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SFRP3_BOVIN
ID   SFRP3_BOVIN             Reviewed;         325 AA.
AC   Q95117; Q2KHY0;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 147.
DE   RecName: Full=Secreted frizzled-related protein 3;
DE            Short=sFRP-3;
DE   AltName: Full=Frizzled-related protein 1;
DE   AltName: Full=FrzB-1;
DE   Flags: Precursor;
GN   Name=FRZB; Synonyms=FRZB1, SFRP3;
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].
RC   TISSUE=Cartilage;
RX   PubMed=8824257; DOI=10.1074/jbc.271.42.26131;
RA   Hoang B., Moos M. Jr., Vukicevic S., Luyten F.P.;
RT   "Primary structure and tissue distribution of FRZB, a novel protein related
RT   to Drosophila frizzled, suggest a role in skeletal morphogenesis.";
RL   J. Biol. Chem. 271:26131-26137(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Kidney;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   INTERACTION OF THE FZ DOMAIN WITH WNT PROTEINS.
RX   PubMed=9326585; DOI=10.1073/pnas.94.21.11196;
RA   Lin K., Wang S., Julius M.A., Kitajewski J., Moos M. Jr., Luyten F.P.;
RT   "The cysteine-rich frizzled domain of Frzb-1 is required and sufficient for
RT   modulation of Wnt signaling.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:11196-11200(1997).
CC   -!- FUNCTION: Soluble frizzled-related proteins (sFRPS) function as
CC       modulators of Wnt signaling through direct interaction with Wnts. They
CC       have a role in regulating cell growth and differentiation in specific
CC       cell types. SFRP3/FRZB appears to be involved in limb skeletogenesis.
CC       Antagonist of Wnt8 signaling. Regulates chondrocyte maturation and long
CC       bone development.
CC   -!- SUBUNIT: Interacts with MYOC. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- DOMAIN: The FZ domain is involved in binding with Wnt ligands.
CC   -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC       family. {ECO:0000305}.
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DR   EMBL; U24164; AAC48662.1; -; mRNA.
DR   EMBL; BC112842; AAI12843.1; -; mRNA.
DR   RefSeq; NP_776484.1; NM_174059.2.
DR   RefSeq; XP_005202312.1; XM_005202255.3.
DR   RefSeq; XP_005202313.1; XM_005202256.3.
DR   RefSeq; XP_015330109.1; XM_015474623.1.
DR   AlphaFoldDB; Q95117; -.
DR   SMR; Q95117; -.
DR   STRING; 9913.ENSBTAP00000014572; -.
DR   PaxDb; Q95117; -.
DR   PRIDE; Q95117; -.
DR   Ensembl; ENSBTAT00000014572; ENSBTAP00000014572; ENSBTAG00000010977.
DR   GeneID; 281170; -.
DR   KEGG; bta:281170; -.
DR   CTD; 2487; -.
DR   VEuPathDB; HostDB:ENSBTAG00000010977; -.
DR   VGNC; VGNC:29124; FRZB.
DR   eggNOG; KOG3577; Eukaryota.
DR   GeneTree; ENSGT00940000160494; -.
DR   HOGENOM; CLU_058446_1_0_1; -.
DR   InParanoid; Q95117; -.
DR   OMA; CNELPLY; -.
DR   OrthoDB; 1339129at2759; -.
DR   Proteomes; UP000009136; Chromosome 2.
DR   Bgee; ENSBTAG00000010977; Expressed in retina and 100 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0017147; F:Wnt-protein binding; ISS:AgBase.
DR   GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR   GO; GO:0060029; P:convergent extension involved in organogenesis; IEA:Ensembl.
DR   GO; GO:0002064; P:epithelial cell development; IEA:Ensembl.
DR   GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IBA:GO_Central.
DR   GO; GO:0061037; P:negative regulation of cartilage development; IEA:Ensembl.
DR   GO; GO:0010721; P:negative regulation of cell development; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR   GO; GO:0070367; P:negative regulation of hepatocyte differentiation; IEA:Ensembl.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; ISS:AgBase.
DR   GO; GO:0014033; P:neural crest cell differentiation; IEA:Ensembl.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
DR   GO; GO:0045600; P:positive regulation of fat cell differentiation; IEA:Ensembl.
DR   GO; GO:0061053; P:somite development; IEA:Ensembl.
DR   CDD; cd07441; CRD_SFRP3; 1.
DR   CDD; cd03581; NTR_Sfrp3_like; 1.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   Gene3D; 2.40.50.120; -; 1.
DR   InterPro; IPR015526; Frizzled/SFRP.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   InterPro; IPR001134; Netrin_domain.
DR   InterPro; IPR018933; Netrin_module_non-TIMP.
DR   InterPro; IPR035813; NTR_Sfrp3.
DR   InterPro; IPR026556; SFRP3.
DR   InterPro; IPR041759; SFRP3_CRD.
DR   InterPro; IPR008993; TIMP-like_OB-fold.
DR   PANTHER; PTHR11309; PTHR11309; 1.
DR   PANTHER; PTHR11309:SF97; PTHR11309:SF97; 1.
DR   Pfam; PF01392; Fz; 1.
DR   Pfam; PF01759; NTR; 1.
DR   SMART; SM00643; C345C; 1.
DR   SMART; SM00063; FRI; 1.
DR   SUPFAM; SSF50242; SSF50242; 1.
DR   SUPFAM; SSF63501; SSF63501; 1.
DR   PROSITE; PS50038; FZ; 1.
DR   PROSITE; PS50189; NTR; 1.
PE   1: Evidence at protein level;
KW   Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW   Reference proteome; Secreted; Signal; Wnt signaling pathway.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..325
FT                   /note="Secreted frizzled-related protein 3"
FT                   /id="PRO_0000032545"
FT   DOMAIN          33..150
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DOMAIN          178..298
FT                   /note="NTR"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00295"
FT   REGION          299..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        299
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..96
FT                   /evidence="ECO:0000250"
FT   DISULFID        43..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        80..119
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..147
FT                   /evidence="ECO:0000250"
FT   DISULFID        112..136
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   325 AA;  36234 MW;  39E337A9C6E98BB3 CRC64;
     MVCGSRGGML LLPAGLLALA ALCLLRVPGA RAAACEPVRI PLCKSLPWNM TKMPNHLHHS
     TQANAILAIE QFEGLLGTHC SPDLLFFLCA MYAPICTIDF QHEPIKPCKS VCERARQGCE
     PILIKYRHSW PESLACEELP VYDRGVCISP EAIVTADGAD FPMDSSNGNC RGASSERCKC
     KPVRATQKTY FRNNYNYVIR AKVKEIKTKC HDVTAVVEVK EILKASLVNI PRETVNLYTS
     SGCLCPPLNV NEEYLIMGYE DEERSRLLLV EGSIAEKWKD RLGKKVKRWD MKLRHLGLNT
     SDSSHSDSTQ SQKPGRNSNS RQARN
 
 
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