SPRC_COTJA
ID SPRC_COTJA Reviewed; 298 AA.
AC O93390;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=SPARC;
DE AltName: Full=Osteonectin;
DE Short=ON;
DE AltName: Full=Secreted protein acidic and rich in cysteine;
DE Flags: Precursor;
GN Name=SPARC;
OS Coturnix japonica (Japanese quail) (Coturnix coturnix japonica).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Perdicinae; Coturnix.
OX NCBI_TaxID=93934;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Weiskirchen R., Bister K.;
RT "Isolation of quail osteonectin cDNA.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Appears to regulate cell growth through interactions with the
CC extracellular matrix and cytokines. Binds calcium and copper, several
CC types of collagen, albumin, thrombospondin, PDGF and cell membranes.
CC There are two calcium binding sites; an acidic domain that binds 5 to 8
CC Ca(2+) with a low affinity and an EF-hand loop that binds a Ca(2+) ion
CC with a high affinity (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000250}. Note=In or around the basement
CC membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; AF077327; AAD12179.1; -; mRNA.
DR RefSeq; XP_015731286.1; XM_015875800.1.
DR AlphaFoldDB; O93390; -.
DR SMR; O93390; -.
DR Ensembl; ENSCJPT00005011895; ENSCJPP00005007746; ENSCJPG00005007052.
DR GeneID; 107320174; -.
DR KEGG; cjo:107320174; -.
DR CTD; 6678; -.
DR GeneTree; ENSGT00510000046787; -.
DR OrthoDB; 1528521at2759; -.
DR Proteomes; UP000694412; Chromosome 13.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
DR GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR015369; Follistatin/Osteonectin_EGF.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR001999; Osteonectin_CS.
DR InterPro; IPR037641; SPARC.
DR InterPro; IPR019577; SPARC/Testican_Ca-bd-dom.
DR PANTHER; PTHR13866:SF6; PTHR13866:SF6; 1.
DR Pfam; PF09289; FOLN; 1.
DR Pfam; PF00050; Kazal_1; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR SMART; SM00274; FOLN; 1.
DR SMART; SM00280; KAZAL; 1.
DR SUPFAM; SSF100895; SSF100895; 1.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS00612; OSTEONECTIN_1; 1.
DR PROSITE; PS00613; OSTEONECTIN_2; 1.
PE 2: Evidence at transcript level;
KW Basement membrane; Calcium; Copper; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..298
FT /note="SPARC"
FT /id="PRO_0000020309"
FT DOMAIN 66..88
FT /note="Follistatin-like"
FT DOMAIN 84..146
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 256..291
FT /note="EF-hand"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 90..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 96..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 107..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 150..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 268..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ 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
