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Conserved domains on  [gi|688545034|ref|XP_009298078|]
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testis-expressed protein 2 isoform X1 [Danio rerio]

Protein Classification

SMP domain-containing protein( domain architecture ID 17749740)

SMP (synaptotagmin-like mitochondrial-lipid-binding) domain-containing protein contains a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers

Gene Ontology:  GO:0006869|GO:0008289|GO:0016020
PubMed:  24847877|31002947|26686281

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 771-1040 3.23e-88

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: 281.30  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  771 WINALLGRMFWDFLREKYWADVVSKKIQKKLSKIRLPYFMNELTLTELDMGISIPKILSSSKPSVD-HKGLWFDLEISYN 849
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  850 GSFLMTLETKMNLTRLGKegeglgeqgkegsrprtyfladsdeesssagssdeedtvevpeipgvegfvgghkpskimrf 929
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  930 vdkiakskyfqkatetefikkkiEEVSNTPLLLTVEVQECQGTLAVNIPPPPTDRIWYGFRRPPRLELKARPKLGEREVT 1009
Cdd:cd21675    99 -----------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIEPVVGERQVT 155

                         250       260       270
                  ....*....|....*....|....*....|.
gi 688545034 1010 FAHVTDWIEKKLDQEFQKIFVMPNMDDVWLP 1040
Cdd:cd21675   156 LPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 771-1040 3.23e-88

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: 281.30  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  771 WINALLGRMFWDFLREKYWADVVSKKIQKKLSKIRLPYFMNELTLTELDMGISIPKILSSSKPSVD-HKGLWFDLEISYN 849
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  850 GSFLMTLETKMNLTRLGKegeglgeqgkegsrprtyfladsdeesssagssdeedtvevpeipgvegfvgghkpskimrf 929
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  930 vdkiakskyfqkatetefikkkiEEVSNTPLLLTVEVQECQGTLAVNIPPPPTDRIWYGFRRPPRLELKARPKLGEREVT 1009
Cdd:cd21675    99 -----------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIEPVVGERQVT 155

                         250       260       270
                  ....*....|....*....|....*....|.
gi 688545034 1010 FAHVTDWIEKKLDQEFQKIFVMPNMDDVWLP 1040
Cdd:cd21675   156 LPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 771-1040 3.23e-88

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: 281.30  E-value: 3.23e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  771 WINALLGRMFWDFLREKYWADVVSKKIQKKLSKIRLPYFMNELTLTELDMGISIPKILSSSKPSVD-HKGLWFDLEISYN 849
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  850 GSFLMTLETKMNLTRLGKegeglgeqgkegsrprtyfladsdeesssagssdeedtvevpeipgvegfvgghkpskimrf 929
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  930 vdkiakskyfqkatetefikkkiEEVSNTPLLLTVEVQECQGTLAVNIPPPPTDRIWYGFRRPPRLELKARPKLGEREVT 1009
Cdd:cd21675    99 -----------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIEPVVGERQVT 155

                         250       260       270
                  ....*....|....*....|....*....|.
gi 688545034 1010 FAHVTDWIEKKLDQEFQKIFVMPNMDDVWLP 1040
Cdd:cd21675   156 LPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 789-1037 4.32e-10

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: 59.64  E-value: 4.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  789 WADVVSKKIQKKLSKIRLPYFMNELTLTELDMGISIPKILS--SSKPSVDHKGLWFDLEISYNGSFLMTLETKMNLTRLG 866
Cdd:cd21669     1 LEQLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIKSvrVLDSPSSDLQLVLDLDLEYAGDFSVVLSAKLGGGGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  867 Kegeglgeqgkegsrprtyfladsdeesssagssdeedtvevpeipgvegfvgghkpskimrfvdkiakskyfqkatete 946
Cdd:cd21669    81 L------------------------------------------------------------------------------- 81

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  947 fikkkieevsntPLLLTVEVQECQGTLAVNI----PPPPTDRIWYGFRRPPRLELKARPKLGEREVTFAHVTDWIEKKLD 1022
Cdd:cd21669    82 ------------PVPVSVSDLSLEGRLRVRLtllpEFPYVGALSISFVEPPDIDFSIRPLGGVDLMELPGLSSWLEKLLT 149

                         250
                  ....*....|....*
gi 688545034 1023 QEFQKIFVMPNMDDV 1037
Cdd:cd21669   150 DALVELLVEPNRIVI 164
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 759-862 1.85e-07

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: 52.91  E-value: 1.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  759 PESCEqsaeteaWINALLGRmFWDFLREKYWA-DVVSKKIQKKLSKIRLPYFMNELTLTELDMGISIPKILS-SSKPSVD 836
Cdd:cd21671    18 PESLD-------WLNVLLAQ-ILAQYRSDAEGdDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFSNaRIRPSDD 89

                          90       100
                  ....*....|....*....|....*.
gi 688545034  837 HKGLWFDLEISYNGSFLMTLETKMNL 862
Cdd:cd21671    90 SGGLRAEIDIDYSDTISLGIDTSLLL 115
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 767-862 3.76e-06

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: 48.32  E-value: 3.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  767 ETEAWINALLGRMfWDFLREkYWADVVSKKIQKKLSKIrLPYFMNELTLTELDMGISIPKI--LSSSKPSVDHKGLWFDL 844
Cdd:cd21670     1 ERAEWLNKIIKQL-WPYINE-YVEKLLKEKIEPSIRAL-LPGPLKSFRFEKIDLGDKPPRIggVKVYTDNVDRDEIILDL 77

                          90       100
                  ....*....|....*....|
gi 688545034  845 EISYNG--SFLMTLETKMNL 862
Cdd:cd21670    78 DISYDGdaDIEVSVGTGIKA 97
SMP_TCB cd21678
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the tricalbin ...
 767-848 1.18e-03

synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in the tricalbin (TCB) family; The tricalbin (TCB) family includes Saccharomyces cerevisiae TCB1-3 and similar proteins. They may play a role in membrane trafficking. This model corresponds to the SMP domain of TCB family proteins, which may be implicated in lipid transport.


Pssm-ID: 439234  Cd Length: 203  Bit Score: 41.39  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  767 ETEAWINALLGRmFWDFLrEKYWADVVSKKIQKKLSKIrLPYFMNELTLTELDMGISIPKILS-SSKPSVDHKGLWFDLE 845
Cdd:cd21678     1 ESVEWLNYFLQK-FWLIY-EPVLSETIVTNVNPVLAEN-CPSFLDSLRLTEFTLGTKAPRIEGvRTYPKTEDDVVVMDWE 77


                  ...
gi 688545034  846 ISY 848
Cdd:cd21678    78 FSF 80
SMP_PDZD8 cd21674
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in PDZ ...
 767-867 5.12e-03

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: 39.46  E-value: 5.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688545034  767 ETEAWINALLGRMFW---DFLREKYWadvVSKKIQKK----LSKIRLPYFMNELTLTELDMGISIPKI----LSSSKPSV 835
Cdd:cd21674     1 ESCVWLNLLFQFLFQelrDTKRVRRW---VTKKLNVEfeelLKTKTAGKFLESITVRDLSLGTSFPVIknvtVINVKLSE 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 688545034  836 DHKG---LWFDLEISYNGSFLMTLETKMnltRLGK 867
Cdd:cd21674    78 DEDVpeeLDLALDLEYSGGFQLAIDVDL---VFGK 109
 
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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