DP00011: Sulfotransferase 1A3/1A4FASTA viewXML view

General information
DisProt:DP00011
Name:Sulfotransferase 1A3/1A4
Synonym(s):ST1A3_HUMAN
Monoamine-sulfating phenol sulfotransferase
Sulfotransferase, monoamine-preferring
Catecholamine-sulfating phenol sulfotransferase
HAST3
M-PST
Thermolabile phenol sulfotransferase
Placental estrogen sulfotransferase
TL-PST
EC=2.8.2.1
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P50224
UniGene:Hs.460558
SwissProt: ST1A3_HUMAN
TrEMBL:  
NCBI (GI): 1711609
Source organism:Homo sapiens (Human)
Sequence length:295
Percent disordered:24%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MELIQDTSRP PLEYVKGVPL IKYFAEALGP LQSFQARPDD LLINTYPKSG TTWVSQILDM - 60
IYQGGDLEKC NRAPIYVRVP FLEVNDPGEP SGLETLKDTP PPRLIKSHLP LALLPQTLLD - 120
QKVKVVYVAR NPKDVAVSYY HFHRMEKAHP EPGTWDSFLE KFMAGEVSYG SWYQHVQEWW - 180
ELSRTHPVLY LFYEDMKENP KREIQKILEF VGRSLPEETM DFMVQHTSFK EMKKNPMTNY - 240
TTVPQELMDH SISPFMRKGM AGDWKTTFTV AQNERFDADY AEKMAGCSLS FRSEL



Functional narrative    

Catecholamine sulfotransferase is a member of the cytosolic sulfotransferase superfamily. Catecholamine sulfotransferase is primarily responsible for sulfonation of catecholamines which is regarded as a detoxification pathway and leads to the formation of readily excretable water soluble metabolites (Bidwell, 1999). Catecholamine sulfotransferase is located in the cytosol of the cell and interacts with adenosine 3’, 5’-diphosphate, sulfate, and dopamine, as well as other catecholamines. A shortage of catecholamine sulfotransferase may be linked to pseudopheochromocytoma. Many of the residues involved in cofactor and substrate binding are disordered or flexible in the catecholamine sulfotransferase (Bidwell, 1999).

Region 2: 1-7 Region 7: 8-63 Region 3: 64-77 Region 8: 78-90 Region 4: 91-93 Region 9: 94-215 Region 1: 216-261 Region 10: 262-293 Region 5: 294-295

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 - Extended
Name: 
Location:216 - 261
Length:46
Region sequence:

PEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMA

Modification type: Fragment
PDB: 1CJM:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Metal sponge
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (293 K; PAP at 277 K (pre-incubation for 1-2 hours); lithium sulfate 0.5 M; polyethylene glycol 8000 (5-7% (w/v)))
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 2
Type:Disordered
Name: 
Location:1 - 7
Length:7
Region sequence:

MELIQDT

Modification type: Fragment
PDB: 1CJM:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (293 K; lithium sulfate 0.5 M; PAP at 277 K (pre-incubation for 1-2 hours); polyethylene glycol 8000 (5-7% (w/v)))
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 3
Type:Disordered
Name: 
Location:64 - 77
Length:14
Region sequence:

GGDLEKCNRAPIYV

Modification type: Fragment
PDB: 1CJM:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (293 K; lithium sulfate 0.5 M; PAP at 277 K (pre-incubation for 1-2 hours); polyethylene glycol 8000 (5-7% (w/v)))
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 4
Type:Disordered
Name: 
Location:91 - 93
Length:3
Region sequence:

SGL

Modification type: Fragment
PDB: 1CJM:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (293 K; lithium sulfate 0.5 M; PAP at 277 K (pre-incubation for 1-2 hours); polyethylene glycol 8000 (5-7% (w/v)))
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 5
Type:Disordered
Name: 
Location:294 - 295
Length:2
Region sequence:

EL

Modification type: Fragment
PDB: 1CJM:A
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Unknown
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. X-ray crystallography (293 K; lithium sulfate 0.5 M; PAP at 277 K (pre-incubation for 1-2 hours); polyethylene glycol 8000 (5-7% (w/v)))
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 7
Type:Ordered
Name: 
Location:8 - 63
Length:56
Region sequence:

SRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQ

Modification type:  
PDB: 1CJM:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 8
Type:Ordered
Name: 
Location:78 - 90
Length:13
Region sequence:

RVPFLEVNDPGEP

Modification type:  
PDB: 1CJM:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 9
Type:Ordered
Name: 
Location:94 - 215
Length:122
Region sequence:

ETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPG
TWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGR
SL

Modification type:  
PDB: 1CJM:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



Region 10
Type:Ordered
Name: 
Location:262 - 293
Length:32
Region sequence:

GDWKTTFTVAQNERFDADYAEKMAGCSLSFRS

Modification type:  
PDB: 1CJM:A
Structural/functional type:  
Functional classes:  
Functional subclasses:  
Detection methods:
 
References:
  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947
Comments:
 



References

  1. Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL. "Crystal structure of human catecholamine sulfotransferase." J Mol Biol. 1999; 293(3): 521-30. PubMed: 10543947

  2. Dajani R, Cleasby A, Neu M, Wonacott AJ, Jhoti H, Hood AM, Modi S, Hersey A, Taskinen J, Cooke RM, Manchee GR, Coughtrie MW. "X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity." J Biol Chem. 1999; 274(53): 37862-8. PubMed: 10608851



Comments


Former DP00011 Region 6 (aa 216-224), was determined to be part of disordered Region 1 (aa 216-261) with no distinct separate disorder of its own, therefore it has been been 'decommissioned.'


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