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Database: UniProt
Entry: A0A091E923_FUKDA
LinkDB: A0A091E923_FUKDA
Original site: A0A091E923_FUKDA 
ID   A0A091E923_FUKDA        Unreviewed;       238 AA.
AC   A0A091E923;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Secreted frizzled-related protein 2 {ECO:0000313|EMBL:KFO31681.1};
GN   ORFNames=H920_06880 {ECO:0000313|EMBL:KFO31681.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO31681.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO31681.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO31681.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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; KN122248; KFO31681.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091E923; -.
DR   SMR; A0A091E923; -.
DR   STRING; 885580.ENSFDAP00000018863; -.
DR   MEROPS; I93.002; -.
DR   eggNOG; KOG3577; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0030178; P:negative regulation of Wnt signaling pathway; IEA:UniProt.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR   CDD; cd03580; NTR_Sfrp1_like; 1.
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:SF149; SECRETED FRIZZLED-RELATED PROTEIN 1; 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:UP000028990};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT   DOMAIN          1..98
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          115..238
FT                   /note="NTR"
FT                   /evidence="ECO:0000259|PROSITE:PS50189"
FT   DISULFID        30..68
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        61..85
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   238 AA;  27239 MW;  D925BA5E6BABE534 CRC64;
     MRLPNLLGHE TMKEVLEQAG AWIPLVMKQC HPDTKKFLCS LFAPVCLDDL DETIQPCHSL
     CVQVKDRCAP VMSAFGFPWP DMLECDRFPQ DNDLCIPLAS SDHLLPATEE APKVCEACKN
     KNDDDNDIME TLCKNDFALK IKVKEITYIN RDTKIILETK SKTIYKLNGV SERDLKKSVL
     WLKDSLQCTC EEMNDINAPY LVMGQKQGGE LVITSVKRWQ KGQREFKRIS RSIRKLQC
//
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