DP00386_C001: Truncated apolipoprotein A-IFASTA viewXML view

General information
DisProt:DP00386_C001
Name:Truncated apolipoprotein A-I
Synonym(s):APOA1_HUMAN
Apo-AI
ApoA-I
cleavage product 1 of Apolipoprotein A-I
Apolipoprotein A-I (1-242)
First appeared in release:Release 3.0 (02/17/2006)
UniProt:P02647
UniGene:Hs.633003
SwissProt: APOA1_HUMAN
TrEMBL:  
NCBI (GI): 113992
Source organism:Homo sapiens (Human)
Sequence length:242
Percent disordered:31%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
DEPPQSPWDR VKDLATVYVD VLKDSGRDYV SQFEGSALGK QLNLKLLDNW DSVTSTFSKL - 60
REQLGPVTQE FWDNLEKETE GLRQEMSKDL EEVKAKVQPY LDDFQKKWQE EMELYRQKVE - 120
PLRAELQEGA RQKLHELQEK LSPLGEEMRD RARAHVDALR THLAPYSDEL RQRLAARLEA - 180
LKENGGARLA EYHAKATEHL STLSEKAKPA LEDLRQGLLP VLESFKVSFL SALEEYTKKL - 240
NT



Functional narrative    

Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. Apolipoprotein A-I (1-242) is cleavage product 1 of Apolipoprotein A-I, comprised of amino acid residues 25-266 of the polyprotein. This cleavage product is often referred to by the same name as the 'parent' polyprotein. Additionally, a chain of 243 aa, identical to this cleavage product with the addition of a Glutamine at position 243, exists.

Region 2: 1-8 Region 3: 33-43 Region 1: 1-44 Region 4: 65-66 Region 5: 78-81 Region 6: 87-89 Region 7: 98-99 Region 8: 119-121 Region 9: 141-145 Region 10: 163-166 Region 11: 206-209 Region 12: 217-220

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name: 
Location:1 - 44
Length:44
Region sequence:

DEPPQSPWDRVKDLATVYVDVLKDSGRDYVSQFEGSALGKQLNL

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Protein-lipid interaction
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; )

References:
  1. Zhu HL, Atkinson D. "Conformation and lipid binding of the N-terminal (1-44) domain of human apolipoprotein A-I." Biochemistry. 2004; 43(41): 13156-64. PubMed: 15476409

Comments:
 



Region 2
Type:Disordered
Name: 
Location:1 - 8
Length:8
Region sequence:

DEPPQSPW

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 3
Type:Disordered
Name: 
Location:33 - 43
Length:11
Region sequence:

FEGSALGKQLN

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 4
Type:Disordered
Name: 
Location:65 - 66
Length:2
Region sequence:

GP

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 5
Type:Disordered
Name: 
Location:78 - 81
Length:4
Region sequence:

ETEG

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 6
Type:Disordered
Name: 
Location:87 - 89
Length:3
Region sequence:

SKD

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 7
Type:Disordered
Name: 
Location:98 - 99
Length:2
Region sequence:

QP

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 8
Type:Disordered
Name: 
Location:119 - 121
Length:3
Region sequence:

VEP

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 9
Type:Disordered
Name: 
Location:141 - 145
Length:5
Region sequence:

LSPLG

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 10
Type:Disordered
Name: 
Location:163 - 166
Length:4
Region sequence:

LAPY

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 11
Type:Disordered
Name: 
Location:206 - 209
Length:4
Region sequence:

KAKP

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Region 12
Type:Disordered
Name: 
Location:217 - 220
Length:4
Region sequence:

GLLP

Modification type: Complex
Monomeric
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Unknown
Functional subclasses: Unknown
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (315 K; pH: 7; )

  2. Nuclear magnetic resonance (NMR) (315 K; pH: 7; D2O 5 %; H2O 95 %)

References:
  1. Okon M, Frank PG, Marcel YL, Cushley RJ. "Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution." FEBS Lett. 2002; 517(1-3): 139-43. PubMed: 12062424

Comments:
 



Comments


Previous entry DP00386 has been split into the polyprotein (DP00386) and cleavage product 1 DP00386_C001. Disorder is characterized on the cleavage product.

A 243-aa form also exists that is identical to the cleavage product but for the addition of a Glutamine at what would be position 243 in the cleavage product (position 267 in the polyprotein).


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