ID Q7ZXF8_XENLA Unreviewed; 300 AA.
AC Q7ZXF8;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 120.
DE RecName: Full=SPARC {ECO:0000256|ARBA:ARBA00019049};
DE AltName: Full=Osteonectin {ECO:0000256|ARBA:ARBA00032081};
DE AltName: Full=Secreted protein acidic and rich in cysteine {ECO:0000256|ARBA:ARBA00031976};
GN Name=sparc.S {ECO:0000313|RefSeq:NP_001079590.1,
GN ECO:0000313|Xenbase:XB-GENE-1009638};
GN Synonyms=MGC53121 {ECO:0000313|EMBL:AAH45013.1}, sparc
GN {ECO:0000313|RefSeq:NP_001079590.1,
GN ECO:0000313|Xenbase:XB-GENE-1009638};
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 {ECO:0000313|EMBL:AAH45013.1};
RN [1] {ECO:0000313|RefSeq:NP_001079590.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=12454917; DOI=10.1002/dvdy.10174;
RA Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA Richardson P.;
RT "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT initiative.";
RL Dev. Dyn. 225:384-391(2002).
RN [2] {ECO:0000313|EMBL:AAH45013.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000313|EMBL:AAH45013.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|RefSeq:NP_001079590.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=21384171;
RA Huynh M.H., Zhu S.J., Kollara A., Brown T., Winklbauer R., Ringuette M.;
RT "Knockdown of SPARC leads to decreased cell-cell adhesion and lens
RT cataracts during post-gastrula development in Xenopus laevis.";
RL Dev. Genes Evol. 220:315-327(2011).
RN [4] {ECO:0000313|RefSeq:NP_001079590.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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. {ECO:0000256|ARBA:ARBA00025574}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}.
CC Secreted, extracellular space, extracellular matrix, basement membrane
CC {ECO:0000256|ARBA:ARBA00004302}.
CC -!- SIMILARITY: Belongs to the SPARC family.
CC {ECO:0000256|ARBA:ARBA00006404}.
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DR EMBL; BC045013; AAH45013.1; -; mRNA.
DR EMBL; BC106298; AAI06299.1; -; mRNA.
DR RefSeq; NP_001079590.1; NM_001086121.1.
DR STRING; 8355.Q7ZXF8; -.
DR PaxDb; 8355-Q7ZXF8; -.
DR DNASU; 379277; -.
DR GeneID; 379277; -.
DR KEGG; xla:379277; -.
DR AGR; Xenbase:XB-GENE-1009638; -.
DR CTD; 379277; -.
DR Xenbase; XB-GENE-1009638; sparc.S.
DR OMA; IWKFCEL; -.
DR OrthoDB; 4695638at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 379277; Expressed in internal ear and 19 other cell types or tissues.
DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd16235; EFh_SPARC_SPARC; 1.
DR CDD; cd01328; FSL_SPARC; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 1.10.238.10; EF-hand; 1.
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 InterPro; IPR037641; SPARC_FS.
DR PANTHER; PTHR13866:SF14; BM-40; 1.
DR PANTHER; PTHR13866; SPARC OSTEONECTIN; 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; SSF47473; EF-hand; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 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 2: Evidence at transcript level;
KW Basement membrane {ECO:0000256|ARBA:ARBA00022869};
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR637641-50};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000186698};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..300
FT /note="SPARC"
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001079590.1"
FT /id="PRO_5033206464"
FT DOMAIN 91..148
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DISULFID 69..80
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 74..90
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 92..127
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 98..120
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 109..146
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 152..262
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
FT DISULFID 270..286
FT /evidence="ECO:0000256|PIRSR:PIRSR637641-50"
SQ SEQUENCE 300 AA; 34540 MW; 8EAB4958834C166F CRC64;
MRVWVFFVLC LAGKALAAPQ QDALPEEEEV IEDVPTEETV GVNPVQVEVG EFDDAINEEE
EEEPSENPCL NHHCKHGKVC EVDESNTPMC VCQDPSTCPA TVGEFEKVCG TDNKTYESSC
HFFATKCTLE GTKKGHKLHL DYIGPCKYIA PCLDNELSEF PMRMRDWLKN VLVSLYERDE
NNNLLNEKQK LRVKKIHENE KRLEAGDHSM ELLARDFEKN YNMYIFPVHW QFGQLDQHPI
DGYLSHTELS PLRAPLIPME HCTTRFFDEC DTDNDKYIAL EEWGNCFGIK EQDVDKDMIV
//
