKFdtqypYGEKQDEFKRLA-ENSASSEEL--LVAEVGISDYGDKLNMELSEKYKLdkESYPVFYLF 123
Cdd:PTZ00102  41 TFDKFITENEIVLVKF-----YAPWCGHCKRLApEYKKAAKMLkeKKSEIVLASVDATEEMELAQEFGV--RGYPTIKFF 113

                         90       100
                 ....*....|....*....|....*
gi 19526463  124 RDGdleNPVLYNGAVKVGAIQRWLK 148
Cdd:PTZ00102 114 NKG---NPVNYSGGRTADGIVSWIK 135
 
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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