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Conserved domains on  [gi|568964362|ref|XP_006512436|]
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oxysterol-binding protein-related protein 10 isoform X4 [Mus musculus]

Protein Classification

oxysterol-binding protein-related protein( domain architecture ID 10352147)

oxysterol-binding protein-related protein is a lipid transporter involved in lipid counter-transport between the endoplasmic reticulum and the plasma membrane; similar to Arabidopsis thaliana oxysterol-binding protein-related proteins 2B and 1D

Gene Ontology:  GO:0005319|GO:0008289|GO:0008142
PubMed:  26715851|26784528|26811291|34999137|16709169|24196413|12573443
SCOP:  4000415
TCDB:  2.D.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
265-625 4.75e-103

Oxysterol-binding protein;


:

Pssm-ID: 460126  Cd Length: 366  Bit Score: 317.18  E-value: 4.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  265 HLISQLK--LGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVISFVEYYLTAFHEGRKGTlaKKPY 342
Cdd:pfam01237   1 SLWSILKknIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRV--KKPF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  343 NPIIGETFHCSWevpkdrvkskwtsphppisahehpmaddPSKSYklRFVAEQVSHHPPISCFYCECKEkrLCVNTHVWT 422
Cdd:pfam01237  79 NPLLGETFELVR----------------------------PDKGF--RFIAEQVSHHPPISAFHAESKG--WTFWGEIAP 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  423 KSKFMGMSVGVSMIGEGVLRLLDHGEEYVFTLPSAYARSILTV-PWVELGGKVNISCAKTGYSATVTFHTKPFYG-GKVH 500
Cdd:pfam01237 127 KSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTKPTTYVHNIIFGkLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  501 RVTAEVKhNPTNTIVCKAHGEWNGTLEFTYSNGETKVIDTTtlpvypkklrPLEKQGPMESRNLWQ-------------- 566
Cdd:pfam01237 207 EVTGKVY-DKNGKVLYTLSGKWNESLYIKDVSTGKKSSEDD----------SVEEQPDGESRLLWKagplpnayygftsf 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  567 -----EVT-----------------HYLRLGDIDAATEQKRRLEERQRVEERKRETLRTPWRPKYFIPEGDGWVYFNPLW 624
Cdd:pfam01237 276 avtlnELTdelgklpptdsrlrpdqRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKVKDDPVTGEEYW 355


                  .
gi 568964362  625 K 625
Cdd:pfam01237 356 K 356
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
 1-46 2.53e-18

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13291:

Pssm-ID: 473070  Cd Length: 107  Bit Score: 80.80  E-value: 2.53e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568964362   1 MLVVYSANGEMYKLRAADSKEKQLWVTQLRACAKYHMEMSSKTTPG 46
Cdd:cd13291   62 TFTVNAANGEMYKLRAADAKERQEWVNRLRAVAEHHTEAIAKSNSS 107
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
265-625 4.75e-103

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 317.18  E-value: 4.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  265 HLISQLK--LGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVISFVEYYLTAFHEGRKGTlaKKPY 342
Cdd:pfam01237   1 SLWSILKknIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRV--KKPF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  343 NPIIGETFHCSWevpkdrvkskwtsphppisahehpmaddPSKSYklRFVAEQVSHHPPISCFYCECKEkrLCVNTHVWT 422
Cdd:pfam01237  79 NPLLGETFELVR----------------------------PDKGF--RFIAEQVSHHPPISAFHAESKG--WTFWGEIAP 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  423 KSKFMGMSVGVSMIGEGVLRLLDHGEEYVFTLPSAYARSILTV-PWVELGGKVNISCAKTGYSATVTFHTKPFYG-GKVH 500
Cdd:pfam01237 127 KSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTKPTTYVHNIIFGkLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  501 RVTAEVKhNPTNTIVCKAHGEWNGTLEFTYSNGETKVIDTTtlpvypkklrPLEKQGPMESRNLWQ-------------- 566
Cdd:pfam01237 207 EVTGKVY-DKNGKVLYTLSGKWNESLYIKDVSTGKKSSEDD----------SVEEQPDGESRLLWKagplpnayygftsf 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  567 -----EVT-----------------HYLRLGDIDAATEQKRRLEERQRVEERKRETLRTPWRPKYFIPEGDGWVYFNPLW 624
Cdd:pfam01237 276 avtlnELTdelgklpptdsrlrpdqRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKVKDDPVTGEEYW 355


                  .
gi 568964362  625 K 625
Cdd:pfam01237 356 K 356
PH_ORP10_ORP11 cd13291
Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin ...
 1-46 2.53e-18

Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology (PH) domain; Human ORP10 is involvedt in intracellular transport or organelle positioning and is proposed to function as a regulator of cellular lipid metabolism. Human ORP11 localizes at the Golgi-late endosome interface and is thought to form a dimer with ORP9 functioning as an intracellular lipid sensor or transporter. Both ORP10 and ORP11 contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270106  Cd Length: 107  Bit Score: 80.80  E-value: 2.53e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568964362   1 MLVVYSANGEMYKLRAADSKEKQLWVTQLRACAKYHMEMSSKTTPG 46
Cdd:cd13291   62 TFTVNAANGEMYKLRAADAKERQEWVNRLRAVAEHHTEAIAKSNSS 107
 
Name Accession Description Interval E-value
Oxysterol_BP pfam01237
Oxysterol-binding protein;
265-625 4.75e-103

Oxysterol-binding protein;


Pssm-ID: 460126  Cd Length: 366  Bit Score: 317.18  E-value: 4.75e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  265 HLISQLK--LGMDLTKVVLPTFILEKRSLLEMYADFMAHPDLLLAITAGATPEERVISFVEYYLTAFHEGRKGTlaKKPY 342
Cdd:pfam01237   1 SLWSILKknIGKDLSKITMPVFFNEPLSLLQRLAEDLEYSELLDKAAEEDDPLERMLYVAAFAVSGYSSTRRRV--KKPF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  343 NPIIGETFHCSWevpkdrvkskwtsphppisahehpmaddPSKSYklRFVAEQVSHHPPISCFYCECKEkrLCVNTHVWT 422
Cdd:pfam01237  79 NPLLGETFELVR----------------------------PDKGF--RFIAEQVSHHPPISAFHAESKG--WTFWGEIAP 126

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  423 KSKFMGMSVGVSMIGEGVLRLLDHGEEYVFTLPSAYARSILTV-PWVELGGKVNISCAKTGYSATVTFHTKPFYG-GKVH 500
Cdd:pfam01237 127 KSKFWGKSLEVNPEGTVHLTLKKTGEHYTWTKPTTYVHNIIFGkLWVEHYGEMTITNHTTGYKAVLEFKPKGYFSsGRSN 206

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  501 RVTAEVKhNPTNTIVCKAHGEWNGTLEFTYSNGETKVIDTTtlpvypkklrPLEKQGPMESRNLWQ-------------- 566
Cdd:pfam01237 207 EVTGKVY-DKNGKVLYTLSGKWNESLYIKDVSTGKKSSEDD----------SVEEQPDGESRLLWKagplpnayygftsf 275

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568964362  567 -----EVT-----------------HYLRLGDIDAATEQKRRLEERQRVEERKRETLRTPWRPKYFIPEGDGWVYFNPLW 624
Cdd:pfam01237 276 avtlnELTdelgklpptdsrlrpdqRALENGDIDEAEEEKLRLEEKQRARRKEREEKGEEWKPRWFKKVKDDPVTGEEYW 355


                  .
gi 568964362  625 K 625
Cdd:pfam01237 356 K 356
PH_ORP10_ORP11 cd13291
Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin ...
 1-46 2.53e-18

Human Oxysterol binding protein (OSBP) related proteins 10 and 11 (ORP10 and ORP11) Pleckstrin homology (PH) domain; Human ORP10 is involvedt in intracellular transport or organelle positioning and is proposed to function as a regulator of cellular lipid metabolism. Human ORP11 localizes at the Golgi-late endosome interface and is thought to form a dimer with ORP9 functioning as an intracellular lipid sensor or transporter. Both ORP10 and ORP11 contain a N-terminal PH domain, a FFAT motif (two phenylalanines in an acidic tract), and a C-terminal OSBP-related domain. Oxysterol binding proteins are a multigene family that is conserved in yeast, flies, worms, mammals and plants. In general OSBPs and ORPs have been found to be involved in the transport and metabolism of cholesterol and related lipids in eukaryotes. They all contain a C-terminal oxysterol binding domain, and most contain an N-terminal PH domain. OSBP PH domains bind to membrane phosphoinositides and thus likely play an important role in intracellular targeting. They are members of the oxysterol binding protein (OSBP) family which includes OSBP, OSBP-related proteins (ORP), Goodpasture antigen binding protein (GPBP), and Four phosphate adaptor protein 1 (FAPP1). They have a wide range of purported functions including sterol transport, cell cycle control, pollen development and vessicle transport from Golgi recognize both PI lipids and ARF proteins. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270106  Cd Length: 107  Bit Score: 80.80  E-value: 2.53e-18
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 568964362   1 MLVVYSANGEMYKLRAADSKEKQLWVTQLRACAKYHMEMSSKTTPG 46
Cdd:cd13291   62 TFTVNAANGEMYKLRAADAKERQEWVNRLRAVAEHHTEAIAKSNSS 107
 
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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