| General information | | DisProt: | DP00052 | | Name: | SPARC | | Synonym(s): | SPRC_MOUSE
Secreted protein acidic and rich in cysteine
Osteonectin
ON
Basement-membrane protein 40
BM-40
| | First appeared in release: | Release 1.0 (08/01/2003) | | UniProt: | P07214 | | UniGene: | Mm.291442 | | SwissProt: | SPRC_MOUSE | | TrEMBL: | | | NCBI (GI): | 129284 | | Source organism: | Mus musculus (Mouse) | | Sequence length: | 302 | | Percent disordered: | 94% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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MRAWIFFLLC LAGRALAAPQ QTEVAEEIVE EETVVEETGV PVGANPVQVE MGEFEDGAEE - 60
TVEEVVADNP CQNHHCKHGK VCELDESNTP MCVCQDPTSC PAPIGEFEKV CSNDNKTFDS - 120
SCHFFATKCT LEGTKKGHKL HLDYIGPCKY IAPCLDSELT EFPLRMRDWL KNVLVTLYER - 180
DEGNNLLTEK QKLRVKKIHE NEKRLEAGDH PVELLARDFE KNYNMYIFPV HWQFGQLDQH - 240
PIDGYLSHTE LAPLRAPLIP MEHCTTRFFE TCDLDNDKYI ALEEWAGCFG IKEQDINKDL - 300
VI
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| Functional narrative |
SPARC is a small acidic secreted protein. The SPARC precursor consists of 302 amino acid from which an N-term 17-residue signaling sequence is removed posttranslationally. SPARC is a Ca2+ dependant phosphorylated glycoprotein associated with extracellular matrix synthesis and remodeling. Conformational changes upon Ca2+ binding result in a 35% increase in alpha-helicity. SPARC was originally isolated from parietal endoderm cells, basement membrane producing tumors, and bone, but has since been found in various other tissues as well. SPARC content increases during morphogenesis to aid in remodeling and wound repair.
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| 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.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 18 - 302 | | Length: | 285 | | Region sequence: |
APQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCK
HGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKG
HKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKK
IHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAP
LIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI | | Modification type: | Native
| | PDB: | | | Structural/functional type: | Function arises via a disorder to pre-molten globule transition
| | Functional classes: | Unknown
| | Functional subclasses: | Unknown
| Detection methods:
- X-ray crystallography
- Circular dichroism (CD) spectroscopy, far-UV (293 K; )
| References:
- Engel J, Taylor W, Paulsson M, Sage H, Hogan B. "Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues." Biochemistry. 1987; 26(22): 6958-65. PubMed: 3427055
| Comments:Two calcium binding domains are known but more may exist.
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| If you have any comments or wish to provide additional references to this protein or its disordered region(s), please click here to e-mail us. |
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