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SPARC (Osteonectin) (ON) (Secreted protein acidic and rich in cysteine)

 SPRC_PONAB              Reviewed;         303 AA.
Q5R767; Q5R433;
10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
21-DEC-2004, sequence version 1.
30-AUG-2017, entry version 69.
RecName: Full=SPARC;
AltName: Full=Osteonectin;
Short=ON;
AltName: Full=Secreted protein acidic and rich in cysteine;
Flags: Precursor;
Name=SPARC;
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Pongo.
NCBI_TaxID=9601;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex, and Heart;
The German cDNA consortium;
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
-!- 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 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000250}. Note=In or around the
basement membrane. {ECO:0000250}.
-!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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EMBL; CR860251; CAH92393.1; -; mRNA.
EMBL; CR861427; CAH93483.1; -; mRNA.
RefSeq; NP_001127042.1; NM_001133570.1.
RefSeq; NP_001128859.1; NM_001135387.1.
UniGene; Pab.19702; -.
ProteinModelPortal; Q5R767; -.
SMR; Q5R767; -.
PRIDE; Q5R767; -.
GeneID; 100174069; -.
GeneID; 100189783; -.
KEGG; pon:100174069; -.
KEGG; pon:100189783; -.
CTD; 6678; -.
HOVERGEN; HBG002746; -.
InParanoid; Q5R767; -.
Proteomes; UP000001595; Unplaced.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0007165; P:signal transduction; IEA:InterPro.
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; 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.
2: Evidence at transcript level;
Basement membrane; Calcium; Complete proteome; Copper; Disulfide bond;
Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
Secreted; Signal.
SIGNAL 1 17 {ECO:0000250}.
CHAIN 18 303 SPARC.
/FTId=PRO_0000293538.
DOMAIN 71 93 Follistatin-like.
DOMAIN 89 151 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 261 296 EF-hand.
CA_BIND 274 285 {ECO:0000250}.
COMPBIAS 22 69 Asp/Glu-rich (acidic; binds calcium).
CARBOHYD 116 116 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
DISULFID 72 83 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 77 93 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 95 130 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 101 123 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 112 149 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 155 265 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 273 289 {ECO:0000255|PROSITE-ProRule:PRU00798}.
CONFLICT 94 94 V -> M (in Ref. 1; CAH93483).
{ECO:0000305}.
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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