SPRC_PIG
ID SPRC_PIG Reviewed; 300 AA.
AC P20112; Q4Z8Q2;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 114.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 18-30 AND 216-228.
RC TISSUE=Enamel epithelium;
RX PubMed=16674666; DOI=10.1111/j.1600-0722.2006.00280.x;
RA Chun Y.-H.P., Yamakoshi Y., Kim J.-W., Iwata T., Hu J.C.-C., Simmer J.P.;
RT "Porcine SPARC: isolation from dentin, cDNA sequence, and computer model.";
RL Eur. J. Oral Sci. 114:78-85(2006).
RN [2]
RP PROTEIN SEQUENCE OF 18-52, AND CHARACTERIZATION.
RX PubMed=3421938; DOI=10.1042/bj2530139;
RA Domenicucci C., Goldberg H.A., Hofmann T., Isenman D., Wasi S., Sodek J.;
RT "Characterization of porcine osteonectin extracted from foetal calvariae.";
RL Biochem. J. 253:139-151(1988).
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. Note=In or around the basement membrane.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; AY963262; AAX83050.1; -; mRNA.
DR PIR; S00998; S00998.
DR RefSeq; NP_001026964.1; NM_001031794.1.
DR AlphaFoldDB; P20112; -.
DR SMR; P20112; -.
DR STRING; 9823.ENSSSCP00000018098; -.
DR PaxDb; P20112; -.
DR PeptideAtlas; P20112; -.
DR Ensembl; ENSSSCT00005028103; ENSSSCP00005017157; ENSSSCG00005017688.
DR Ensembl; ENSSSCT00005028143; ENSSSCP00005017187; ENSSSCG00005017688.
DR Ensembl; ENSSSCT00005028179; ENSSSCP00005017209; ENSSSCG00005017688.
DR Ensembl; ENSSSCT00015032407; ENSSSCP00015012870; ENSSSCG00015024195.
DR Ensembl; ENSSSCT00025051623; ENSSSCP00025022032; ENSSSCG00025037875.
DR Ensembl; ENSSSCT00030010505; ENSSSCP00030004544; ENSSSCG00030007808.
DR Ensembl; ENSSSCT00035066175; ENSSSCP00035026843; ENSSSCG00035049628.
DR Ensembl; ENSSSCT00040105033; ENSSSCP00040047984; ENSSSCG00040075656.
DR Ensembl; ENSSSCT00045006510; ENSSSCP00045004433; ENSSSCG00045003926.
DR Ensembl; ENSSSCT00050077449; ENSSSCP00050033326; ENSSSCG00050056796.
DR Ensembl; ENSSSCT00060084460; ENSSSCP00060036582; ENSSSCG00060061892.
DR Ensembl; ENSSSCT00065046549; ENSSSCP00065019995; ENSSSCG00065034205.
DR GeneID; 595124; -.
DR KEGG; ssc:595124; -.
DR CTD; 6678; -.
DR eggNOG; KOG4004; Eukaryota.
DR InParanoid; P20112; -.
DR OrthoDB; 1528521at2759; -.
DR Reactome; R-SSC-114608; Platelet degranulation.
DR Reactome; R-SSC-3000178; ECM proteoglycans.
DR Reactome; R-SSC-3000497; Scavenging by Class H Receptors.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
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; 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:16674666,
FT ECO:0000269|PubMed:3421938"
FT CHAIN 18..300
FT /note="SPARC"
FT /id="PRO_0000160590"
FT DOMAIN 68..90
FT /note="Follistatin-like"
FT DOMAIN 86..148
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 258..293
FT /note="EF-hand"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 277
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 282
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 113
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 69..80
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 74..90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 92..127
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 98..120
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 109..146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 152..262
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 270..286
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 300 AA; 34240 MW; 2462A2D7C6FE6CB5 CRC64;
MRAWIFFLLC LAGKALAAPQ QEALPDETEV VEETVAEVPV GANPVQVEVG EFDDGAEEAE
EEVVAENPCQ NHHCKHGKVC ELDENNSPMC VCQDPTSCPA PIGEFEKVCS NDNKTFDSSC
HFFATKCTLE GTKKGHKLHL DYIGPCKYIP PCLDSELTEF PLRMRDWLKN VLVTLYERDE
NNNLLTEKQK LRVKKIHENE KRLEAGDHPV ELLARDFEKN YNMYIFPVHW QFGQLDQHPI
DGYLSHTELA PLRAPLIPME HCTTRFFQTC DLDNDKYIAL DEWAGCFGIK EQDIDKDLVI
