ID Q5NCU3_MOUSE Unreviewed; 172 AA. AC Q5NCU3; DT 05-FEB-2008, integrated into UniProtKB/TrEMBL. DT 05-FEB-2008, sequence version 1. DT 25-MAY-2022, entry version 87. DE RecName: Full=SPARC {ECO:0000256|ARBA:ARBA00019049}; DE AltName: Full=Osteonectin {ECO:0000256|ARBA:ARBA00032081}; DE AltName: Full=Secreted protein acidic and rich in cysteine {ECO:0000256|ARBA:ARBA00031976}; DE Flags: Fragment; GN Name=Sparc {ECO:0000313|Ensembl:ENSMUSP00000119475, GN ECO:0000313|MGI:MGI:98373}; 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 {ECO:0000313|Ensembl:ENSMUSP00000119475, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000119475, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119475, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000119475} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000119475}; RG Ensembl; RL Submitted (FEB-2012) to UniProtKB. 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. {ECO:0000256|ARBA:ARBA00025574}. CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. CC Secreted, extracellular space, extracellular matrix, basement membrane CC {ECO:0000256|ARBA:ARBA00004302}. CC -!- SIMILARITY: Belongs to the SPARC family. CC {ECO:0000256|ARBA:ARBA00006404}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR SMR; Q5NCU3; -. DR jPOST; Q5NCU3; -. DR MaxQB; Q5NCU3; -. DR PeptideAtlas; Q5NCU3; -. DR PRIDE; Q5NCU3; -. DR ProteomicsDB; 350855; -. DR Antibodypedia; 878; 788 antibodies from 42 providers. DR Ensembl; ENSMUST00000141530.2; ENSMUSP00000119475.2; ENSMUSG00000018593.14. DR MGI; MGI:98373; Sparc. DR VEuPathDB; HostDB:ENSMUSG00000018593; -. DR GeneTree; ENSGT00510000046787; -. DR HOGENOM; CLU_141982_0_0_1; -. DR ChiTaRS; Sparc; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000018593; Expressed in vault of skull and 351 other tissues. DR ExpressionAtlas; Q5NCU3; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005615; C:extracellular space; IEA:InterPro. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005518; F:collagen binding; IEA:InterPro. 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 PANTHER; PTHR13866:SF6; PTHR13866:SF6; 1. DR Pfam; PF09289; FOLN; 1. DR Pfam; PF00050; Kazal_1; 1. DR SMART; SM00274; FOLN; 1. DR SMART; SM00280; KAZAL; 1. DR SUPFAM; SSF100895; SSF100895; 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 {ECO:0000256|ARBA:ARBA00022869}; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022869}; KW Proteomics identification {ECO:0007829|EPD:Q5NCU3, KW ECO:0007829|MaxQB:Q5NCU3}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Secreted {ECO:0000256|ARBA:ARBA00022869}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1..17 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 18..172 FT /note="SPARC" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5004260259" FT DOMAIN 91..148 FT /note="Kazal-like" FT /evidence="ECO:0000259|PROSITE:PS51465" FT NON_TER 172 FT /evidence="ECO:0000313|Ensembl:ENSMUSP00000119475" SQ SEQUENCE 172 AA; 19096 MW; CAEEDC2D79984AF0 CRC64; MRAWIFFLLC LAGRALAAPT EVAEEIVEEE TVVEETGVPV GANPVQVEMG EFEDGAEETV EEVVADNPCQ NHHCKHGKVC ELDESNTPMC VCQDPTSCPA PIGEFEKVCS NDNKTFDSSC HFFATKCTLE GTKKGHKLHL DYIGPCKYIA PCLDSELTEF PLRMRDWLKN VL //