位置:首页 > 蛋白库 > SPRC_PONAB
SPRC_PONAB
ID   SPRC_PONAB              Reviewed;         303 AA.
AC   Q5R767; Q5R433;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=SPARC;
DE   AltName: Full=Osteonectin;
DE            Short=ON;
DE   AltName: Full=Secreted protein acidic and rich in cysteine;
DE   Flags: Precursor;
GN   Name=SPARC;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex, and Heart;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the SPARC family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR860251; CAH92393.1; -; mRNA.
DR   EMBL; CR861427; CAH93483.1; -; mRNA.
DR   RefSeq; NP_001127042.1; NM_001133570.1.
DR   RefSeq; NP_001128859.1; NM_001135387.1.
DR   AlphaFoldDB; Q5R767; -.
DR   SMR; Q5R767; -.
DR   PRIDE; Q5R767; -.
DR   Ensembl; ENSPPYT00000057620; ENSPPYP00000032437; ENSPPYG00000030691.
DR   GeneID; 100174069; -.
DR   GeneID; 100189783; -.
DR   KEGG; pon:100174069; -.
DR   CTD; 6678; -.
DR   GeneTree; ENSGT00510000046787; -.
DR   InParanoid; Q5R767; -.
DR   OrthoDB; 1528521at2759; -.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0016363; C:nuclear matrix; IEA:Ensembl.
DR   GO; GO:0031092; C:platelet alpha granule membrane; IEA:Ensembl.
DR   GO; GO:0005509; F:calcium ion binding; IEA:Ensembl.
DR   GO; GO:0005518; F:collagen binding; IEA:Ensembl.
DR   GO; GO:0016525; P:negative regulation of angiogenesis; IEA:Ensembl.
DR   GO; GO:0001937; P:negative regulation of endothelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0010595; P:positive regulation of endothelial cell migration; IEA:Ensembl.
DR   GO; GO:0022604; P:regulation of cell morphogenesis; IEA:Ensembl.
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   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..303
FT                   /note="SPARC"
FT                   /id="PRO_0000293538"
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        94
FT                   /note="V -> M (in Ref. 1; CAH93483)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  34632 MW;  B914599F79705945 CRC64;
     MRAWIFFLLC LAGRALAAPQ QEALPDETEV VEETVAEVTE VSVGANPVQV EVGEFDDGAE
     ETEEEVVAEN PCQNHHCKHG KVCELDENNT PMCVCQDPTS CPAPIGEFEK VCSNDNKTFD
     SSCHFFATKC TLEGTKKGHK LHLDYIGPCK YIPPCLDSEL TEFPLRMRDW LKNVLVTLYE
     RDEDNNLLTE KQKLRVKKIH ENEKRLEAGD HPVELLARDF EKNYNMYIFP VHWQFGQLDQ
     HPIDGYLSHT ELAPLRAPLI PMEHCTTRFF ETCDLDNDKY IALDEWAGCF GIKQKDIDKD
     LVI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024