DP00214: OsteopontinFASTA viewXML view

General information
DisProt:DP00214
Name:Osteopontin
Synonym(s):OSTP_HUMAN
Bone sialoprotein 1
Secreted phosphoprotein 1
SPP-1
Urinary stone protein
Nephropontin
Uropontin
First appeared in release:Release 2.0 (02/14/2005)
UniProt:P10451
UniGene:Hs.313
SwissProt: OSTP_HUMAN
TrEMBL:  
NCBI (GI): 129260
Source organism:Homo sapiens (Human)
Sequence length:314
Percent disordered:100%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MRIAVICFCL LGITCAIPVK QADSGSSEEK QLYNKYPDAV ATWLNPDPSQ KQNLLAPQNA - 60
VSSEETNDFK QETLPSKSNE SHDHMDDMDD EDDDDHVDSQ DSIDSNDSDD VDDTDDSHQS - 120
DESHHSDESD ELVTDFPTDL PATEVFTPVV PTVDTYDGRG DSVVYGLRSK SKKFRRPDIQ - 180
YPDATDEDIT SHMESEELNG AYKAIPVAQD LNAPSDWDSR GKDSYETSQL DDQSAETHSH - 240
KQSRLYKRKA NDESNEHSDV IDSQELSKVS REFHSHEFHS HEDMLVVDPK SKEEDKHLKF - 300
RISHELDSAS SEVN



Functional narrative    

Osteopontin is a member of the Small Integrin-Binding LIgand, N-linked Glycoprotein (SIBLING) family. They are involved in hydroxyapatite binding, which allows osteoclasts to connect integrins on the surface of the cell with minerals during bone resorption. It can also bind to other proteins, like CD44, which enables a cell to protect surface receptors from lysis by forming a complex with it. These proteins are highly flexible in solution, which allows them to associate with a number of potential target molecules. This flexibility is vital for their function.

Region 1: 1-314

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 - 314
Length:314
Region sequence:

MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNA
VSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQS
DESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQ
YPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSH
KQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKF
RISHELDSASSEVN

Modification type: Native
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes: Molecular assembly
Functional subclasses: Substrate/ligand binding
Protein-protein binding
Detection methods:
  1. Nuclear magnetic resonance (NMR) (303 K; pH: 6; protein (per mL water (BSP)) 15 mg)

  2. Nuclear magnetic resonance (NMR) (303 K; pH: 6; protein 15 mg; sodium phosphate 10 mM)
References:
  1. Fisher LW, Torchia DA, Fohr B, Young MF, Fedarko NS. "Flexible structures of SIBLING proteins, bone sialoprotein, and osteopontin." Biochem Biophys Res Commun. 2001; 280(2): 460-5. PubMed: 11162539
Comments:
 


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