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Conserved domains on  [gi|226528371|ref|NP_001147107|]
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short coiled-coil protein isoform 5 [Homo sapiens]

Protein Classification

short coiled-coil protein( domain architecture ID 10562948)

short coiled-coil protein is a positive regulator of amino acid starvation-induced autophagy

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF2205 pfam10224
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ...
 42-112 2.36e-23

Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons.


:

Pssm-ID: 431150  Cd Length: 71  Bit Score: 85.45  E-value: 2.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226528371   42 MNADMDVDAENQVELEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQ 112
Cdd:pfam10224   1 MSPRRNSEDLEKLGREARERLIQQAKTLQSSLLALADRIDAVKEEHDKLESENRFLQDYIGDLMSTSKITS 71
 
Name Accession Description Interval E-value
DUF2205 pfam10224
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ...
 42-112 2.36e-23

Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons.


Pssm-ID: 431150  Cd Length: 71  Bit Score: 85.45  E-value: 2.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226528371   42 MNADMDVDAENQVELEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQ 112
Cdd:pfam10224   1 MSPRRNSEDLEKLGREARERLIQQAKTLQSSLLALADRIDAVKEEHDKLESENRFLQDYIGDLMSTSKITS 71
 
Name Accession Description Interval E-value
DUF2205 pfam10224
Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil ...
 42-112 2.36e-23

Short coiled-coil protein; This entry represents a highly conserved 100 residue coiled-coil region which is found in short coiled-coil protein (SCOC) in human and UNC-69 in Caenorhabditis elegans. In human, SCOC is required for autophagosome formation during amino acid starvation. It forms a starvation-sensitive trimeric complex with UVRAG (UV radiation resistance associated gene) and FEZ1 and may regulate ULK1 and Beclin 1 complex activities. In C. elegans, this small, evolutionarily conserved coiled-coil domain-containing protein, UNC-69, acts as a binding partner of UNC-76. Together they participate in a common genetic pathway necessary for axon extension and cooperate to regulate the size and position of synaptic vesicles in axons. Moreover, both proteins colocalize as puncta in neuronal processes and mutations in UNC-69 preferentially disrupt membrane traffic within axons.


Pssm-ID: 431150  Cd Length: 71  Bit Score: 85.45  E-value: 2.36e-23
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 226528371   42 MNADMDVDAENQVELEEKTRLINQVLELQHTLEDLSARVDAVKEENLKLKSENQVLGQYIENLMSASSVFQ 112
Cdd:pfam10224   1 MSPRRNSEDLEKLGREARERLIQQAKTLQSSLLALADRIDAVKEEHDKLESENRFLQDYIGDLMSTSKITS 71
 
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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