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Conserved domains on  [gi|148685961|gb|EDL17908|]
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proline-rich acidic protein 1, isoform CRA_b [Mus musculus]

Protein Classification

PRAP domain-containing protein( domain architecture ID 10633912)

PRAP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRAP pfam15314
Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic ...
 100-144 1.27e-14

Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic protein 1, is a family of eukaryotic proteins. PRAP is abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. It is significantly down-regulated in hepatocellular carcinoma and right colon adenocarcinoma compared with the respective adjacent normal tissues. In the mouse it is expressed in the epithelial cells of the mouse and rat gastrointestinal tracts, and pregnant mouse uterus. This article describes the isolation, distribution, and functional characterization of the human homolog. PRAP was abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. PRAP plays an important role in maintaining normal growth suppression.


:

Pssm-ID: 464639  Cd Length: 45  Bit Score: 63.64  E-value: 1.27e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 148685961  100 PELDLDSIDHPMSDDVQDEEVPQSRPILYRQVLQGPEEDLDHLAH 144
Cdd:pfam15314   1 PEPDRDSLYHPPPEEAQEEERPWSRALLSRQVLQGPEEDRDHIYH 45
 
Name Accession Description Interval E-value
PRAP pfam15314
Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic ...
 100-144 1.27e-14

Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic protein 1, is a family of eukaryotic proteins. PRAP is abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. It is significantly down-regulated in hepatocellular carcinoma and right colon adenocarcinoma compared with the respective adjacent normal tissues. In the mouse it is expressed in the epithelial cells of the mouse and rat gastrointestinal tracts, and pregnant mouse uterus. This article describes the isolation, distribution, and functional characterization of the human homolog. PRAP was abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. PRAP plays an important role in maintaining normal growth suppression.


Pssm-ID: 464639  Cd Length: 45  Bit Score: 63.64  E-value: 1.27e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 148685961  100 PELDLDSIDHPMSDDVQDEEVPQSRPILYRQVLQGPEEDLDHLAH 144
Cdd:pfam15314   1 PEPDRDSLYHPPPEEAQEEERPWSRALLSRQVLQGPEEDRDHIYH 45
 
Name Accession Description Interval E-value
PRAP pfam15314
Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic ...
 100-144 1.27e-14

Proline-rich acidic protein 1, pregnancy-specific uterine; PRAP, or proline-rich acidic protein 1, is a family of eukaryotic proteins. PRAP is abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. It is significantly down-regulated in hepatocellular carcinoma and right colon adenocarcinoma compared with the respective adjacent normal tissues. In the mouse it is expressed in the epithelial cells of the mouse and rat gastrointestinal tracts, and pregnant mouse uterus. This article describes the isolation, distribution, and functional characterization of the human homolog. PRAP was abundantly expressed in the epithelial cells of the human liver, kidney, gastrointestinal tract, and cervix. PRAP plays an important role in maintaining normal growth suppression.


Pssm-ID: 464639  Cd Length: 45  Bit Score: 63.64  E-value: 1.27e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 148685961  100 PELDLDSIDHPMSDDVQDEEVPQSRPILYRQVLQGPEEDLDHLAH 144
Cdd:pfam15314   1 PEPDRDSLYHPPPEEAQEEERPWSRALLSRQVLQGPEEDRDHIYH 45
 
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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