SPRC_XENLA
ID SPRC_XENLA Reviewed; 300 AA.
AC P36378;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1736898; DOI=10.1042/bj2810513;
RA Damjanovski S., Liu F., Ringuette M.J.;
RT "Molecular analysis of Xenopus laevis SPARC (Secreted Protein, Acidic, Rich
RT in Cysteine). A highly conserved acidic calcium-binding extracellular-
RT matrix protein.";
RL Biochem. J. 281:513-517(1992).
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:0000269|PubMed:1736898}. Note=In or
CC around the basement membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in long bone (at protein level).
CC {ECO:0000269|PubMed:1736898}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; X62483; CAA44350.1; -; mRNA.
DR PIR; S18992; S18992.
DR AlphaFoldDB; P36378; -.
DR SMR; P36378; -.
DR Proteomes; UP000186698; Genome assembly.
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; 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; Disulfide bond; Extracellular matrix;
KW Glycoprotein; Metal-binding; Reference proteome; Secreted; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..300
FT /note="SPARC"
FT /id="PRO_0000020310"
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:0000255"
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; 34596 MW; 673E5875E3B7BBCA CRC64;
MRVWVFFVLC LAGKALAAPQ QDALPEEEEV IEDVPAEETV GTNPVQVDVG EFDEAINEEE
EEEPSENPCL NHHCKHGKVC EVDESNTPLC VCQDPSTCPT SVGEFEKICG TDNKTYDSSC
HFFATKCTLE GTKKGHKLHL DYIGPCKYIA PCLDNELSEF PLRIGDWLKN VLVSLYERDE
NNNLLNEKQK LRVKKIHENE KRLESWRPHS ELLVRDFEKN YNMYIFPVHW QFGQLDQHPI
DGYLSHTELS PLRAPLIPME HCTTRFFDEC DIDDDKYIAL EEWAKCFGIK EQDVDKDMIV
