NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1276317729|ref|NP_001344813|]
View 

transmembrane protein 181 isoform 2 [Mus musculus]

Protein Classification

TMEM181/wntless family protein( domain architecture ID 10535260)

TMEM181/wntless family protein may be involved in the secretion of Wnt proteins from signaling cells

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
168-463 1.86e-97

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


:

Pssm-ID: 461980  Cd Length: 294  Bit Score: 296.47  E-value: 1.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 168 KCAEIIVAHLGYLNYTQYRVTVGFEHL-----NQPIKDMNFTWKTYNPAFSRLEIWFHFVFVVLTFIVICLFVHSLRKFS 242
Cdd:pfam06664   1 NCDPITLFELGSLDYSYYLINIRFPNLeefhdNYDGKELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFLFSLRKLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 243 MRDWGIEQKWMSVLLALLLLYNDPFFPLSFLVNSWFPGMLDDFFQSLFLCALLLFWLCVYHGIRV-QGERKCLTFYLPKF 321
Cdd:pfam06664  81 SRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFFDHLRDeQNERKSLSFYLPKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 322 FIVGLLWLASVTLGIWQTFNELNDPMYQYrVDTGNFQGMKVFFMVVAAVYILYLLFLIVRACSELRH--MPYVDLRLKFL 399
Cdd:pfam06664 161 LLVGVLWLSLLILDIWERGVQLKDPFYSI-WDSELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSkrMPEGDIRFKFL 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276317729 400 ---TALTFVVLVISIVILYLRFGAQVLqdnfvaelsahyQNSAEFLSFYGLLNFYLYTLAFVYSPSK 463
Cdd:pfam06664 240 mllTLLCAAVTVIFIILGQFSFGQNFN------------STSAFFLGFYGMLNLYVYTLAYLYAPSH 294
 
Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
168-463 1.86e-97

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


Pssm-ID: 461980  Cd Length: 294  Bit Score: 296.47  E-value: 1.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 168 KCAEIIVAHLGYLNYTQYRVTVGFEHL-----NQPIKDMNFTWKTYNPAFSRLEIWFHFVFVVLTFIVICLFVHSLRKFS 242
Cdd:pfam06664   1 NCDPITLFELGSLDYSYYLINIRFPNLeefhdNYDGKELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFLFSLRKLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 243 MRDWGIEQKWMSVLLALLLLYNDPFFPLSFLVNSWFPGMLDDFFQSLFLCALLLFWLCVYHGIRV-QGERKCLTFYLPKF 321
Cdd:pfam06664  81 SRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFFDHLRDeQNERKSLSFYLPKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 322 FIVGLLWLASVTLGIWQTFNELNDPMYQYrVDTGNFQGMKVFFMVVAAVYILYLLFLIVRACSELRH--MPYVDLRLKFL 399
Cdd:pfam06664 161 LLVGVLWLSLLILDIWERGVQLKDPFYSI-WDSELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSkrMPEGDIRFKFL 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276317729 400 ---TALTFVVLVISIVILYLRFGAQVLqdnfvaelsahyQNSAEFLSFYGLLNFYLYTLAFVYSPSK 463
Cdd:pfam06664 240 mllTLLCAAVTVIFIILGQFSFGQNFN------------STSAFFLGFYGMLNLYVYTLAYLYAPSH 294
 
Name Accession Description Interval E-value
MIG-14_Wnt-bd pfam06664
Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly ...
168-463 1.86e-97

Wnt-binding factor required for Wnt secretion; MIG-14 is a Wnt-binding factor. Newly synthesized EGL-20/Wnt binds to MIG-14 in the Golgi, targetting the Wnt to the cell membrane for secretion. AP-2-mediated endocytosis and retromer retrieval at the sorting endosome would recycle MIG-14 to the Golgi, where it can bind to EGL-20/Wnt for next cycle of secretion.


Pssm-ID: 461980  Cd Length: 294  Bit Score: 296.47  E-value: 1.86e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 168 KCAEIIVAHLGYLNYTQYRVTVGFEHL-----NQPIKDMNFTWKTYNPAFSRLEIWFHFVFVVLTFIVICLFVHSLRKFS 242
Cdd:pfam06664   1 NCDPITLFELGSLDYSYYLINIRFPNLeefhdNYDGKELVFTFIHQNPGFTLFEIWFRTIFLIISFIVLIWFLFSLRKLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 243 MRDWGIEQKWMSVLLALLLLYNDPFFPLSFLVNSWFPGMLDDFFQSLFLCALLLFWLCVYHGIRV-QGERKCLTFYLPKF 321
Cdd:pfam06664  81 SRDWSLEQKWLFVLLILLILFNNPFFPLTLLFNSWFFLLLDDIFQGIFYSALLLFWLVFFDHLRDeQNERKSLSFYLPKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 322 FIVGLLWLASVTLGIWQTFNELNDPMYQYrVDTGNFQGMKVFFMVVAAVYILYLLFLIVRACSELRH--MPYVDLRLKFL 399
Cdd:pfam06664 161 LLVGVLWLSLLILDIWERGVQLKDPFYSI-WDSELADGFKILAGILAVLYFLYLLYLIFRVFSEIRSkrMPEGDIRFKFL 239
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1276317729 400 ---TALTFVVLVISIVILYLRFGAQVLqdnfvaelsahyQNSAEFLSFYGLLNFYLYTLAFVYSPSK 463
Cdd:pfam06664 240 mllTLLCAAVTVIFIILGQFSFGQNFN------------STSAFFLGFYGMLNLYVYTLAYLYAPSH 294
Frag1 pfam10277
Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF ...
285-419 4.50e-03

Frag1/DRAM/Sfk1 family; This family includes Frag1, DRAM and Sfk1 proteins. Frag1 (FGF receptor activating protein 1) is a protein that is conserved from fungi to humans. There are four potential iso-prenylation sites throughout the peptide, viz CILW, CIIW and CIGL. Frag1 is a membrane-spanning protein that is ubiquitously expressed in adult tissues suggesting an important cellular function. Dram is a family of proteins conserved from nematodes to humans with six hydrophobic transmembrane regions and an Endoplasmic Reticulum signal peptide. It is a lysosomal protein that induces macro-autophagy as an effector of p53-mediated death, where p53 is the tumour-suppressor gene that is frequently mutated in cancer. Expression of Dram is stress-induced. This region is also part of a family of small plasma membrane proteins, referred to as Sfk1, that may act together with or upstream of Stt4p to generate normal levels of the essential phospholipid PI4P, thus allowing proper localization of Stt4p to the actin cytoskeleton.


Pssm-ID: 431193  Cd Length: 220  Bit Score: 38.78  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276317729 285 FFQSLFLCALLLFWLCV--YHGIRVQGERKCLTFYLPkFFIVGLLWLASVTLGIWQTFNELNDPMYQYrvdtgnfqGMKV 362
Cdd:pfam10277  57 FSIAINIGAFLRLAVAFlrYLRLRPLARRSERVLRLN-ILALVFGLLGALGLSLVSNFQSTEDHSVHD--------IGAI 127
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1276317729 363 FFMVVAAVYILYLLFLIVRACSELRHMPYVDLRLKFLTALTFVVLVISIVILYLRFG 419
Cdd:pfam10277 128 LFFVFGFIYMLLQTALSYRLGPHYTPKSRKSFRLKLVLLILAFVSAVAFIVFFIRHK 184
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH