SPRC_RAT
ID SPRC_RAT Reviewed; 301 AA.
AC P16975; O08953; Q6GSZ4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 4.
DT 03-AUG-2022, entry version 168.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Kidney;
RX PubMed=8660135; DOI=10.1007/s002040050218;
RA Lee M.J., Saijoh K., Nestler E.J., Duman R.S., Sumino K.;
RT "Regional differences in expression of osteonectin mRNA after
RT administration of cadmium to rats.";
RL Arch. Toxicol. 69:590-595(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Sprague-Dawley; TISSUE=Bone;
RX PubMed=9541258; DOI=10.1111/j.1600-0722.1998.tb02208.x;
RA Liao H., Brandsten C., Lundmark C., Christersson C., Wurtz T.;
RT "Osteonectin RNA and collagen alpha1(I) RNA in the developing rat
RT maxilla.";
RL Eur. J. Oral Sci. 106:418-423(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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 [4]
RP PROTEIN SEQUENCE OF 18-34, CALCIUM-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=2322281; DOI=10.1016/0006-291x(90)90677-f;
RA Cheng C.Y.;
RT "Purification of a calcium binding protein (rat SPARC) from primary Sertoli
RT cell-enriched culture medium.";
RL Biochem. Biophys. Res. Commun. 167:1393-1399(1990).
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:2322281}. Note=In or
CC around the basement membrane. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; D28875; BAA06029.1; -; mRNA.
DR EMBL; Y13714; CAA74042.1; -; mRNA.
DR EMBL; BC061777; AAH61777.1; -; mRNA.
DR PIR; A34572; A34572.
DR RefSeq; NP_036788.1; NM_012656.1.
DR AlphaFoldDB; P16975; -.
DR SMR; P16975; -.
DR BioGRID; 246915; 1.
DR IntAct; P16975; 1.
DR STRING; 10116.ENSRNOP00000017486; -.
DR GlyGen; P16975; 1 site.
DR jPOST; P16975; -.
DR PaxDb; P16975; -.
DR PRIDE; P16975; -.
DR GeneID; 24791; -.
DR KEGG; rno:24791; -.
DR UCSC; RGD:3742; rat.
DR CTD; 6678; -.
DR RGD; 3742; Sparc.
DR VEuPathDB; HostDB:ENSRNOG00000012840; -.
DR eggNOG; KOG4004; Eukaryota.
DR HOGENOM; CLU_047416_0_0_1; -.
DR InParanoid; P16975; -.
DR OMA; IWKFCEL; -.
DR OrthoDB; 1528521at2759; -.
DR Reactome; R-RNO-114608; Platelet degranulation.
DR Reactome; R-RNO-3000178; ECM proteoglycans.
DR Reactome; R-RNO-3000497; Scavenging by Class H Receptors.
DR PRO; PR:P16975; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000012840; Expressed in lung and 19 other tissues.
DR Genevisible; P16975; RN.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031012; C:extracellular matrix; ISO:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0016363; C:nuclear matrix; ISO:RGD.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0031091; C:platelet alpha granule; ISO:RGD.
DR GO; GO:0031092; C:platelet alpha granule membrane; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0031982; C:vesicle; IDA:RGD.
DR GO; GO:0005509; F:calcium ion binding; IDA:RGD.
DR GO; GO:0005518; F:collagen binding; ISO:RGD.
DR GO; GO:0050840; F:extracellular matrix binding; ISO:RGD.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0060348; P:bone development; ISO:RGD.
DR GO; GO:0071363; P:cellular response to growth factor stimulus; ISO:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0048839; P:inner ear development; IEP:RGD.
DR GO; GO:0030324; P:lung development; IMP:RGD.
DR GO; GO:0016525; P:negative regulation of angiogenesis; ISO:RGD.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; ISO:RGD.
DR GO; GO:0001503; P:ossification; IEP:RGD.
DR GO; GO:0043473; P:pigmentation; ISO:RGD.
DR GO; GO:0010595; P:positive regulation of endothelial cell migration; ISO:RGD.
DR GO; GO:0022604; P:regulation of cell morphogenesis; ISO:RGD.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0050807; P:regulation of synapse organization; IDA:SynGO.
DR GO; GO:0046686; P:response to cadmium ion; IEP:RGD.
DR GO; GO:0051592; P:response to calcium ion; IEP:RGD.
DR GO; GO:0051591; P:response to cAMP; IEP:RGD.
DR GO; GO:0034097; P:response to cytokine; IEP:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IEP:RGD.
DR GO; GO:0009629; P:response to gravity; IEP:RGD.
DR GO; GO:0033591; P:response to L-ascorbic acid; IEP:RGD.
DR GO; GO:0010288; P:response to lead ion; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0043434; P:response to peptide hormone; IEP:RGD.
DR GO; GO:0042060; P:wound healing; IEP:RGD.
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:2322281"
FT CHAIN 18..301
FT /note="SPARC"
FT /id="PRO_0000020306"
FT DOMAIN 69..91
FT /note="Follistatin-like"
FT DOMAIN 87..149
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 259..294
FT /note="EF-hand"
FT BINDING 272
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 274
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 276
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 283
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 70..81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 75..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 93..128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 99..121
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 110..147
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 153..263
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 271..287
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 61
FT /note="V -> P (in Ref. 1; BAA06029)"
FT /evidence="ECO:0000305"
FT CONFLICT 67
FT /note="E -> CN (in Ref. 1; BAA06029)"
FT /evidence="ECO:0000305"
FT CONFLICT 82..84
FT /note="ELD -> DG (in Ref. 1; BAA06029)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 301 AA; 34296 MW; F522EA716C7EF1A1 CRC64;
MRAWIFFLLC LAGRALAAPQ TEAAEEMVAE ETVVEETGLP VGANPVQVEM GEFEEGAEET
VEEVVAENPC QNHHCKHGKV CELDESNTPM CVCQDPTSCP APIGEFEKVC SNDNKTFDSS
CHFFATKCTL EGTKKGHKLH LDYIGPCKYI APCLDSELTE FPLRMRDWLK NVLVTLYERD
EGNNLLTEKQ KLRVKKIHEN EKRLEAGDHP VELLARDFEK NYNMYIFPVH WQFGQLDQHP
IDGYLSHTEL APLRAPLIPM EHCTTRFFET CDLDNDKYIA LEEWAGCFGI KEQDINKDLV
I
