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Conserved domains on  [gi|767961568|ref|XP_011537568|]
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PDZ domain-containing protein 8 isoform X3 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 93-296 3.51e-107

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.


:

Pssm-ID: 439230  Cd Length: 191  Bit Score: 312.56  E-value: 3.51e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568  93 ETCYFLNATILFLFRELRDTALTRRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPSATG 172
Cdd:cd21674    1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 173 epdgpegealpaaCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRLVFTRVPFTHWFFSFVEDPLID 252
Cdd:cd21674   81 -------------VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIE 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767961568 253 FEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPNYKIRFKPFF 296
Cdd:cd21674  148 FDVESRFEGRQLPQLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191
 
Name Accession Description Interval E-value
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 93-296 3.51e-107

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.


Pssm-ID: 439230  Cd Length: 191  Bit Score: 312.56  E-value: 3.51e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568  93 ETCYFLNATILFLFRELRDTALTRRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPSATG 172
Cdd:cd21674    1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 173 epdgpegealpaaCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRLVFTRVPFTHWFFSFVEDPLID 252
Cdd:cd21674   81 -------------VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIE 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767961568 253 FEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPNYKIRFKPFF 296
Cdd:cd21674  148 FDVESRFEGRQLPQLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191
 
Name Accession Description Interval E-value
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 93-296 3.51e-107

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ domain-containing protein 8 (PDZD8) and similar proteins; PDZ domain-containing protein 8 (PDZD8), also called Sarcoma antigen NY-SAR-84/NY-SAR-104, is a molecular tethering protein that connects endoplasmic reticulum (ER) and mitochondria membranes. PDZD8-dependent endoplasmic reticulum-mitochondria membrane tethering is essential for ER-mitochondria Ca(2+) transfer. In neurons, PDZD8 is involved in the regulation of dendritic Ca(2+) dynamics by regulating mitochondrial Ca(2+) uptake in neurons. It plays an indirect role in the regulation of cell morphology and cytoskeletal organization. PDZD8 is also a novel Gag-interacting factor that promotes retroviral infection. It may act as a novel moesin-interacting cytoskeletal regulatory protein that suppresses infection by herpes simplex virus type 1 (HSV1). This model corresponds to the SMP domain of PDZD8, which may be implicated in lipid transport.


Pssm-ID: 439230  Cd Length: 191  Bit Score: 312.56  E-value: 3.51e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568  93 ETCYFLNATILFLFRELRDTALTRRWVTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPSATG 172
Cdd:cd21674    1 ESCVWLNLLFQFLFQELRDTKRVRRWVTKKLNVEFEELLKTKTAGKFLESITVRDLSLGTSFPVIKNVTVINVKLSEDED 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 173 epdgpegealpaaCPEELAFEAEVEYNGGFHLAIDVDLVFGKSAYLFVKLSRVVGRLRLVFTRVPFTHWFFSFVEDPLID 252
Cdd:cd21674   81 -------------VPEELDLALDLEYSGGFQLAIDVDLVFGKSAYLSIKVVKLSGRLRLQFSRLPYTHWSFSFYEEPIIE 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 767961568 253 FEVRSQFEGRPMPQLTSIIVNQLKKIIKRKHTLPNYKIRFKPFF 296
Cdd:cd21674  148 FDVESRFEGRQLPQLTSLIINQIRRVIRKKHTLPNYKIRYKPFF 191
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 119-287 1.57e-22

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP domain is a lipid transport domain found in phospholipid transfer proteins such as synaptotagmin family proteins, tricalbin (TCB) family proteins, maintenance of mitochondrial morphology protein 1 (MMM1), mitochondrial distribution and morphology protein 12 (MDM12), mitochondrial distribution and morphology protein 34 (MDM34), PDZ domain-containing protein 8 (PDZD8), testis-expressed protein 2 (TEX2), meiotically up-regulated gene 190 protein (Mug190), C2 domain-containing protein 2 (C2CD2) and C2 domain-containing protein 2-like (C2CD2L). The SMP domain belongs to a superfamily of lipid/hydrophobic ligand-binding domains called TULIP (tubular lipid-binding proteins). It adopts a TULIP fold with two alpha helices and a highly curved antiparallel beta sheet forming a cornucopia-like structure.


Pssm-ID: 439225  Cd Length: 165  Bit Score: 92.77  E-value: 1.57e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 119 VTKKIKVEFEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRLVRPVVPsatgepdgpegealpaacPEELAFEAEVEY 198
Cdd:cd21669    1 LEQLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIKSVRVLDSPSS------------------DLQLVLDLDLEY 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 199 NGGFHLAIDVDLV---FGKSAYLFVKLSRVVGRLRLVFTRVP----FTHWFFSFVEDPLIDFEVRSQFEGRPM--PQLTS 269
Cdd:cd21669   63 AGDFSVVLSAKLGgggLGLPVPVSVSDLSLEGRLRVRLTLLPefpyVGALSISFVEPPDIDFSIRPLGGVDLMelPGLSS 142

                        170
                 ....*....|....*...
gi 767961568 270 IIVNQLKKIIKRKHTLPN 287
Cdd:cd21669  143 WLEKLLTDALVELLVEPN 160
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 98-287 1.46e-16

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed protein 2 (TEX2) and similar proteins; testis-expressed protein 2 (TEX2), also called transmembrane protein 96 (TMEM96), is a transmembrane protein with uncharacterized biological function. Diseases associated with TEX2 include Wernicke-Korsakoff Syndrome. This model corresponds to the SMP domain of TEX2, which may be implicated in lipid transport.


Pssm-ID: 439231  Cd Length: 186  Bit Score: 77.15  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568  98 LNATILFLFRELRDTALTRRWVTKKIkvefeellQTKTAgRL-----LEGLSLRDVFLGETVPFIKTIRLVrpvvpsaTG 172
Cdd:cd21675    2 LNALLGRLFFDFLRTKYWKEFIKEKI--------QKKLS-KIklpsfLGEITVTDLDLGTSVPVISNPKLP-------SL 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 173 EPDGpegealpaacpeELAFEAEVEYNGGFHLAID--VDLVFGKSAY-------LFVKLSRVVGRLRLVFTRVPFTHWFF 243
Cdd:cd21675   66 DPDG------------GLWVDLDVSYRGGFSLTLEtkLNLSKLKKEKvsnvplvLAVEVKSLSGTLRLNIKPPPSNRLWY 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767961568 244 SFVEDPLIDFEVRSQFEGR--PMPQLTSIIVNQLKKIIKRKHTLPN 287
Cdd:cd21675  134 GFREMPKLELEIEPVVGERqvTLPHVTNWIEKKLKEEIKESLVLPN 179
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 89-289 1.15e-06

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of mitochondrial morphology protein 1 (Mmm1) and similar proteins; Maintenance of mitochondrial morphology protein 1 (Mmm1), also called mitochondrial outer membrane protein Mmm1, or yeast mitochondrial escape protein 6 (YME6), is a mitochondrial outer membrane protein essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids. It is a component of the ER-mitochondrion encounter structure/ mitochondrial distribution and morphology (ERMES/Mdm) complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The Mdm12-Mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The Mdm10-Mdm12-Mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the Mdm12-Mmm1 complex. This model corresponds to the SMP domain of Mmm1, which may be implicated in lipid transport.


Pssm-ID: 439227  Cd Length: 216  Bit Score: 49.06  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568  89 PPTRETCYFLNATILFLFRELRDTALTRRWVTKKIkvefEELLQTKTAGRLLEGLSLRDVFLGETVPFIKTIRlVRPVvp 168
Cdd:cd21671   15 EHPPESLDWLNVLLAQILAQYRSDAEGDDNLLRKL----EEALNGERKPSFLDPIKVTDLDLGDDFPRFSNAR-IRPS-- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 169 satgePDGPEGEAlpaacpeelafEAEVEYNGGFHLAIDVDLVFG----KSAYL----FVKLSRVVGRLRLVFTRVPFTH 240
Cdd:cd21671   88 -----DDSGGLRA-----------EIDIDYSDTISLGIDTSLLLNypkpRFASLpvslSVSLVRFSGTLTIELPSPSSPG 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 767961568 241 WF--FSFVEDPLIDFEVRSQFEGRPM----PQLTSIIVNQLKKIIKRKHTLPNYK 289
Cdd:cd21671  152 PTlsFSLLPDFRLDLKVSSLIGSRAKlqdvPKLHSLIESRLRRWFADRCVEPNFW 206
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 116-293 4.85e-05

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended synaptotagmin (E-Syt) family; The extended synaptotagmin (E-Syt) family includes a group of Ca2+-regulated intrinsic membrane proteins, such as E-Syt1, E-Syt2 and E-Syt3. They are composed of an N-terminal endoplasmic reticulum (ER)-membrane anchor, a central SMP-domain, and five (E-Syt1) or three C-terminal cytoplasmic C2-domains (E-Syt2 and E-Syt3). The ER-membrane anchor and C2 domains are required for tethering, while the SMP domain is a lipid-binding domain that links the ER with other lipid bilayer-membranes within the cell. This model corresponds to the SMP domain, which has a beta-barrel structure like protein modules in the tubular-lipid-binding (TULIP) superfamily. It dimerizes to form an approximately 90-Angstrom-long cylinder traversed by a channel lined entirely with hydrophobic residues. The following two C2 domains then form arched structures flexibly linked to the SMP domain.


Pssm-ID: 439226  Cd Length: 177  Bit Score: 43.70  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 116 RRWVTKKIKVEFEELLQtKTAGRLLEGLSLRDVFLGETVPFIKTIRlvrpVVPSATGepdgpegealpaacPEELAFEAE 195
Cdd:cd21670   18 NEYVEKLLKEKIEPSIR-ALLPGPLKSFRFEKIDLGDKPPRIGGVK----VYTDNVD--------------RDEIILDLD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 196 VEYNGgfhlaiDVDLVFGKSAYLFVKLSRV--VGRLRLVFT----RVPFTHWF-FSFVEDPLIDFEvrsqFEG----RPM 264
Cdd:cd21670   79 ISYDG------DADIEVSVGTGIKAGIKDIqlRGTLRIVLKpllsELPLVGGVqIFFLNPPEIDFD----LTGlanlLDI 148

                        170       180
                 ....*....|....*....|....*....
gi 767961568 265 PQLTSIIVNQLKKIIKRKHTLPNyKIRFK 293
Cdd:cd21670  149 PGLSNLLRKIIVDQIASFLVLPN-RITIP 176
SMP_SYT cd21677
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the synaptotagmin ...
 187-287 9.03e-03

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the synaptotagmin family, mostly plants; The synaptotagmin family includes Arabidopsis thaliana synaptotagmins (AtSYT1-5) and similar proteins. AtSYT1, also called NTMC2T1.1, or synaptotagmin A (SYTA), plays an important role in maintaining plasma membrane integrity during freezing and osmotic stresses. It may function in membrane resealing during calcium-dependent freezing tolerance. It regulates endocytosis and endosome recycling at the plasma membrane and cell-to-cell trafficking of cabbage leaf curl virus (CaLCuV) and tobacco mosaic virus (TMV) movement proteins via plasmodesmata. AtSYT2, also called NTMC2T1.2, or synaptotagmin B (SYTB), may play an important role in regulating an unconventional protein trafficking from the cytosol to the extracellular matrix. AtSYT3 (also called NTMC2T1.3, or synaptotagmin C, or SYTC), AtSYT4 (also called NTMC2T2.2, or synaptotagmin D, or SYTD) and AtSYT5 (also called NTMC2T2.1, or synaptotagmin E, or SYTE) may also be involved in membrane trafficking. This model corresponds to the SMP domain of SYT family proteins, which may be implicated in lipid transport.


Pssm-ID: 439233  Cd Length: 189  Bit Score: 36.76  E-value: 9.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961568 187 PEELAFEAEVEYNGGFHLAIDVDLVFGksAYLFVKLSR--VVGRLRLVFTrvPFTHWF-------FSFVEDPLIDFEVRs 257
Cdd:cd21677   77 EDEVILDVDFRWAGDPDIVLAVKLLPG--LSLPVQVKDlqLSGTVRITLK--PLVDELpcfgavsVSLVEKPVVDFDLK- 151

                         90       100       110
                 ....*....|....*....|....*....|...
gi 767961568 258 qFEGRP---MPQLTSIIVNQLKKIIKRKHTLPN 287
Cdd:cd21677  152 -LLGGDdmaLPGLKSWLDSFIRDALLDMLVWPK 183
 
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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