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SPARC (Basement-membrane protein 40) (BM-40) (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine)

 SPRC_HUMAN              Reviewed;         303 AA.
P09486; D3DQH9; Q6IBK4;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-JUL-1989, sequence version 1.
22-NOV-2017, entry version 192.
RecName: Full=SPARC;
AltName: Full=Basement-membrane protein 40;
Short=BM-40;
AltName: Full=Osteonectin;
Short=ON;
AltName: Full=Secreted protein acidic and rich in cysteine;
Flags: Precursor;
Name=SPARC; Synonyms=ON;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
TISSUE=Placenta;
PubMed=3410046; DOI=10.1016/0014-5793(88)80054-1;
Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., Krieg T.;
"Cloning and complete amino acid sequences of human and murine
basement membrane protein BM-40 (SPARC, osteonectin).";
FEBS Lett. 236:352-356(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2838412; DOI=10.1016/0888-7543(88)90107-3;
Swaroop A., Hogan B.L.M., Francke U.;
"Molecular analysis of the cDNA for human SPARC/osteonectin/BM-40:
sequence, expression, and localization of the gene to chromosome 5q31-
q33.";
Genomics 2:37-47(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2790009; DOI=10.1021/bi00441a049;
Villarreal X.C., Mann K.G., Long G.L.;
"Structure of human osteonectin based upon analysis of cDNA and
genomic sequences.";
Biochemistry 28:6483-6491(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2338025; DOI=10.3109/03008209009152419;
Young M.F., Day A.A., Dominquez P., McQuillan C.I., Fisher L.W.,
Termine J.D.;
"Structure and expression of osteonectin mRNA in human tissue.";
Connect. Tissue Res. 24:17-28(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, PNS, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-154.
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[9]
PROTEIN SEQUENCE OF 18-53, AND CHARACTERIZATION.
PubMed=3597437;
Fisher L.W., Hawkins G.R., Tuross N., Termine J.D.;
"Purification and partial characterization of small proteoglycans I
and II, bone sialoproteins I and II, and osteonectin from the mineral
compartment of developing human bone.";
J. Biol. Chem. 262:9702-9708(1987).
[10]
PROTEIN SEQUENCE OF 18-41, CHARACTERIZATION, AND SUBCELLULAR LOCATION.
PubMed=2306517;
Kelm R.J. Jr., Mann K.G.;
"Human platelet osteonectin: release, surface expression, and partial
characterization.";
Blood 75:1105-1113(1990).
[11]
SUBCELLULAR LOCATION.
PubMed=3400777;
Wewer U.M., Albrechtsen R., Fisher L.W., Young M.F., Termine J.D.;
"Osteonectin/SPARC/BM-40 in human decidua and carcinoma, tissues
characterized by de novo formation of basement membrane.";
Am. J. Pathol. 132:345-355(1988).
[12]
SUBCELLULAR LOCATION.
PubMed=7495300;
Kuhn C., Mason R.J.;
"Immunolocalization of SPARC, tenascin, and thrombospondin in
pulmonary fibrosis.";
Am. J. Pathol. 147:1759-1769(1995).
[13]
SUBCELLULAR LOCATION.
PubMed=9457905; DOI=10.1046/j.1523-1747.1998.00094.x;
Hunzelmann N., Hafner M., Anders S., Krieg T., Nischt R.;
"BM-40 (osteonectin, SPARC) is expressed both in the epidermal and in
the dermal compartment of adult human skin.";
J. Invest. Dermatol. 110:122-126(1998).
[14]
INVOLVEMENT IN OI17, VARIANTS OI17 HIS-166 AND LYS-263, AND
CHARACTERIZATION OF VARIANTS OI17 HIS-166 AND LYS-263.
PubMed=26027498; DOI=10.1016/j.ajhg.2015.04.021;
Care4Rare Canada Consortium;
Mendoza-Londono R., Fahiminiya S., Majewski J., Tetreault M.,
Nadaf J., Kannu P., Sochett E., Howard A., Stimec J., Dupuis L.,
Roschger P., Klaushofer K., Palomo T., Ouellet J., Al-Jallad H.,
Mort J.S., Moffatt P., Boudko S., Baechinger H.P., Rauch F.;
"Recessive osteogenesis imperfecta caused by missense mutations in
SPARC.";
Am. J. Hum. Genet. 96:979-985(2015).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 153-303.
PubMed=8548457; DOI=10.1038/nsb0196-67;
Hohenester E., Maurer P., Hahoenadl C., Timpl R., Jansonius J.N.,
Engel J.;
"Structure of a novel extracellular Ca(2+)-binding module in BM-40.";
Nat. Struct. Biol. 3:67-73(1996).
[16]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 71-303 IN COMPLEX WITH
CALCIUM IONS, GLYCOSYLATION AT ASN-116, AND DISULFIDE BONDS.
PubMed=9233787; DOI=10.1093/emboj/16.13.3778;
Hohenester E., Maurer P., Timpl R.;
"Crystal structure of a pair of follistatin-like and EF-hand calcium-
binding domains in BM-40.";
EMBO J. 16:3778-3786(1997).
[17]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 71-303 IN COMPLEX WITH
CALCIUM IONS, GLYCOSYLATION AT ASN-116, INTERACTION WITH COLLAGEN, AND
MUTAGENESIS OF ARG-166; ASN-173; LEU-259; MET-262 AND GLU-263.
PubMed=9501084; DOI=10.1093/emboj/17.6.1625;
Sasaki T., Hohenester E., Gohring W., Timpl R.;
"Crystal structure and mapping by site-directed mutagenesis of the
collagen-binding epitope of an activated form of BM-
40/SPARC/osteonectin.";
EMBO J. 17:1625-1634(1998).
-!- FUNCTION: Appears to regulate cell growth through interactions
with the extracellular matrix and cytokines. Binds calcium and
copper, several types of collagen, albumin, thrombospondin, PDGF
and cell membranes. There are two calcium binding sites; an acidic
domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-hand
loop that binds a Ca(2+) ion with a high affinity.
-!- INTERACTION:
P02461-1:COL3A1; NbExp=4; IntAct=EBI-2800983, EBI-15740444;
Q2TV77:faf (xeno); NbExp=4; IntAct=EBI-2800983, EBI-6405263;
Q99972:MYOC; NbExp=3; IntAct=EBI-2800983, EBI-11692272;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000269|PubMed:2306517,
ECO:0000269|PubMed:3400777, ECO:0000269|PubMed:7495300,
ECO:0000269|PubMed:9457905}. Note=In or around the basement
membrane.
-!- DEVELOPMENTAL STAGE: Expressed at high levels in tissues
undergoing morphogenesis, remodeling and wound repair.
-!- DISEASE: Osteogenesis imperfecta 17 (OI17) [MIM:616507]: An
autosomal recessive form of osteogenesis imperfecta, a connective
tissue disorder characterized by low bone mass, bone fragility and
susceptibility to fractures after minimal trauma. Disease severity
ranges from very mild forms without fractures to intrauterine
fractures and perinatal lethality. Extraskeletal manifestations,
which affect a variable number of patients, are dentinogenesis
imperfecta, hearing loss, and blue sclerae.
{ECO:0000269|PubMed:26027498}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA60993.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the C-terminal part.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Osteonectin entry;
URL="https://en.wikipedia.org/wiki/Osteonectin";
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EMBL; Y00755; CAA68724.1; -; mRNA.
EMBL; J03040; AAA60570.1; -; mRNA.
EMBL; M25746; AAA60993.1; ALT_SEQ; Genomic_DNA.
EMBL; M25738; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25739; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25740; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25741; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25742; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25743; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25744; AAA60993.1; JOINED; Genomic_DNA.
EMBL; M25745; AAA60993.1; JOINED; Genomic_DNA.
EMBL; CR456799; CAG33080.1; -; mRNA.
EMBL; CH471062; EAW61668.1; -; Genomic_DNA.
EMBL; CH471062; EAW61669.1; -; Genomic_DNA.
EMBL; CH471062; EAW61670.1; -; Genomic_DNA.
EMBL; CH471062; EAW61672.1; -; Genomic_DNA.
EMBL; BC004974; AAH04974.1; -; mRNA.
EMBL; BC008011; AAH08011.1; -; mRNA.
EMBL; BC072457; AAH72457.1; -; mRNA.
EMBL; AL709729; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS4318.1; -.
PIR; A32821; GEHUN.
RefSeq; NP_001296372.1; NM_001309443.1.
RefSeq; NP_001296373.1; NM_001309444.1.
RefSeq; NP_003109.1; NM_003118.3.
UniGene; Hs.111779; -.
PDB; 1BMO; X-ray; 3.10 A; A/B=71-303.
PDB; 1NUB; X-ray; 2.80 A; A/B=71-303.
PDB; 1SRA; X-ray; 2.00 A; A=153-303.
PDB; 2V53; X-ray; 3.20 A; A=70-303.
PDBsum; 1BMO; -.
PDBsum; 1NUB; -.
PDBsum; 1SRA; -.
PDBsum; 2V53; -.
ProteinModelPortal; P09486; -.
SMR; P09486; -.
BioGrid; 112560; 10.
DIP; DIP-46426N; -.
IntAct; P09486; 14.
MINT; MINT-3006855; -.
STRING; 9606.ENSP00000231061; -.
iPTMnet; P09486; -.
PhosphoSitePlus; P09486; -.
UniCarbKB; P09486; -.
BioMuta; SPARC; -.
DMDM; 129283; -.
OGP; P09486; -.
EPD; P09486; -.
MaxQB; P09486; -.
PaxDb; P09486; -.
PeptideAtlas; P09486; -.
PRIDE; P09486; -.
DNASU; 6678; -.
Ensembl; ENST00000231061; ENSP00000231061; ENSG00000113140.
GeneID; 6678; -.
KEGG; hsa:6678; -.
UCSC; uc003lui.5; human.
CTD; 6678; -.
DisGeNET; 6678; -.
EuPathDB; HostDB:ENSG00000113140.10; -.
GeneCards; SPARC; -.
HGNC; HGNC:11219; SPARC.
HPA; CAB002306; -.
HPA; HPA002989; -.
HPA; HPA003020; -.
MalaCards; SPARC; -.
MIM; 182120; gene.
MIM; 616507; phenotype.
neXtProt; NX_P09486; -.
OpenTargets; ENSG00000113140; -.
PharmGKB; PA36055; -.
eggNOG; KOG4004; Eukaryota.
eggNOG; ENOG41101WW; LUCA.
GeneTree; ENSGT00510000046787; -.
HOVERGEN; HBG002746; -.
InParanoid; P09486; -.
OMA; KDFPRRM; -.
OrthoDB; EOG091G0CPG; -.
PhylomeDB; P09486; -.
TreeFam; TF319356; -.
Reactome; R-HSA-114608; Platelet degranulation.
Reactome; R-HSA-3000178; ECM proteoglycans.
Reactome; R-HSA-3000497; Scavenging by Class H Receptors.
ChiTaRS; SPARC; human.
EvolutionaryTrace; P09486; -.
GeneWiki; Osteonectin; -.
GenomeRNAi; 6678; -.
PMAP-CutDB; P09486; -.
PRO; PR:P09486; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113140; -.
CleanEx; HS_SPARC; -.
ExpressionAtlas; P09486; baseline and differential.
Genevisible; P09486; HS.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0071682; C:endocytic vesicle lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IBA:GO_Central.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0031091; C:platelet alpha granule; IDA:UniProtKB.
GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
GO; GO:0031092; C:platelet alpha granule membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
GO; GO:0005518; F:collagen binding; IDA:UniProtKB.
GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
GO; GO:0060348; P:bone development; IEA:Ensembl.
GO; GO:0071363; P:cellular response to growth factor stimulus; IEA:Ensembl.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0048839; P:inner ear development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0016525; P:negative regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IDA:UniProtKB.
GO; GO:0001503; P:ossification; IEA:Ensembl.
GO; GO:0043473; P:pigmentation; IEA:Ensembl.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0010595; P:positive regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0022604; P:regulation of cell morphogenesis; IDA:UniProtKB.
GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0051591; P:response to cAMP; IEA:Ensembl.
GO; GO:0034097; P:response to cytokine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0009629; P:response to gravity; IEA:Ensembl.
GO; GO:0033591; P:response to L-ascorbic acid; IEA:Ensembl.
GO; GO:0010288; P:response to lead ion; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0043434; P:response to peptide hormone; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR003645; Fol_N.
InterPro; IPR015369; Follistatin/Osteonectin_EGF.
InterPro; IPR002350; Kazal_dom.
InterPro; IPR036058; Kazal_dom_sf.
InterPro; IPR001999; Osteonectin_CS.
InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
Pfam; PF09289; FOLN; 1.
Pfam; PF00050; Kazal_1; 1.
Pfam; PF10591; SPARC_Ca_bdg; 1.
SMART; SM00274; FOLN; 1.
SMART; SM00280; KAZAL; 1.
SUPFAM; SSF100895; SSF100895; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS51465; KAZAL_2; 1.
PROSITE; PS00612; OSTEONECTIN_1; 1.
PROSITE; PS00613; OSTEONECTIN_2; 1.
1: Evidence at protein level;
3D-structure; Basement membrane; Calcium; Complete proteome; Copper;
Direct protein sequencing; Disease mutation; Disulfide bond;
Extracellular matrix; Glycoprotein; Metal-binding;
Osteogenesis imperfecta; Polymorphism; Reference proteome; Secreted;
Signal.
SIGNAL 1 17 {ECO:0000269|PubMed:2306517,
ECO:0000269|PubMed:3597437}.
CHAIN 18 303 SPARC.
/FTId=PRO_0000020304.
DOMAIN 71 93 Follistatin-like.
DOMAIN 89 151 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 261 296 EF-hand.
CA_BIND 274 285
COMPBIAS 22 69 Asp/Glu-rich (acidic; binds calcium).
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:9233787,
ECO:0000269|PubMed:9501084}.
DISULFID 72 83 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 77 93 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 95 130 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 101 123 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 112 149 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 155 265 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
DISULFID 273 289 {ECO:0000255|PROSITE-ProRule:PRU00798,
ECO:0000269|PubMed:9233787}.
VARIANT 19 19 P -> S (in dbSNP:rs6874468).
/FTId=VAR_050431.
VARIANT 70 70 N -> S (in dbSNP:rs13359508).
/FTId=VAR_059530.
VARIANT 166 166 R -> H (in OI17; decreased secretion of
the protein; altered secretion of
procollagen type I).
{ECO:0000269|PubMed:26027498}.
/FTId=VAR_075142.
VARIANT 263 263 E -> K (in OI17; no effect on expression
and secretion of the protein; altered
secretion of procollagen type I).
{ECO:0000269|PubMed:26027498}.
/FTId=VAR_075143.
MUTAGEN 166 166 R->A,L,K: Strongly reduced collagen
binding. {ECO:0000269|PubMed:9501084}.
MUTAGEN 173 173 N->A,Q: Strongly reduced collagen
binding. {ECO:0000269|PubMed:9501084}.
MUTAGEN 259 259 L->A: Loss of collagen binding.
{ECO:0000269|PubMed:9501084}.
MUTAGEN 262 262 M->A: Strongly reduced collagen binding.
{ECO:0000269|PubMed:9501084}.
MUTAGEN 263 263 E->A: Loss of collagen binding.
{ECO:0000269|PubMed:9501084}.
CONFLICT 42 43 SV -> PT (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 205 205 R -> L (in Ref. 3; AAA60993).
{ECO:0000305}.
CONFLICT 269 269 F -> L (in Ref. 3; AAA60993).
{ECO:0000305}.
TURN 71 74 {ECO:0000244|PDB:1NUB}.
STRAND 81 85 {ECO:0000244|PDB:1NUB}.
STRAND 91 95 {ECO:0000244|PDB:1NUB}.
HELIX 98 100 {ECO:0000244|PDB:1NUB}.
HELIX 107 109 {ECO:0000244|PDB:1NUB}.
STRAND 111 113 {ECO:0000244|PDB:1NUB}.
TURN 114 116 {ECO:0000244|PDB:2V53}.
STRAND 118 121 {ECO:0000244|PDB:1NUB}.
HELIX 122 131 {ECO:0000244|PDB:1NUB}.
TURN 132 134 {ECO:0000244|PDB:1NUB}.
HELIX 136 140 {ECO:0000244|PDB:1NUB}.
STRAND 143 148 {ECO:0000244|PDB:1NUB}.
HELIX 157 181 {ECO:0000244|PDB:1SRA}.
STRAND 183 188 {ECO:0000244|PDB:1SRA}.
HELIX 190 201 {ECO:0000244|PDB:1SRA}.
HELIX 213 222 {ECO:0000244|PDB:1SRA}.
HELIX 224 227 {ECO:0000244|PDB:1SRA}.
HELIX 228 238 {ECO:0000244|PDB:1SRA}.
STRAND 244 247 {ECO:0000244|PDB:1SRA}.
TURN 249 252 {ECO:0000244|PDB:1SRA}.
HELIX 253 256 {ECO:0000244|PDB:1SRA}.
TURN 257 259 {ECO:0000244|PDB:2V53}.
HELIX 260 262 {ECO:0000244|PDB:2V53}.
HELIX 263 265 {ECO:0000244|PDB:1SRA}.
HELIX 266 273 {ECO:0000244|PDB:1SRA}.
STRAND 278 282 {ECO:0000244|PDB:1SRA}.
HELIX 283 289 {ECO:0000244|PDB:1SRA}.
HELIX 294 296 {ECO:0000244|PDB:1SRA}.
HELIX 299 301 {ECO:0000244|PDB:1SRA}.
SEQUENCE 303 AA; 34632 MW; B914599F79705945 CRC64;
MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV EVGEFDDGAE
ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS CPAPIGEFEK VCSNDNKTFD
SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE
RDEDNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ
HPIDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD
LVI


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E0791r ELISA Basement-membrane protein 40,BM-40,ON,Osteonectin,Rat,Rattus norvegicus,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
U0791r CLIA Basement-membrane protein 40,BM-40,ON,Osteonectin,Rat,Rattus norvegicus,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
E0791r ELISA kit Basement-membrane protein 40,BM-40,ON,Osteonectin,Rat,Rattus norvegicus,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
E0791m ELISA Basement-membrane protein 40,BM-40,Mouse,Mus musculus,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
U0791m CLIA Basement-membrane protein 40,BM-40,Mouse,Mus musculus,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
U0791b CLIA Basement-membrane protein 40,BM-40,Bos taurus,Bovine,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791m ELISA kit Basement-membrane protein 40,BM-40,Mouse,Mus musculus,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,Sparc 96T
E0791b ELISA Basement-membrane protein 40,BM-40,Bos taurus,Bovine,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791b ELISA kit Basement-membrane protein 40,BM-40,Bos taurus,Bovine,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
U0791Rb CLIA Basement-membrane protein 40,BM-40,ON,Oryctolagus cuniculus,Osteonectin,Rabbit,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
U0791h CLIA Basement-membrane protein 40,BM-40,Homo sapiens,Human,ON,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791Rb ELISA kit Basement-membrane protein 40,BM-40,ON,Oryctolagus cuniculus,Osteonectin,Rabbit,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791Rb ELISA Basement-membrane protein 40,BM-40,ON,Oryctolagus cuniculus,Osteonectin,Rabbit,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791h ELISA Basement-membrane protein 40,BM-40,Homo sapiens,Human,ON,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
E0791h ELISA kit Basement-membrane protein 40,BM-40,Homo sapiens,Human,ON,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
10-288-22268F SPARC - Secreted protein acidic and rich in cysteine; Osteonectin; ON; Basement-membrane protein 40; BM-40 0.1 mg
10-288-22268F SPARC - Secreted protein acidic and rich in cysteine; Osteonectin; ON; Basement-membrane protein 40; BM-40 0.05 mg
10-664-50018 SPARC - Secreted protein acidic and rich in cysteine; Osteonectin; ON; Basement-membrane protein 40; BM-40 N_A 0.1 mg
15-288-22268F SPARC - Secreted protein acidic and rich in cysteine; Osteonectin; ON; Basement-membrane protein 40; BM-40 Polyclonal 0.05 mg
15-288-22268F SPARC - Secreted protein acidic and rich in cysteine; Osteonectin; ON; Basement-membrane protein 40; BM-40 Polyclonal 0.1 mg
E0791c ELISA kit Basement-membrane protein 40,BM-40,Chicken,Gallus gallus,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T
U0791c CLIA Basement-membrane protein 40,BM-40,Chicken,Gallus gallus,ON,Osteonectin,Secreted protein acidic and rich in cysteine,SPARC,SPARC 96T


 

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