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Conserved domains on  [gi|767934462|ref|XP_011512357|]
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reticulophagy regulator 1 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Arl6IP1_RETR3-like super family cl41772
ADP-ribosylation factor-like protein 6-interacting protein 1, Reticulophagy regulator 3, and ...
 13-126 8.05e-80

ADP-ribosylation factor-like protein 6-interacting protein 1, Reticulophagy regulator 3, and similar proteins; This family contains ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1) and the N-terminal reticulon-homology domain (RHD) of Reticulophagy regulators 1-3. Arl6IP1 is an endoplasmic reticulum (ER) protein that has an important role in cell conduction and material transport. Arl6IP1, a tetraspan membrane protein, is an anti-apoptotic protein specific to multicellular organisms, and is a potential player in shaping the ER tubules in mammalian cells. In Drosophila, knockdown of the Arl6IP1 gene leads to progressive motor deficit. An Arl6IP1 variant has also been associated with hereditary spastic paraplegia (HSP), motor and sensory polyneuropathy, and acromutilation. Reticulophagy regulator 1 (RETREG1/FAM134B) is an endoplasmic reticulum (ER)-anchored autophagy receptor that regulates the size and shape of the ER. It regulates turnover of the ER by selective phagocytosis, mediating ER delivery into lysosomes through sequestration into autophagosomes. It promotes membrane remodeling and ER scission through its membrane bending activity, and targets the fragments into autophagosomes by interacting with ATG8 family modifier proteins such as MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. RETREG2/FAM134A and RETREG3/FAM134C has been shown to interact with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1. Arl6IP1 shows some sequence similarity to the RHD of reticulophagy regulators, which may function in inducing membrane curvature.


The actual alignment was detected with superfamily member cd22560:

Pssm-ID: 425403  Cd Length: 198  Bit Score: 242.74  E-value: 8.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  13 RSLQAevSWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLL 92
Cdd:cd22560   87 RSLSE--SWEVIDSKPDERPRLSQCIAESWMNFSAFLQEMSHFKQQNPGKFCLLVCSVCTFFTILGSYIPGVVLSYLLLL 164

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767934462  93 CAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGIGE 126
Cdd:cd22560  165 CAFLCPLFKCNEFGQKVYSKVKSVLQKLDFGIGE 198
HAD_like super family cl21460
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ...
 190-282 4.03e-03

Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions.


The actual alignment was detected with superfamily member TIGR01493:

Pssm-ID: 473868 [Multi-domain]  Cd Length: 175  Bit Score: 37.89  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  190 EGYTPQTDTSDDLDRPSEEVFSR------DLSDFPslENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGL 263
Cdd:TIGR01493  22 AAIAPEGGAFSDLWRAKQQEYSWrrslmgDRRAFP--EDTVRALRYIADRLGLDAEPKYGERLRDAYKNLPPWPDSAAAL 99

                          90       100
                  ....*....|....*....|
gi 767934462  264 -TLPLNSDQTFHLMSNLAGD 282
Cdd:TIGR01493 100 aRVAILSNASHWAFDQFAQQ 119
 
Name Accession Description Interval E-value
RETR1_RHD cd22560
N-terminal reticulon-homology domain of Reticulophagy regulator 1; Reticulophagy regulator 1 ...
 13-126 8.05e-80

N-terminal reticulon-homology domain of Reticulophagy regulator 1; Reticulophagy regulator 1 (RETR1 or RETREG1), also called reticulophagy receptor 1 or FAM134B (family with sequence similarity 134, member B), is an endoplasmic reticulum (ER)-anchored autophagy receptor that regulates the size and shape of the ER. It regulates turnover of the ER by selective phagocytosis, mediating ER delivery into lysosomes through sequestration into autophagosomes. It promotes membrane remodeling and ER scission through its membrane bending activity, and targets the fragments into autophagosomes by interacting with ATG8 family modifier proteins such as MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. Loss of function of FAM134B is associated with diseases and cancer, including hereditary sensory and autonomic neuropathy type IIB (HSAN IIB), colorectal adenocarcinoma, and oesophageal squamous cell carcinoma, and other progressive neuronal degenerative diseases. FAM134B is also implicated in the suppression of viral replication during Ebola, Dengue, Zika, and West Nile viral infections. RETREG1/FAM134B contains an N-terminal reticulon-homology domain (RHD) that shows sequence similarity to ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), an ER protein that has an important role in cell conduction and material transport. The RHD may function in inducing membrane curvature.


Pssm-ID: 411699  Cd Length: 198  Bit Score: 242.74  E-value: 8.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  13 RSLQAevSWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLL 92
Cdd:cd22560   87 RSLSE--SWEVIDSKPDERPRLSQCIAESWMNFSAFLQEMSHFKQQNPGKFCLLVCSVCTFFTILGSYIPGVVLSYLLLL 164

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767934462  93 CAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGIGE 126
Cdd:cd22560  165 CAFLCPLFKCNEFGQKVYSKVKSVLQKLDFGIGE 198
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 190-282 4.03e-03

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 37.89  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  190 EGYTPQTDTSDDLDRPSEEVFSR------DLSDFPslENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGL 263
Cdd:TIGR01493  22 AAIAPEGGAFSDLWRAKQQEYSWrrslmgDRRAFP--EDTVRALRYIADRLGLDAEPKYGERLRDAYKNLPPWPDSAAAL 99

                          90       100
                  ....*....|....*....|
gi 767934462  264 -TLPLNSDQTFHLMSNLAGD 282
Cdd:TIGR01493 100 aRVAILSNASHWAFDQFAQQ 119
 
Name Accession Description Interval E-value
RETR1_RHD cd22560
N-terminal reticulon-homology domain of Reticulophagy regulator 1; Reticulophagy regulator 1 ...
 13-126 8.05e-80

N-terminal reticulon-homology domain of Reticulophagy regulator 1; Reticulophagy regulator 1 (RETR1 or RETREG1), also called reticulophagy receptor 1 or FAM134B (family with sequence similarity 134, member B), is an endoplasmic reticulum (ER)-anchored autophagy receptor that regulates the size and shape of the ER. It regulates turnover of the ER by selective phagocytosis, mediating ER delivery into lysosomes through sequestration into autophagosomes. It promotes membrane remodeling and ER scission through its membrane bending activity, and targets the fragments into autophagosomes by interacting with ATG8 family modifier proteins such as MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. Loss of function of FAM134B is associated with diseases and cancer, including hereditary sensory and autonomic neuropathy type IIB (HSAN IIB), colorectal adenocarcinoma, and oesophageal squamous cell carcinoma, and other progressive neuronal degenerative diseases. FAM134B is also implicated in the suppression of viral replication during Ebola, Dengue, Zika, and West Nile viral infections. RETREG1/FAM134B contains an N-terminal reticulon-homology domain (RHD) that shows sequence similarity to ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), an ER protein that has an important role in cell conduction and material transport. The RHD may function in inducing membrane curvature.


Pssm-ID: 411699  Cd Length: 198  Bit Score: 242.74  E-value: 8.05e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  13 RSLQAevSWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLL 92
Cdd:cd22560   87 RSLSE--SWEVIDSKPDERPRLSQCIAESWMNFSAFLQEMSHFKQQNPGKFCLLVCSVCTFFTILGSYIPGVVLSYLLLL 164

                         90       100       110
                 ....*....|....*....|....*....|....
gi 767934462  93 CAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGIGE 126
Cdd:cd22560  165 CAFLCPLFKCNEFGQKVYSKVKSVLQKLDFGIGE 198
RETR_RHD cd22558
N-terminal reticulon-homology domain of Reticulophagy regulators and similar proteins; This ...
 20-126 4.79e-54

N-terminal reticulon-homology domain of Reticulophagy regulators and similar proteins; This subfamily includes Reticulophagy regulators 1-3. Reticulophagy regulator 1 (RETREG1/FAM134B) is an endoplasmic reticulum (ER)-anchored autophagy receptor that regulates the size and shape of the ER. It regulates turnover of the ER by selective phagocytosis, mediating ER delivery into lysosomes through sequestration into autophagosomes. It promotes membrane remodeling and ER scission through its membrane bending activity, and targets the fragments into autophagosomes by interacting with ATG8 family modifier proteins such as MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. RETREG2/FAM134A and RETREG3/FAM134C has been shown to interact with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1. Members of this subfamily contain an N-terminal reticulon-homology domain (RHD) that shows sequence similarity to ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), an ER protein that has an important role in cell conduction and material transport. The RHD may function in inducing membrane curvature.


Pssm-ID: 411697  Cd Length: 192  Bit Score: 176.34  E-value: 4.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  20 SWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPL 99
Cdd:cd22558   86 SWTPIHPRLLSVPELCRHLAESWVSFTIFLQKLWQFRKQHPGKFCLLVCSFCTCLAVIGHYVPGVLLSYIILLSLLLWPL 165

                         90       100
                 ....*....|....*....|....*..
gi 767934462 100 FKCNDIGQKIYSKIKSVLLKLDFGIGE 126
Cdd:cd22558  166 VVYHRVPQKIYTKLEPVLMQLEYSMKI 192
Arl6IP1_RETR3-like cd21102
ADP-ribosylation factor-like protein 6-interacting protein 1, Reticulophagy regulator 3, and ...
 9-123 2.57e-48

ADP-ribosylation factor-like protein 6-interacting protein 1, Reticulophagy regulator 3, and similar proteins; This family contains ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1) and the N-terminal reticulon-homology domain (RHD) of Reticulophagy regulators 1-3. Arl6IP1 is an endoplasmic reticulum (ER) protein that has an important role in cell conduction and material transport. Arl6IP1, a tetraspan membrane protein, is an anti-apoptotic protein specific to multicellular organisms, and is a potential player in shaping the ER tubules in mammalian cells. In Drosophila, knockdown of the Arl6IP1 gene leads to progressive motor deficit. An Arl6IP1 variant has also been associated with hereditary spastic paraplegia (HSP), motor and sensory polyneuropathy, and acromutilation. Reticulophagy regulator 1 (RETREG1/FAM134B) is an endoplasmic reticulum (ER)-anchored autophagy receptor that regulates the size and shape of the ER. It regulates turnover of the ER by selective phagocytosis, mediating ER delivery into lysosomes through sequestration into autophagosomes. It promotes membrane remodeling and ER scission through its membrane bending activity, and targets the fragments into autophagosomes by interacting with ATG8 family modifier proteins such as MAP1LC3A, MAP1LC3B, GABARAP, GABARAPL1 and GABARAPL2. RETREG2/FAM134A and RETREG3/FAM134C has been shown to interact with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1. Arl6IP1 shows some sequence similarity to the RHD of reticulophagy regulators, which may function in inducing membrane curvature.


Pssm-ID: 411696  Cd Length: 178  Bit Score: 161.07  E-value: 2.57e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462   9 SPQLRSLQAEVsWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSY 88
Cdd:cd21102   62 GARSNKSTSEV-GFEFHPMLLSVPELCHNIAESWMSAVIFLLELLQLKEQNPGKFCLLVCVGLAVLAILGQYIPGVLLSY 140

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767934462  89 LLLLCAFLCPLFKCNDIGQKIY---SKIKSVLLKLDFG 123
Cdd:cd21102  141 LILTSLLLWPLLNYHGLIDKLYgmaKRLHPKLLKLDES 178
RETR3_RHD cd22562
N-terminal reticulon-homology domain of Reticulophagy regulator 3; Reticulophagy regulator 3 ...
 10-124 2.00e-32

N-terminal reticulon-homology domain of Reticulophagy regulator 3; Reticulophagy regulator 3 (RETR3 or RETREG3), also called FAM134C (family with sequence similarity 134, member C), mediates NRF1-enhanced neurite outgrowth. It interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1. RETREG3/FAM134C contains an N-terminal reticulon-homology domain (RHD) that shows sequence similarity to ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), an endoplasmic reticulum protein that has an important role in cell conduction and material transport. The RHD may function in inducing membrane curvature.


Pssm-ID: 411701  Cd Length: 192  Bit Score: 120.23  E-value: 2.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  10 PQLRSLQAEvSWEVINSKPDERPRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYL 89
Cdd:cd22562   77 ARPDELDNE-SWGFVHPRLLSVPELCHHVAEVWVSGTNFLRNLLLFKKQNPGKFCLLVCGVLTFLAVLGRYIPGLLLSYL 155

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 767934462  90 LLLCAFLCPLFKCNDIGQKIYSKIKSVLLKLDFGI 124
Cdd:cd22562  156 LLLFVLLWPLAVYHRLGQRIYVKLEPALQRLDFSV 190
RETR2_RHD cd22561
N-terminal reticulon-homology domain of Reticulophagy regulator 2; Reticulophagy regulator 2 ...
 32-122 2.37e-28

N-terminal reticulon-homology domain of Reticulophagy regulator 2; Reticulophagy regulator 2 (RETR2 or RETREG2), also called FAM134A (family with sequence similarity 134, member A), C2orf17, or MAG2, interacts with ATG8 family modifier proteins MAP1LC3A, MAP1LC3B, GABARAP, and GABARAPL1. RETREG2/FAM134A contains an N-terminal reticulon-homology domain (RHD) that shows sequence similarity to ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), an endoplasmic reticulum protein that has an important role in cell conduction and material transport. The RHD may function in inducing membrane curvature.


Pssm-ID: 411700  Cd Length: 199  Bit Score: 109.49  E-value: 2.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  32 PRLSHCIAESWMNFSIFLQEMSLFKQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYS 111
Cdd:cd22561  105 PELCHYLAESWLTFQLYLQELLQYKRQNPGQFCARVCSGCAVLAVLGHYVPGIMISYIVLLSVLLWPLVVYHELIQRMYT 184

                         90
                 ....*....|.
gi 767934462 112 KIKSVLLKLDF 122
Cdd:cd22561  185 RLEPVLMKLDY 195
HAD-SF-IA-v2 TIGR01493
Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid ...
 190-282 4.03e-03

Haloacid dehalogenase superfamily, subfamily IA, variant 2 with 3rd motif like haloacid dehalogenase; This model represents part of one structural subfamily of the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The superfamily is defined by the presence of three short catalytic motifs. The subfamilies are defined based on the location and the observed or predicted fold of a so-called 'capping domain', or the absence of such a domain. Subfamily I consists of sequences in which the capping domain is found in between the first and second catalytic motifs. Subfamily II consists of sequences in which the capping domain is found between the second and third motifs. Subfamily III sequences have no capping domain in either of these positions. The Subfamily IA and IB capping domains are predicted by PSI-PRED to consist of an alpha helical bundle. Subfamily I encompasses such a wide region of sequence space (the sequences are highly divergent) that representing it with a single model is impossible, resulting in an overly broad description which allows in many unrelated sequences. Subfamily IA and IB are separated based on an aparrent phylogenetic bifurcation. Subfamily IA is still too broad to model, but cannot be further subdivided into large chunks based on phylogenetic trees. Of the three motifs defining the HAD superfamily, the third has three variant forms: (1) hhhhsDxxx(x)D, (2) hhhhssxxx(x)D and (3) hhhhDDxxx(x)s where _s_ refers to a small amino acid and _h_ to a hydrophobic one. All three of these variants are found in subfamily IA. Individual models were made based on seeds exhibiting only one of the variants each. Variant 2 (this model) is distinctive of the type II haloacid dehalogenases, and nearly all of the sequences are also part of the HAD, type II equivalog model (TIGR01428). These three variant models were created with the knowledge that there will be overlap among them - this is by design and serves the purpose of eliminating the overlap with models of more distantly related HAD subfamilies caused by an overly broad single model.


Pssm-ID: 130557 [Multi-domain]  Cd Length: 175  Bit Score: 37.89  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767934462  190 EGYTPQTDTSDDLDRPSEEVFSR------DLSDFPslENGMGTNDEDELSLGLPTELKRKKEQLDSGHRPSKETQSAAGL 263
Cdd:TIGR01493  22 AAIAPEGGAFSDLWRAKQQEYSWrrslmgDRRAFP--EDTVRALRYIADRLGLDAEPKYGERLRDAYKNLPPWPDSAAAL 99

                          90       100
                  ....*....|....*....|
gi 767934462  264 -TLPLNSDQTFHLMSNLAGD 282
Cdd:TIGR01493 100 aRVAILSNASHWAFDQFAQQ 119
Arl6IP1 cd22559
ADP-ribosylation factor-like protein 6-interacting protein 1; ADP-ribosylation factor-like 6 ...
 56-120 6.62e-03

ADP-ribosylation factor-like protein 6-interacting protein 1; ADP-ribosylation factor-like 6 binding factor 1 (Arl6IP1 or Arl6ip-1), also called apoptotic regulator in the membrane of the endoplasmic reticulum (ARMER), is an endoplasmic reticulum (ER) protein that has an important role in cell conduction and material transport. Arl6IP1, a tetraspan membrane protein, is an anti-apoptotic protein specific to multicellular organisms, and is a potential player in shaping the ER tubules in mammalian cells. In neurons, Arl6IP1 has been associated with the regulation of glutamate, a major excitatory neurotransmitter in excitatory synapses. In Drosophila, knockdown of the Arl6IP1 gene leads to progressive motor deficit. An Arl6IP1 variant has also been associated with hereditary spastic paraplegia (HSP), motor and sensory polyneuropathy, and acromutilation. Arl6IP1 shows some sequence similarity to the reticulon-homology domain (RHD) of reticulophagy regulators, which may function in inducing membrane curvature.


Pssm-ID: 411698  Cd Length: 167  Bit Score: 36.85  E-value: 6.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767934462  56 KQQSPGKFCLLVCSVCTFFTILGSYIPGVILSYLLLLCAFLCPLFKCNDIGQKIYSKIKSVLLKL 120
Cdd:cd22559   97 KEEKPKMYFISVMGSLAAVAWIGNQVHNLLLTYLIVLFLLLLPGLKHHGILQKYIGMAKRVINKL 161
 
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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