ID SPRC_PONAB Reviewed; 303 AA.
AC Q5R767; Q5R433;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 24-JAN-2024, entry version 85.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain cortex, and Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860251; CAH92393.1; -; mRNA.
DR EMBL; CR861427; CAH93483.1; -; mRNA.
DR RefSeq; NP_001127042.1; NM_001133570.1.
DR RefSeq; NP_001128859.1; NM_001135387.1.
DR AlphaFoldDB; Q5R767; -.
DR SMR; Q5R767; -.
DR GlyCosmos; Q5R767; 1 site, No reported glycans.
DR Ensembl; ENSPPYT00000057620.1; ENSPPYP00000032437.1; ENSPPYG00000030691.1.
DR GeneID; 100174069; -.
DR GeneID; 100189783; -.
DR KEGG; pon:100174069; -.
DR CTD; 6678; -.
DR GeneTree; ENSGT00510000046787; -.
DR InParanoid; Q5R767; -.
DR OMA; IWKFCEL; -.
DR OrthoDB; 4695638at2759; -.
DR Proteomes; UP000001595; Chromosome 5.
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 CDD; cd16231; EFh_SPARC_like; 1.
DR CDD; cd01328; FSL_SPARC; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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; IPR019577; SPARC/Testican_Ca-bd-dom.
DR InterPro; IPR037641; SPARC_FS.
DR PANTHER; PTHR13866:SF6; SPARC; 1.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 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..303
FT /note="SPARC"
FT /id="PRO_0000293538"
FT DOMAIN 71..93
FT /note="Follistatin-like"
FT DOMAIN 89..151
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 261..296
FT /note="EF-hand"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 278
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 BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 72..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 77..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 95..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 101..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 112..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 155..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 273..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 94
FT /note="V -> M (in Ref. 1; CAH93483)"
FT /evidence="ECO:0000305"
SQ 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
//
