DP00138: Parathyroid hormone-related proteinFASTA viewXML view

General information
DisProt:DP00138
Name:Parathyroid hormone-related protein
Synonym(s):PTHR_HUMAN
PTH-rP
PTHrP
PTHrP[1-36][cleavage product 1]
PTHrP[38-94][cleavage product 2]
Osteostatin [cleavage product 3]
PTHrP[107-139]
First appeared in release:Release 1.0 (08/01/2003)
UniProt:P12272
UniGene:Hs.591159
SwissProt: PTHR_HUMAN
TrEMBL:  
NCBI (GI): 131542
Source organism:Homo sapiens (Human)
Sequence length:177
Percent disordered:10%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MQRRLVQQWS VAVFLLSYAV PSCGRSVEGL SRRLKRAVSE HQLLHDKGKS IQDLRRRFFL - 60
HHLIAEIHTA EIRATSEVSP NSKPSPNTKN HPVRFGSDDE GRYLTQETNK VETYKEQPLK - 120
TPGKKKKGKP GKRKEQEKKK RRTRSAWLDS GVTGSGLEGD HLSDTSTTSL ELDSRRH



Functional narrative    

Parathyroid hormone-related protein precursor (PTHrP) is similar to parathyroid hormone, however it is produced in almost all types of tissues. It is involved in many physiological processes, including lactation, calcium transport, and signaling. PTHrP interacts with various receptor binding proteins including the G-protein-coupled receptor. PTHrP is produced by tumors associated with humoral hypercalcemia of malignancy (HHM). The first disordered region is thought to function in a signal transduction pathway that initiates a cascade similar to parathyroid hormone. The disordered regions near the N-terminus are involved in protein-protein interactions with G-protein-coupled receptors.

Region 1: 1-4 Region 2: 9-15 Region 3: 28-34

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:1 - 4
Length:4
Region sequence:

MQRR

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular assembly
Molecular recognition effectors
Functional subclasses: Protein-protein binding
Substrate/ligand binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 5.1; )

  2. Nuclear magnetic resonance (NMR) (277 K; pH: 5.1; )

References:
  1. Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P. "The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution." FEBS Lett. 1999; 444(2-3): 239-244. PubMed: 10050767

  2. Willis KJ. "Interaction with model membrane systems induces secondary structure in amino-terminal fragments of parathyroid hormone related protein." Int J Pept Protein Res. 1994; 43(1): 23-28. PubMed: 8138348

Comments:
 



Region 2
Type:Disordered - Extended
Name: 
Location:9 - 15
Length:7
Region sequence:

WSVAVFL

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Entropic chain
Functional subclasses: Flexible linkers/spacers
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 5.1; )

  2. Nuclear magnetic resonance (NMR) (277 K; pH: 5.1; )

References:
  1. Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P. "The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution." FEBS Lett. 1999; 444(2-3): 239-244. PubMed: 10050767

  2. Willis KJ. "Interaction with model membrane systems induces secondary structure in amino-terminal fragments of parathyroid hormone related protein." Int J Pept Protein Res. 1994; 43(1): 23-28. PubMed: 8138348

Comments:
 



Region 3
Type:Disordered - Extended
Name: 
Location:28 - 34
Length:7
Region sequence:

EGLSRRL

Modification type: Engineered
Fragment
PDB:  
Structural/functional type: Relationship to function unknown
Functional classes: Molecular recognition effectors
Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Circular dichroism (CD) spectroscopy, far-UV (298 K; pH: 5.1; )

  2. Nuclear magnetic resonance (NMR) (277 K; pH: 5.1; )

References:
  1. Weidler M, Marx UC, Seidel G, Schafer W, Hoffmann E, Esswein A, Rosch P. "The structure of human parathyroid hormone-related protein(1-34) in near-physiological solution." FEBS Lett. 1999; 444(2-3): 239-244. PubMed: 10050767

  2. Willis KJ. "Interaction with model membrane systems induces secondary structure in amino-terminal fragments of parathyroid hormone related protein." Int J Pept Protein Res. 1994; 43(1): 23-28. PubMed: 8138348

Comments:
 



Comments


Disordered regions are not associated with any of the cleavage products.


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