SPRC_CAEEL
ID SPRC_CAEEL Reviewed; 264 AA.
AC P34714;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 03-AUG-2022, entry version 164.
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=ost-1; Synonyms=sparc; ORFNames=C44B12.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND TISSUE SPECIFICITY.
RC STRAIN=Bristol N2;
RX PubMed=8257796; DOI=10.1091/mbc.4.9.941;
RA Schwarzbauer J.E., Spencer C.S.;
RT "The Caenorhabditis elegans homologue of the extracellular calcium binding
RT protein SPARC/osteonectin affects nematode body morphology and mobility.";
RL Mol. Biol. Cell 4:941-952(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Has a high affinity for collagen. Affects nematode body
CC morphology and mobility. Essential for C.elegans development and muscle
CC function. The cysteine-rich region could have protease inhibitory
CC activity or may provide the framework for a protein binding module.
CC Probable role in skeletal morphogenesis.
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: Expressed by body wall and sex muscle cells.
CC Probable association with basement membranes.
CC {ECO:0000269|PubMed:8257796}.
CC -!- DEVELOPMENTAL STAGE: First expressed in unhatched larvae; continuous
CC throughout subsequent larval stages and in adults.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; L21758; AAA16827.1; -; Unassigned_DNA.
DR EMBL; FO080852; CCD67228.1; -; Genomic_DNA.
DR PIR; A47737; A47737.
DR RefSeq; NP_500039.1; NM_067638.6.
DR AlphaFoldDB; P34714; -.
DR SMR; P34714; -.
DR BioGRID; 42089; 7.
DR STRING; 6239.C44B12.2a; -.
DR EPD; P34714; -.
DR PaxDb; P34714; -.
DR PeptideAtlas; P34714; -.
DR EnsemblMetazoa; C44B12.2a.1; C44B12.2a.1; WBGene00003893.
DR GeneID; 176931; -.
DR KEGG; cel:CELE_C44B12.2; -.
DR UCSC; C44B12.2; c. elegans.
DR CTD; 176931; -.
DR WormBase; C44B12.2a; CE08703; WBGene00003893; ost-1.
DR eggNOG; KOG4004; Eukaryota.
DR HOGENOM; CLU_047416_1_0_1; -.
DR InParanoid; P34714; -.
DR OMA; IWKFCEL; -.
DR OrthoDB; 1528521at2759; -.
DR PhylomeDB; P34714; -.
DR Reactome; R-CEL-114608; Platelet degranulation.
DR Reactome; R-CEL-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-CEL-8957275; Post-translational protein phosphorylation.
DR PRO; PR:P34714; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003893; Expressed in larva and 3 other tissues.
DR ExpressionAtlas; P34714; baseline and differential.
DR GO; GO:0005604; C:basement membrane; IDA:WormBase.
DR GO; GO:0005615; C:extracellular space; IDA:WormBase.
DR GO; GO:0005509; F:calcium ion binding; IDA:WormBase.
DR GO; GO:0005518; F:collagen binding; IBA:GO_Central.
DR GO; GO:0050840; F:extracellular matrix binding; IBA:GO_Central.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
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 Pfam; PF09289; FOLN; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF10591; SPARC_Ca_bdg; 1.
DR SMART; SM00274; FOLN; 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; Developmental protein; Disulfide bond;
KW Extracellular matrix; Glycoprotein; Metal-binding; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..16
FT /evidence="ECO:0000255"
FT CHAIN 17..264
FT /note="SPARC"
FT /id="PRO_0000020311"
FT DOMAIN 52..74
FT /note="Follistatin-like"
FT DOMAIN 68..137
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 224..259
FT /note="EF-hand"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 243
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 53..64
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 58..74
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 76..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 80..103
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 92..135
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 141..228
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 236..252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 264 AA; 30173 MW; 2F952056B466E18F CRC64;
MRYALAACLL LLAASSFVDA KKKKIADDEL GELLDNIDAD EEKKSVEPAK NPCEDHQCGW
GKECVVGKKG EPTCECISKC PELDGDPMDK VCANNNQTFT SLCDLYRERC LCKRKSKECS
KAFNAKVHLE YLGECKKLDE CTEEHMAQFP ERMADWLFQV MKELKKRREL HKLEWEELLS
EAENDDEKKH VYPVIWKFCE LDTKPHDKSV SHHELIPITA PVIPMESCIK PFLEGCDANN
DGNISIKEWG KCLGLKEGEI QERC
