ID   SPRC_RABIT              Reviewed;         273 AA.
AC   P36233; Q9GLL0;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   04-MAY-2001, sequence version 2.
DT   25-MAY-2022, entry version 119.
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; Fragment;
GN   Name=SPARC;
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bluteau G., Mathieu P., Conrozier T., Vignon E., Herbage D.,
RA   Mallein-Gerin F.;
RT   "Differential gene expression of matrix metalloproteinases-1, -3, -13 and
RT   aggrecanases-1, -2 in a rabbit model of osteoarthritis.";
RL   Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 18-27, TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=New Zealand white; TISSUE=Cartilage;
RX   PubMed=8130279; DOI=10.1016/0167-4889(94)90209-7;
RA   Chandrasekhar S., Harvey A.K., Johnson M.G., Becker G.W.;
RT   "Osteonectin/SPARC is a product of articular chondrocytes/cartilage and is
RT   regulated by cytokines and growth factors.";
RL   Biochim. Biophys. Acta 1221:7-14(1994).
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   -!- TISSUE SPECIFICITY: Detected in chondrocytes.
CC       {ECO:0000269|PubMed:8130279}.
CC   -!- INDUCTION: By growth factors such as TGF-beta, PDGF, IGF1.
CC       {ECO:0000269|PubMed:8130279}.
CC   -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR   EMBL; AF247647; AAG17615.1; -; mRNA.
DR   PIR; S16170; S16170.
DR   AlphaFoldDB; P36233; -.
DR   SMR; P36233; -.
DR   STRING; 9986.ENSOCUP00000010424; -.
DR   PRIDE; P36233; -.
DR   eggNOG; KOG4004; Eukaryota.
DR   InParanoid; P36233; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
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; 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; 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; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000269|PubMed:8130279"
FT   CHAIN           18..>273
FT                   /note="SPARC"
FT                   /id="PRO_0000020307"
FT   DOMAIN          73..95
FT                   /note="Follistatin-like"
FT   DOMAIN          91..153
FT                   /note="Kazal-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DOMAIN          263..>273
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        74..85
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        79..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        97..132
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        103..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        114..151
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   DISULFID        157..267
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT   NON_TER         273
SQ   SEQUENCE   273 AA;  31141 MW;  14436E3F4F0D4C68 CRC64;
     MKAWIFFLVC LAGRALAAPQ QEALPDETEV VEETVAEVAE VAEVPVGANP VQVEVGEFEE
     VEETEEEVVA ENPCQNHHCK HGKVCELDEN NTPMCVCQDP TSCPAPVGEF EKVCSNDNKT
     FDSSCHFFAT KCTLEGTKKG HKLHLDYIGP CKYIPPCLDS ELSEFPLRMR DWLKNVLVTL
     YERDEGNNLL TEKQKLRVKK IHENEKRLEA GDHPVELLAR DFEKNYNMYI FPVHWQFGQL
     DQHPIDGYLS HTELAPLRAP LIPMEHCTTR FFE