SPRC_BOVIN
ID SPRC_BOVIN Reviewed; 303 AA.
AC P13213; A5D9C9; Q3B7N5;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 157.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2834720; DOI=10.1073/pnas.85.9.2919;
RA Bolander M.E., Young M.F., Fisher L.W., Yamada Y., Termine J.D.;
RT "Osteonectin cDNA sequence reveals potential binding regions for calcium
RT and hydroxyapatite and shows homologies with both a basement membrane
RT protein (SPARC) and a serine proteinase inhibitor (ovomucoid).";
RL Proc. Natl. Acad. Sci. U.S.A. 85:2919-2923(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
RX PubMed=2835093; DOI=10.1021/bi00405a013;
RA Findlay D.M., Fisher L.W., McQuillan C.I., Termine J.D., Young M.F.;
RT "Isolation of the osteonectin gene: evidence that a variable region of the
RT osteonectin molecule is encoded within one exon.";
RL Biochemistry 27:1483-1489(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 18-36.
RX PubMed=3012473; DOI=10.1093/nar/14.11.4483;
RA Young M.F., Bolander M.E., Day A.A., Ramis C.I., Robey P.G., Yamada Y.,
RA Termine J.D.;
RT "Osteonectin mRNA: distribution in normal and transformed cells.";
RL Nucleic Acids Res. 14:4483-4497(1986).
RN [6]
RP PROTEIN SEQUENCE OF 18-55, 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).
RN [7]
RP PROTEIN SEQUENCE OF 19-36, CALCIUM-BINDING, SUBCELLULAR LOCATION, AND
RP CHARACTERIZATION.
RX PubMed=2982834; DOI=10.1016/s0021-9258(18)89422-4;
RA Romberg R.W., Werness P.G., Lollar P., Riggs B.L., Mann K.G.;
RT "Isolation and characterization of native adult osteonectin.";
RL J. Biol. Chem. 260:2728-2736(1985).
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:2982834}. Note=In or
CC around the basement membrane. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Expressed at high levels in tissues undergoing
CC morphogenesis, remodeling and wound repair.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; J03233; AAA30678.1; -; mRNA.
DR EMBL; BT030548; ABQ12988.1; -; mRNA.
DR EMBL; BC107529; AAI07530.1; -; mRNA.
DR EMBL; M18876; AAA51416.1; -; Genomic_DNA.
DR EMBL; M18874; AAA51416.1; JOINED; Genomic_DNA.
DR EMBL; M18875; AAA51416.1; JOINED; Genomic_DNA.
DR EMBL; M31318; AAA30677.1; -; mRNA.
DR PIR; A31333; GEBON.
DR RefSeq; NP_776889.1; NM_174464.2.
DR AlphaFoldDB; P13213; -.
DR SMR; P13213; -.
DR STRING; 9913.ENSBTAP00000019758; -.
DR PaxDb; P13213; -.
DR PeptideAtlas; P13213; -.
DR PRIDE; P13213; -.
DR Ensembl; ENSBTAT00000019758; ENSBTAP00000019758; ENSBTAG00000014835.
DR GeneID; 282077; -.
DR KEGG; bta:282077; -.
DR CTD; 6678; -.
DR VEuPathDB; HostDB:ENSBTAG00000014835; -.
DR VGNC; VGNC:35171; SPARC.
DR eggNOG; KOG4004; Eukaryota.
DR GeneTree; ENSGT00510000046787; -.
DR HOGENOM; CLU_047416_0_0_1; -.
DR InParanoid; P13213; -.
DR OrthoDB; 1528521at2759; -.
DR TreeFam; TF319356; -.
DR Proteomes; UP000009136; Chromosome 7.
DR Bgee; ENSBTAG00000014835; Expressed in uterine cervix and 102 other tissues.
DR ExpressionAtlas; P13213; baseline and differential.
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:3421938"
FT CHAIN 18..303
FT /note="SPARC"
FT /id="PRO_0000020303"
FT DOMAIN 71..93
FT /note="Follistatin-like"
FT DOMAIN 89..151
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 261..296
FT /note="EF-hand"
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 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT BINDING 285
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10142"
FT CARBOHYD 116
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305"
FT DISULFID 72..83
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 77..93
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 95..130
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 101..123
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 112..149
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 155..265
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 273..289
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT CONFLICT 209
FT /note="G -> GC (in Ref. 1; AAA30678)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 303 AA; 34613 MW; BD54FA0F727054D5 CRC64;
MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVAE VPVGANPVQV EVGEFDDGAE
ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS CPAPIGEFEK VCSNDNKTFD
SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE
RDEDNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ
HPIDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKEKDIDKD
LVI
