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Conserved domains on  [gi|6678051|ref|NP_033249|]
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stannin [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Stannin cd20257
Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single ...
 4-88 9.87e-55

Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single transmembrane helix that transverses the lipid bilayer, an unstructured linker which includes a conserved CXC metal-binding motif and a putative 14-3-3zeta binding site, and a C-terminal distorted cytoplasmic helix. It binds and antagonizes 14-3-3zeta and is required for endosomal maturation. It has also been identified as the specific marker for neuronal cell apoptosis induced by trimethyltin (TMT) intoxication. TMT is one of the most toxic organotin compound (or alkyltin), and is known to selectively inflict injury to specific regions of the brain.


:

Pssm-ID: 380774 [Multi-domain]  Cd Length: 84  Bit Score: 163.87  E-value: 9.87e-55
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678051   4 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLmTANS 83
Cdd:cd20257  1 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGEGETKEPFLLVQYSAKGPCVERKAKL-TPNG 79


               ....*
gi 6678051  84 PEVHG 88
Cdd:cd20257 80 TEVHS 84
 
Name Accession Description Interval E-value
Stannin cd20257
Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single ...
 4-88 9.87e-55

Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single transmembrane helix that transverses the lipid bilayer, an unstructured linker which includes a conserved CXC metal-binding motif and a putative 14-3-3zeta binding site, and a C-terminal distorted cytoplasmic helix. It binds and antagonizes 14-3-3zeta and is required for endosomal maturation. It has also been identified as the specific marker for neuronal cell apoptosis induced by trimethyltin (TMT) intoxication. TMT is one of the most toxic organotin compound (or alkyltin), and is known to selectively inflict injury to specific regions of the brain.


Pssm-ID: 380774 [Multi-domain]  Cd Length: 84  Bit Score: 163.87  E-value: 9.87e-55
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678051   4 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLmTANS 83
Cdd:cd20257  1 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGEGETKEPFLLVQYSAKGPCVERKAKL-TPNG 79


               ....*
gi 6678051  84 PEVHG 88
Cdd:cd20257 80 TEVHS 84
SNN_transmemb pfam09049
Stannin transmembrane; Members of this family consist of a single highly hydrophobic ...
 2-33 9.57e-12

Stannin transmembrane; Members of this family consist of a single highly hydrophobic transmembrane helix that transverses the lipid bilayer at a 20 degree angle with respect to the membrane normal. They contain a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimethyltin-binding site that resides at the end of the transmembrane domain close to the lipid/solvent interface.


Pssm-ID: 401113  Cd Length: 32  Bit Score: 54.23  E-value: 9.57e-12
                         10        20        30
                 ....*....|....*....|....*....|..
gi 6678051     2 SIMDHSPTTGVVTVIVILIAIAALGALILGCW 33
Cdd:pfam09049  1 SIMDHNPTTGVVTVIVILIAIAALGALILGCW 32
 
Name Accession Description Interval E-value
Stannin cd20257
Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single ...
 4-88 9.87e-55

Stannin; Stannin (SNN) is a monotopic membrane protein containing an N-terminal single transmembrane helix that transverses the lipid bilayer, an unstructured linker which includes a conserved CXC metal-binding motif and a putative 14-3-3zeta binding site, and a C-terminal distorted cytoplasmic helix. It binds and antagonizes 14-3-3zeta and is required for endosomal maturation. It has also been identified as the specific marker for neuronal cell apoptosis induced by trimethyltin (TMT) intoxication. TMT is one of the most toxic organotin compound (or alkyltin), and is known to selectively inflict injury to specific regions of the brain.


Pssm-ID: 380774 [Multi-domain]  Cd Length: 84  Bit Score: 163.87  E-value: 9.87e-55
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678051   4 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLmTANS 83
Cdd:cd20257  1 MDHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGEGETKEPFLLVQYSAKGPCVERKAKL-TPNG 79


               ....*
gi 6678051  84 PEVHG 88
Cdd:cd20257 80 TEVHS 84
Stannin_family cd20256
Stannin family includes vertebrate Stannin and insect Hemotin; The Stannin family includes ...
 5-87 2.85e-46

Stannin family includes vertebrate Stannin and insect Hemotin; The Stannin family includes vertebrate Stannin and insect Hemotin, which are functional homologs required at the cellular level for endosomal maturation, and at the molecular level, to bind and antagonize 14-3-3zeta. Stannin is a monotopic membrane protein containing an N-terminal single transmembrane helix that transverses the lipid bilayer, an unstructured linker which includes a conserved CXC metal-binding motif and a putative 14-3-3zeta binding site, and a C-terminal distorted cytoplasmic helix. Analysis of the Hemotin sequence using a transmembrane topology prediction program revealed a very similar potential transmembrane alpha-helical domain arrangement as Stannin.


Pssm-ID: 380773 [Multi-domain]  Cd Length: 83  Bit Score: 142.50  E-value: 2.85e-46
                       10        20        30        40        50        60        70        80
               ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6678051   5 DHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTANSP 84
Cdd:cd20256  1 DHSPTTGVVTVIVILIAIAALGALILGCWCYLRLQRISQSEDEESIVGDGETKEPFLLVQYSAKGPCVERKAKLMTRNSP 80


               ...
gi 6678051  85 EVH 87
Cdd:cd20256 81 EVH 83
SNN_transmemb pfam09049
Stannin transmembrane; Members of this family consist of a single highly hydrophobic ...
 2-33 9.57e-12

Stannin transmembrane; Members of this family consist of a single highly hydrophobic transmembrane helix that transverses the lipid bilayer at a 20 degree angle with respect to the membrane normal. They contain a conserved cysteine residue (Cys32) that, together with Cys34 found in the stannin unstructured linker domain, constitutes the putative trimethyltin-binding site that resides at the end of the transmembrane domain close to the lipid/solvent interface.


Pssm-ID: 401113  Cd Length: 32  Bit Score: 54.23  E-value: 9.57e-12
                         10        20        30
                 ....*....|....*....|....*....|..
gi 6678051     2 SIMDHSPTTGVVTVIVILIAIAALGALILGCW 33
Cdd:pfam09049  1 SIMDHNPTTGVVTVIVILIAIAALGALILGCW 32
SNN_linker pfam09050
Stannin unstructured linker; Members of this family are unstructured, acting as connectors of ...
 34-59 3.12e-11

Stannin unstructured linker; Members of this family are unstructured, acting as connectors of the stannin helical domains. They contain a conserved CXC metal-binding motif and a putative 14-3-3-zeta binding domain. Upon coordinating dimethytin, considerable structural or dynamic changes in the flexible loop region of SNN may take place, recruiting other binding partners such as 14-3-3-zeta, and thereby initiating the apoptotic cascade.


Pssm-ID: 370263  Cd Length: 26  Bit Score: 52.86  E-value: 3.12e-11
                         10        20
                 ....*....|....*....|....*.
gi 6678051    34 CYLRLQRISQSEDEESIVGDGETKEP 59
Cdd:pfam09050  1 CYLRLQRISQSEDEESIVGDGETKEP 26
SNN_cytoplasm pfam09051
Stannin cytoplasmic; Members of this family consist of a distorted cytoplasmic helix that is ...
 61-87 8.19e-05

Stannin cytoplasmic; Members of this family consist of a distorted cytoplasmic helix that is partially absorbed into the plane of the lipid bilayer with a tilt angle of approximately 80 degrees from the membrane normal. They interact with the surface of the lipid bilayer, and contribute to the initiation of the apoptotic cascade on binding of the unstructured linker domain to dimethyltin.


Pssm-ID: 401114  Cd Length: 26  Bit Score: 36.37  E-value: 8.19e-05
                         10        20
                 ....*....|....*....|....*..
gi 6678051    61 LLVQYSAKGPCVERKAKLmTANSPEVH 87
Cdd:pfam09051  1 LLVQYSAKGPCVERKAKL-TPNGPEVH 26
 
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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