ID I3MJM5_ICTTR Unreviewed; 347 AA.
AC I3MJM5;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Secreted frizzled related protein 4 {ECO:0000313|Ensembl:ENSSTOP00000011371.3};
GN Name=SFRP4 {ECO:0000313|Ensembl:ENSSTOP00000011371.3};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000011371.3, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000011371.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the secreted frizzled-related protein (sFRP)
CC family. {ECO:0000256|ARBA:ARBA00010054}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00090}.
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DR EMBL; AGTP01012519; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3MJM5; -.
DR STRING; 43179.ENSSTOP00000011371; -.
DR Ensembl; ENSSTOT00000012691.3; ENSSTOP00000011371.3; ENSSTOG00000012692.3.
DR eggNOG; KOG3577; Eukaryota.
DR GeneTree; ENSGT00940000160766; -.
DR HOGENOM; CLU_058446_0_0_1; -.
DR InParanoid; I3MJM5; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0017147; F:Wnt-protein binding; IEA:Ensembl.
DR GO; GO:0060349; P:bone morphogenesis; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2000119; P:negative regulation of sodium-dependent phosphate transport; IEA:Ensembl.
DR GO; GO:0055062; P:phosphate ion homeostasis; IEA:Ensembl.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:1902174; P:positive regulation of keratinocyte apoptotic process; IEA:Ensembl.
DR GO; GO:0002092; P:positive regulation of receptor internalization; IEA:Ensembl.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 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; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF7; SECRETED FRIZZLED-RELATED PROTEIN 4; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF01759; NTR; 1.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00063; FRI; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50189; NTR; 1.
PE 3: Inferred from homology;
KW Developmental protein {ECO:0000256|ARBA:ARBA00022473};
KW Differentiation {ECO:0000256|ARBA:ARBA00022782};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00090}; Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP};
KW Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..347
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013334175"
FT DOMAIN 19..139
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 178..307
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT REGION 293..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 24..85
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 32..78
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 101..125
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 347 AA; 39798 MW; 13BB574ADD5ED798 CRC64;
MLLSILVALC LWLRLALGVR GAPCEAVRIP MCRHMPWNIT RMPNHLHHST QENAILAIEQ
YEELVDVNCS AVLRFFLCAM YAPICTLEFL HDPIKPCKSV CQRARDDCEP LMKMYNHSWP
ESLACDELPV YDRGVCISPE AIVTDLPDDV KWIDITPDMM VQERPLDVDC KRLSPDRCKC
KKVKPTLATY LSKNYSYVIH AKIKAVQRSG CNEVTTVVDV KEIFKSLSPI PRTQVPLITN
SSCQCPHILP HQDVLIMCYE WRSRMMLLEN CLVEKWRDQL SKRSIQWEER LQEQQRTLQD
KKRTAGRTSR SNPPKPKGKP PAPKPASPKK NIKARSAQKK TNPKSVS
//
