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Conserved domains on  [gi|568973581|ref|XP_006533209|]
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testis-expressed protein 2 isoform X1 [Mus musculus]

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 ...
 824-1102 6.20e-84

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: 270.13  E-value: 6.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  824 WVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 902
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  903 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrpraycladsdeesssagsseeddppeptagdkqplpgaegyvgg 982
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  983 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRIWYGFRKPPYVELKAR 1062
Cdd:cd21675    99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568973581 1063 PKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIP 1102
Cdd:cd21675   147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 824-1102 6.20e-84

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: 270.13  E-value: 6.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  824 WVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 902
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  903 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrpraycladsdeesssagsseeddppeptagdkqplpgaegyvgg 982
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  983 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRIWYGFRKPPYVELKAR 1062
Cdd:cd21675    99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568973581 1063 PKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIP 1102
Cdd:cd21675   147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
 
Name Accession Description Interval E-value
SMP_TEX2 cd21675
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in testis-expressed ...
 824-1102 6.20e-84

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: 270.13  E-value: 6.20e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  824 WVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQAFKPYVD-HQGLWIDLEMSYN 902
Cdd:cd21675     1 WLNALLGRLFFDFLRTKYWKEFIKEKIQKKLSKIKLPSFLGEITVTDLDLGTSVPVISNPKLPSLDpDGGLWVDLDVSYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  903 GSFLMTLETKMNLTKLGKeplvealkvgeigkegcrpraycladsdeesssagsseeddppeptagdkqplpgaegyvgg 982
Cdd:cd21675    81 GGFSLTLETKLNLSKLKK-------------------------------------------------------------- 98

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  983 hrtskimrfvdkitkskyfqkatetefikkkiEEVSNTPLLLTVEVQECRGTLAVNIPPPPTDRIWYGFRKPPYVELKAR 1062
Cdd:cd21675    99 --------------------------------EKVSNVPLVLAVEVKSLSGTLRLNIKPPPSNRLWYGFREMPKLELEIE 146

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 568973581 1063 PKLGEREVTLVHVTEWIEKKLEQELQKVFVMPNMDDVYIP 1102
Cdd:cd21675   147 PVVGERQVTLPHVTNWIEKKLKEEIKESLVLPNMDDFPFP 186
SMP_SF cd21669
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain superfamily; The SMP ...
 842-1099 1.39e-09

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: 58.10  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  842 WSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKI--LQAFKPYVDHQGLWIDLEMSYNGSFLMTLETKMNLTKLG 919
Cdd:cd21669     1 LEQLIRESLQELLEEVKKPSFIESLELTEFTLGSNPPRIksVRVLDSPSSDLQLVLDLDLEYAGDFSVVLSAKLGGGGLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  920 Keplvealkvgeigkegcrpraycladsdeesssagsseeddppeptagdkqplpgaegyvgghrtskimrfvdkitksk 999
Cdd:cd21669    81 L------------------------------------------------------------------------------- 81

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581 1000 yfqkatetefikkkieevsntPLLLTVEVQECRGTLAVNI----PPPPTDRIWYGFRKPPYVELKARPKLGEREVTLVHV 1075
Cdd:cd21669    82 ---------------------PVPVSVSDLSLEGRLRVRLtllpEFPYVGALSISFVEPPDIDFSIRPLGGVDLMELPGL 140

                         250       260
                  ....*....|....*....|....
gi 568973581 1076 TEWIEKKLEQELQKVFVMPNMDDV 1099
Cdd:cd21669   141 SSWLEKLLTDALVELLVEPNRIVI 164
SMP_Mmm1 cd21671
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain found in maintenance of ...
 824-915 2.36e-04

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: 43.66  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  824 WVNALLGRIFWDFLGEKYWSDVVSKKIQMKLSKIKLPYFMNELTLTELDMGVAVPKILQA-FKPYVDHQGLWIDLEMSYN 902
Cdd:cd21671    23 WLNVLLAQILAQYRSDAEGDDNLLRKLEEALNGERKPSFLDPIKVTDLDLGDDFPRFSNArIRPSDDSGGLRAEIDIDYS 102

                          90
                  ....*....|...
gi 568973581  903 GSFLMTLETKMNL 915
Cdd:cd21671   103 DTISLGIDTSLLL 115
SMP_ESyt cd21670
synaptotagmin-like mitochondrial-lipid-binding protein (SMP) domain of the extended ...
 824-915 1.44e-03

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: 41.00  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568973581  824 WVNALLGRIfWDFLGEkYWSDVVSKKIQMKLSKIkLPYFMNELTLTELDMGVAVPKI--LQAFKPYVDHQGLWIDLEMSY 901
Cdd:cd21670     5 WLNKIIKQL-WPYINE-YVEKLLKEKIEPSIRAL-LPGPLKSFRFEKIDLGDKPPRIggVKVYTDNVDRDEIILDLDISY 81

                          90
                  ....*....|....*.
gi 568973581  902 NG--SFLMTLETKMNL 915
Cdd:cd21670    82 DGdaDIEVSVGTGIKA 97
 
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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