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

 SPRC_COTJA              Reviewed;         298 AA.
O93390;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
05-JUL-2017, entry version 84.
RecName: Full=SPARC;
AltName: Full=Osteonectin;
Short=ON;
AltName: Full=Secreted protein acidic and rich in cysteine;
Flags: Precursor;
Name=SPARC;
Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Perdicinae; Coturnix.
NCBI_TaxID=93934;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Weiskirchen R., Bister K.;
"Isolation of quail osteonectin cDNA.";
Submitted (JUL-1998) 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; AF077327; AAD12179.1; -; mRNA.
RefSeq; XP_015731286.1; XM_015875800.1.
ProteinModelPortal; O93390; -.
SMR; O93390; -.
PRIDE; O93390; -.
GeneID; 107320174; -.
KEGG; cjo:107320174; -.
CTD; 6678; -.
HOVERGEN; HBG002746; -.
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; Copper; Disulfide bond;
Extracellular matrix; Glycoprotein; Metal-binding; Secreted; Signal.
SIGNAL 1 17 {ECO:0000250}.
CHAIN 18 298 SPARC.
/FTId=PRO_0000020309.
DOMAIN 66 88 Follistatin-like.
DOMAIN 84 146 Kazal-like. {ECO:0000255|PROSITE-
ProRule:PRU00798}.
DOMAIN 256 291 EF-hand.
CA_BIND 269 280 {ECO:0000250}.
COMPBIAS 21 64 Asp/Glu-rich (acidic; binds calcium).
CARBOHYD 111 111 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 67 78 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 72 88 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 90 125 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 96 118 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 107 144 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 150 260 {ECO:0000255|PROSITE-ProRule:PRU00798}.
DISULFID 268 284 {ECO:0000255|PROSITE-ProRule:PRU00798}.
SEQUENCE 298 AA; 34052 MW; 61B4FF59AF6C6D3F CRC64;
MRAWIFFLLC LAGKALAAPQ EALPDETEVI EDVTTEEPVG ANPVQVEVGE FEEPTEDVEE
IVAENPCQNH HCKHGKVCEV DDNNSPMCVC QDPSSCPATS GVFEKVCGTD NKTYDSSCHF
FATKCTLEGT KKGHKLHLDY IGPCKFIPPC LDTELTEFPL RMRDWLKNVL ITLYERDEDN
NLLTEKQKLK VKKIHENEKR LEAGDHTVEL LARDFEKNYN MYIFPVHWQF GQLDQHPIDG
YLSHTELAPL RAPLIPMEHC TTRFFEACDL DNDKYIALEE WASCFGIKEK DIDKDLVI


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