SPRC_MOUSE
ID SPRC_MOUSE Reviewed; 302 AA.
AC P07214;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=SPARC;
DE AltName: Full=Basement-membrane protein 40;
DE Short=BM-40;
DE AltName: Full=Osteonectin;
DE Short=ON;
DE AltName: Full=Secreted protein acidic and rich in cysteine;
DE Flags: Precursor;
GN Name=Sparc;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Placenta;
RX PubMed=3410046; DOI=10.1016/0014-5793(88)80054-1;
RA Lankat-Buttgereit B., Mann K., Deutzmann R., Timpl R., Krieg T.;
RT "Cloning and complete amino acid sequences of human and murine basement
RT membrane protein BM-40 (SPARC, osteonectin).";
RL FEBS Lett. 236:352-356(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3755680; DOI=10.1002/j.1460-2075.1986.tb04383.x;
RA Mason I.J., Taylor A., Williams J.G., Sage H., Hogan B.L.M.;
RT "Evidence from molecular cloning that SPARC, a major product of mouse
RT embryo parietal endoderm, is related to an endothelial cell 'culture shock'
RT glycoprotein of Mr 43,000.";
RL EMBO J. 5:1465-1472(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3165375; DOI=10.1016/s0021-9258(18)37929-8;
RA McVey J.H., Nomura S., Kelly P., Mason I.J., Hogan B.L.M.;
RT "Characterization of the mouse SPARC/osteonectin gene. Intron/exon
RT organization and an unusual promoter region.";
RL J. Biol. Chem. 263:11111-11116(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 18-37 AND 215-234.
RX PubMed=3109947; DOI=10.1016/0014-5793(87)81040-2;
RA Mann K., Deutzmann R., Paulsson M., Timpl R.;
RT "Solubilization of protein BM-40 from a basement membrane tumor with
RT chelating agents and evidence for its identity with osteonectin and
RT SPARC.";
RL FEBS Lett. 218:167-172(1987).
RN [6]
RP GLYCOSYLATION, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=3427055; DOI=10.1021/bi00396a015;
RA Engel J., Taylor W., Paulsson M., Sage H., Hogan B.L.M.;
RT "Calcium binding domains and calcium-induced conformational transition of
RT SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in
RT mineralized and nonmineralized tissues.";
RL Biochemistry 26:6958-6965(1987).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix, basement membrane {ECO:0000269|PubMed:3427055}. Note=In or
CC around the basement membrane.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in tissues undergoing
CC morphogenesis, remodeling and wound repair.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:3427055}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; X04017; CAA27642.1; -; mRNA.
DR EMBL; M20692; AAA40125.1; -; Genomic_DNA.
DR EMBL; M20684; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20685; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20686; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20687; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20688; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20689; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20690; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; M20691; AAA40125.1; JOINED; Genomic_DNA.
DR EMBL; BC004638; AAH04638.1; -; mRNA.
DR CCDS; CCDS24712.1; -.
DR PIR; A29227; GEMSN.
DR RefSeq; NP_033268.1; NM_009242.5.
DR AlphaFoldDB; P07214; -.
DR SMR; P07214; -.
DR BioGRID; 203423; 3.
DR IntAct; P07214; 3.
DR STRING; 10090.ENSMUSP00000018737; -.
DR GlyConnect; 2736; 9 N-Linked glycans (1 site).
DR GlyGen; P07214; 1 site, 9 N-linked glycans (1 site).
DR iPTMnet; P07214; -.
DR PhosphoSitePlus; P07214; -.
DR CPTAC; non-CPTAC-3394; -.
DR jPOST; P07214; -.
DR PaxDb; P07214; -.
DR PeptideAtlas; P07214; -.
DR PRIDE; P07214; -.
DR ProteomicsDB; 263324; -.
DR Antibodypedia; 878; 783 antibodies from 43 providers.
DR DNASU; 20692; -.
DR Ensembl; ENSMUST00000018737; ENSMUSP00000018737; ENSMUSG00000018593.
DR Ensembl; ENSMUST00000214685; ENSMUSP00000151000; ENSMUSG00000018593.
DR GeneID; 20692; -.
DR KEGG; mmu:20692; -.
DR UCSC; uc007izh.3; mouse.
DR CTD; 6678; -.
DR MGI; MGI:98373; Sparc.
DR VEuPathDB; HostDB:ENSMUSG00000018593; -.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR InParanoid; P07214; -.
DR OrthoDB; 1528521at2759; -.
DR PhylomeDB; P07214; -.
DR TreeFam; TF319356; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR Reactome; R-MMU-3000178; ECM proteoglycans.
DR Reactome; R-MMU-3000497; Scavenging by Class H Receptors.
DR BioGRID-ORCS; 20692; 1 hit in 75 CRISPR screens.
DR ChiTaRS; Sparc; mouse.
DR PRO; PR:P07214; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P07214; protein.
DR Bgee; ENSMUSG00000018593; Expressed in vault of skull and 315 other tissues.
DR ExpressionAtlas; P07214; baseline and differential.
DR Genevisible; P07214; MM.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0031012; C:extracellular matrix; IDA:MGI.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0031091; C:platelet alpha granule; ISO:MGI.
DR GO; GO:0031092; C:platelet alpha granule membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0031982; C:vesicle; ISO:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:CAFA.
DR GO; GO:0005518; F:collagen binding; ISO:MGI.
DR GO; GO:0050840; F:extracellular matrix binding; IDA:MGI.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; IMP:MGI.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
DR GO; GO:0030324; P:lung development; ISO:MGI.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:MGI.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0043473; P:pigmentation; IMP:MGI.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:MGI.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:MGI.
DR GO; GO:0042127; P:regulation of cell population proliferation; IGI:MGI.
DR GO; GO:0050807; P:regulation of synapse organization; ISO:MGI.
DR DisProt; DP00052; -.
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 1: Evidence at protein level;
KW Basement membrane; Calcium; Copper; Direct protein sequencing;
KW Disulfide bond; Extracellular matrix; Glycoprotein; Metal-binding;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000269|PubMed:3109947"
FT CHAIN 18..302
FT /note="SPARC"
FT /id="PRO_0000020305"
FT DOMAIN 70..92
FT /note="Follistatin-like"
FT DOMAIN 88..150
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 260..295
FT /note="EF-hand"
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 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 279
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 284
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:3427055"
FT DISULFID 71..82
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 76..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 94..129
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 100..122
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 111..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 154..264
FT DISULFID 272..288
SQ SEQUENCE 302 AA; 34450 MW; A1FF717CA32F0F5C CRC64;
MRAWIFFLLC LAGRALAAPQ QTEVAEEIVE EETVVEETGV PVGANPVQVE MGEFEDGAEE
TVEEVVADNP CQNHHCKHGK VCELDESNTP MCVCQDPTSC PAPIGEFEKV CSNDNKTFDS
SCHFFATKCT LEGTKKGHKL HLDYIGPCKY IAPCLDSELT EFPLRMRDWL KNVLVTLYER
DEGNNLLTEK QKLRVKKIHE NEKRLEAGDH PVELLARDFE KNYNMYIFPV HWQFGQLDQH
PIDGYLSHTE LAPLRAPLIP MEHCTTRFFE TCDLDNDKYI ALEEWAGCFG IKEQDINKDL
VI
