ID A0A1L1SSH9_MOUSE Unreviewed; 332 AA. AC A0A1L1SSH9; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 03-MAY-2023, entry version 38. 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}; GN Name=Sparc {ECO:0000313|Ensembl:ENSMUSP00000149918.2, 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:ENSMUSP00000149918.2, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000149918.2, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000149918.2, 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:ENSMUSP00000149918.2} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000149918.2}; RG Ensembl; RL Submitted (JAN-2023) 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 ProteomicsDB; 341474; -. DR Antibodypedia; 878; 804 antibodies from 43 providers. DR Ensembl; ENSMUST00000213866.2; ENSMUSP00000149604.2; ENSMUSG00000018593.14. DR Ensembl; ENSMUST00000216313.2; ENSMUSP00000149918.2; ENSMUSG00000018593.14. DR AGR; MGI:98373; -. DR MGI; MGI:98373; Sparc. DR VEuPathDB; HostDB:ENSMUSG00000018593; -. DR GeneTree; ENSGT00510000046787; -. DR ChiTaRS; Sparc; mouse. DR Proteomes; UP000000589; Chromosome 11. DR Bgee; ENSMUSG00000018593; Expressed in vault of skull and 315 other tissues. 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 1: Evidence at protein level; KW Basement membrane {ECO:0000256|ARBA:ARBA00022869}; KW Calcium {ECO:0000256|ARBA:ARBA00022837}; KW Copper {ECO:0000256|ARBA:ARBA00023008}; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637641-50}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Proteomics identification {ECO:0007829|EPD:A0A1L1SSH9, KW ECO:0007829|MaxQB:A0A1L1SSH9}; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..47 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 48..332 FT /note="SPARC" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015066558" FT DOMAIN 123..180 FT /note="Kazal-like" FT /evidence="ECO:0000259|PROSITE:PS51465" FT DISULFID 101..112 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 106..122 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 124..159 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 130..152 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 141..178 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 184..294 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" FT DISULFID 302..318 FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50" SQ SEQUENCE 332 AA; 37837 MW; 9B402D49F6947EC8 CRC64; MRQPFRPPEL FCRLPACLPA CLPVPRVPSI 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 //