SPRC_CHICK
ID SPRC_CHICK Reviewed; 298 AA.
AC P36377;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 125.
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 Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=White leghorn; TISSUE=Embryo;
RX PubMed=7916692; DOI=10.1111/j.1432-1033.1993.tb18358.x;
RA Bassuk J.A., Iruela-Arispe M.L., Lane T.L., Benson J.M., Berg R.A.,
RA Sage E.H.;
RT "Molecular analysis of chicken embryo SPARC (osteonectin).";
RL Eur. J. Biochem. 218:117-127(1993).
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:0000250}. Note=In or around the basement
CC membrane. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Detected in aorta, skeletal muscle, calvarium,
CC vertebra, anterior limb, kidney, heart, brain, skin and lung.
CC {ECO:0000269|PubMed:7916692}.
CC -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
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DR EMBL; L24906; AAA16893.1; -; mRNA.
DR PIR; S39539; S39539.
DR RefSeq; NP_989741.1; NM_204410.1.
DR AlphaFoldDB; P36377; -.
DR SMR; P36377; -.
DR STRING; 9031.ENSGALP00000006639; -.
DR PaxDb; P36377; -.
DR GeneID; 386571; -.
DR KEGG; gga:386571; -.
DR CTD; 6678; -.
DR VEuPathDB; HostDB:geneid_386571; -.
DR eggNOG; KOG4004; Eukaryota.
DR InParanoid; P36377; -.
DR OrthoDB; 1528521at2759; -.
DR PhylomeDB; P36377; -.
DR PRO; PR:P36377; -.
DR Proteomes; UP000000539; 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; 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; PS51465; KAZAL_2; 1.
DR PROSITE; PS00612; OSTEONECTIN_1; 1.
DR PROSITE; PS00613; OSTEONECTIN_2; 1.
PE 2: Evidence at transcript 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..298
FT /note="SPARC"
FT /id="PRO_0000020308"
FT DOMAIN 66..88
FT /note="Follistatin-like"
FT DOMAIN 84..146
FT /note="Kazal-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DOMAIN 256..291
FT /note="EF-hand"
FT BINDING 269
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 275
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT BINDING 280
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 67..78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 72..88
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 90..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 96..118
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 107..144
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 150..260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
FT DISULFID 268..284
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00798"
SQ SEQUENCE 298 AA; 34061 MW; 4D5F9145E8FBD149 CRC64;
MRTWIFFFLC LAGKALAAPQ EALADETEVI EDLTTEGPVG ANPVQVEVGE FEEPTEDVEE
IVAENPCQNH HCKHGKVCEV DDNNSPMCVC QDPSSCPAHS GVFEKVCGTD NKTYDSSCHF
FATKCTLEGT KKGHKLHLDY IGPCKFIPAC LDTELTEFPL RMRDWLKNVL ITLYERDEDN
NLLTEKQKLK VKNIHENEKR LEAGDHTVEL LARDFEKNYN MYIFPVHWQF GQLDQHPIDG
YLSHTELAPL RAPLIPMEHC TTRFFEACDL DFDKYIALEE WASCFGIKEQ DIDKDLVI
