ID A0A1L1SSH9_MOUSE Unreviewed; 332 AA. AC A0A1L1SSH9; DT 15-FEB-2017, integrated into UniProtKB/TrEMBL. DT 15-FEB-2017, sequence version 1. DT 10-FEB-2021, entry version 28. DE RecName: Full=Osteonectin {ECO:0000256|ARBA:ARBA00014262}; DE AltName: Full=SPARC {ECO:0000256|ARBA:ARBA00019049}; DE AltName: Full=Secreted protein acidic and rich in cysteine {ECO:0000256|ARBA:ARBA00019366}; GN Name=Sparc {ECO:0000313|Ensembl:ENSMUSP00000149918, 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, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000149918, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000149918, 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:0000213|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} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000149918}; RG Ensembl; RL Submitted (DEC-2016) to UniProtKB. 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 EMBL; AL596207; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL772268; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR SMR; A0A1L1SSH9; -. DR Antibodypedia; 878; 758 antibodies. DR Ensembl; ENSMUST00000213866; ENSMUSP00000149604; ENSMUSG00000018593. DR Ensembl; ENSMUST00000216313; ENSMUSP00000149918; ENSMUSG00000018593. DR MGI; MGI:98373; Sparc. DR GeneTree; ENSGT00510000046787; -. DR ChiTaRS; Sparc; mouse. DR Proteomes; UP000000589; Chromosome 11. DR ExpressionAtlas; A0A1L1SSH9; 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; 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 {ECO:0000256|ARBA:ARBA00022869}; 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 Proteomics identification {ECO:0000213|EPD:A0A1L1SSH9, KW ECO:0000213|MaxQB:A0A1L1SSH9, ECO:0000213|PeptideAtlas: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="Osteonectin" 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 //