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Conserved domains on  [gi|1907165964|ref|XP_036021359|]
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transmembrane protein 214 isoform X1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
TMEM214 super family cl10848
TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane ...
1-378 6.58e-127

TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane family 214, from eukaryotes. The family is localized on the endoplasmic reticulum where it recruits procaspase 4 to the ER and subsequently allows this to be cleaved to caspase 4 so leading to apoptosis.


The actual alignment was detected with superfamily member pfam10151:

Pssm-ID: 462966  Cd Length: 661  Bit Score: 379.85  E-value: 6.58e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964   1 MHPNLTKGFGMIGPKDFFPLLDFAYMPNNSLSPSLQEQLCQLFPRLKVLAFGAKPeSSLHTYFPSFLSRATPSCPAAMKK 80
Cdd:pfam10151 295 GHANLTKGFGLLGPKEFFPLLDFANMPKNNLSKSLQEQLKRSYPRLKVLYFGAKP-STLHTYFPSLLSRATPKCPDDMKK 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964  81 ELLASLTQCLTVDPLSTSVWRQLYPKHLSQSSLLLEHLLKSWEHIPKKAR-KSLQETIQSLKVTNQELLKKGSgGSEHVL 159
Cdd:pfam10151 374 ELIESLTECLLSDPDCLSVWRQLYTKHLYQSSLLLNHIDSNWNSLPKKLQsKSLKETLQSFKVTNEELKKSKD-SDQDLD 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 160 TCDTACKGLLQRARGPRP--PWARLFLLLLVFAVGFLCHDLRSNSSLQASLTGRLLRSSGLLPVGQQVCARLSSYSLQSY 237
Cdd:pfam10151 453 DCNKLCQNLLEKMTAQQRcfPWTKGSLVLLVFIAGFLAYDTRSHGSFEASATGKVLKNSGVLPHSQQAWYKIMSYSARGY 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 238 NWLQETLPACGSHLLAVVQPSLQLAWTHIYAIFSFLSAHCASYLACFSDSLAGFFQRVQ--LPEALQQL-FHALKELLLL 314
Cdd:pfam10151 533 SWLETNSPHYYSATVTVCGPYIKLAGDVTKIARNAASKIYQNGLGYIEEKWPVVIKTIEqyLPGSVDQIeSFASGALDKA 612
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907165964 315 FCHSVLLPTW--HLLLAalaqvqehcheacrGDVTWDCIKTQLSRAAQWTwlclQDVTVAFLDWAL 378
Cdd:pfam10151 613 IESYSASLAYlkELVLV--------------GEVSPENLQNHALSALNST----QNTASEYYNWFH 660
 
Name Accession Description Interval E-value
TMEM214 pfam10151
TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane ...
1-378 6.58e-127

TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane family 214, from eukaryotes. The family is localized on the endoplasmic reticulum where it recruits procaspase 4 to the ER and subsequently allows this to be cleaved to caspase 4 so leading to apoptosis.


Pssm-ID: 462966  Cd Length: 661  Bit Score: 379.85  E-value: 6.58e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964   1 MHPNLTKGFGMIGPKDFFPLLDFAYMPNNSLSPSLQEQLCQLFPRLKVLAFGAKPeSSLHTYFPSFLSRATPSCPAAMKK 80
Cdd:pfam10151 295 GHANLTKGFGLLGPKEFFPLLDFANMPKNNLSKSLQEQLKRSYPRLKVLYFGAKP-STLHTYFPSLLSRATPKCPDDMKK 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964  81 ELLASLTQCLTVDPLSTSVWRQLYPKHLSQSSLLLEHLLKSWEHIPKKAR-KSLQETIQSLKVTNQELLKKGSgGSEHVL 159
Cdd:pfam10151 374 ELIESLTECLLSDPDCLSVWRQLYTKHLYQSSLLLNHIDSNWNSLPKKLQsKSLKETLQSFKVTNEELKKSKD-SDQDLD 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 160 TCDTACKGLLQRARGPRP--PWARLFLLLLVFAVGFLCHDLRSNSSLQASLTGRLLRSSGLLPVGQQVCARLSSYSLQSY 237
Cdd:pfam10151 453 DCNKLCQNLLEKMTAQQRcfPWTKGSLVLLVFIAGFLAYDTRSHGSFEASATGKVLKNSGVLPHSQQAWYKIMSYSARGY 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 238 NWLQETLPACGSHLLAVVQPSLQLAWTHIYAIFSFLSAHCASYLACFSDSLAGFFQRVQ--LPEALQQL-FHALKELLLL 314
Cdd:pfam10151 533 SWLETNSPHYYSATVTVCGPYIKLAGDVTKIARNAASKIYQNGLGYIEEKWPVVIKTIEqyLPGSVDQIeSFASGALDKA 612
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907165964 315 FCHSVLLPTW--HLLLAalaqvqehcheacrGDVTWDCIKTQLSRAAQWTwlclQDVTVAFLDWAL 378
Cdd:pfam10151 613 IESYSASLAYlkELVLV--------------GEVSPENLQNHALSALNST----QNTASEYYNWFH 660
 
Name Accession Description Interval E-value
TMEM214 pfam10151
TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane ...
1-378 6.58e-127

TMEM214, C-terminal, caspase 4 activator; This is the N-terminal domain of transmembrane family 214, from eukaryotes. The family is localized on the endoplasmic reticulum where it recruits procaspase 4 to the ER and subsequently allows this to be cleaved to caspase 4 so leading to apoptosis.


Pssm-ID: 462966  Cd Length: 661  Bit Score: 379.85  E-value: 6.58e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964   1 MHPNLTKGFGMIGPKDFFPLLDFAYMPNNSLSPSLQEQLCQLFPRLKVLAFGAKPeSSLHTYFPSFLSRATPSCPAAMKK 80
Cdd:pfam10151 295 GHANLTKGFGLLGPKEFFPLLDFANMPKNNLSKSLQEQLKRSYPRLKVLYFGAKP-STLHTYFPSLLSRATPKCPDDMKK 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964  81 ELLASLTQCLTVDPLSTSVWRQLYPKHLSQSSLLLEHLLKSWEHIPKKAR-KSLQETIQSLKVTNQELLKKGSgGSEHVL 159
Cdd:pfam10151 374 ELIESLTECLLSDPDCLSVWRQLYTKHLYQSSLLLNHIDSNWNSLPKKLQsKSLKETLQSFKVTNEELKKSKD-SDQDLD 452
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 160 TCDTACKGLLQRARGPRP--PWARLFLLLLVFAVGFLCHDLRSNSSLQASLTGRLLRSSGLLPVGQQVCARLSSYSLQSY 237
Cdd:pfam10151 453 DCNKLCQNLLEKMTAQQRcfPWTKGSLVLLVFIAGFLAYDTRSHGSFEASATGKVLKNSGVLPHSQQAWYKIMSYSARGY 532
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907165964 238 NWLQETLPACGSHLLAVVQPSLQLAWTHIYAIFSFLSAHCASYLACFSDSLAGFFQRVQ--LPEALQQL-FHALKELLLL 314
Cdd:pfam10151 533 SWLETNSPHYYSATVTVCGPYIKLAGDVTKIARNAASKIYQNGLGYIEEKWPVVIKTIEqyLPGSVDQIeSFASGALDKA 612
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907165964 315 FCHSVLLPTW--HLLLAalaqvqehcheacrGDVTWDCIKTQLSRAAQWTwlclQDVTVAFLDWAL 378
Cdd:pfam10151 613 IESYSASLAYlkELVLV--------------GEVSPENLQNHALSALNST----QNTASEYYNWFH 660
 
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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