ID C3XX68_BRAFL Unreviewed; 270 AA.
AC C3XX68;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 83.
DE RecName: Full=FZ domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_278100 {ECO:0000313|EMBL:EEN67328.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN67328.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN67328.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN67328.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
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; GG666471; EEN67328.1; -; Genomic_DNA.
DR RefSeq; XP_002611318.1; XM_002611272.1.
DR AlphaFoldDB; C3XX68; -.
DR STRING; 7739.C3XX68; -.
DR MEROPS; I93.002; -.
DR eggNOG; KOG3577; Eukaryota.
DR InParanoid; C3XX68; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0017147; F:Wnt-protein binding; IBA:GO_Central.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0035567; P:non-canonical Wnt signaling pathway; IBA:GO_Central.
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; IPR008993; TIMP-like_OB-fold.
DR PANTHER; PTHR11309; FRIZZLED; 1.
DR PANTHER; PTHR11309:SF148; SECRETED FRIZZLED-RELATED PROTEIN 1; 1.
DR Pfam; PF01392; Fz; 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}; Wnt signaling pathway {ECO:0000256|ARBA:ARBA00022687}.
FT DOMAIN 5..122
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 143..270
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
FT DISULFID 20..66
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 85..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 270 AA; 30664 MW; 5E58B22F6DB3AFDF CRC64;
MYVSDQPRKC VQIPQSLVLC DGLAYNEMRL PNLLGHENLD EVQEQARSWV PLLAQRCHPD
TKLFLCSLFT PVCLEQDIFP CRSLCEGVRD SCAPVMAQHG FPWPKMLKCD KYPPDNDMCI
KSQTTPGPYD PRRPKPAQHP GSCIVCLEEG DDRSSDFCSS DVVLRVRVEE KHFDDGDLVF
TTKKKVRVFH ASEALGGGRR RLNLPVQDME FRVIGGEKCA CSALARRKPG QLLLSARRDG
SKFFVTSVRK WQKGDKAFKR LLRSMRDMTC
//