ID   FSLO_DICDI              Reviewed;         695 AA.
AC   Q1ZXI9;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Frizzled and smoothened-like protein O;
DE   Flags: Precursor;
GN   Name=fslO; ORFNames=DDB_G0278289;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
RN   [2]
RP   NOMENCLATURE.
RX   PubMed=16735079; DOI=10.1016/j.ejcb.2006.04.003;
RA   Prabhu Y., Eichinger L.;
RT   "The Dictyostelium repertoire of seven transmembrane domain receptors.";
RL   Eur. J. Cell Biol. 85:937-946(2006).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC       {ECO:0000305}.
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DR   EMBL; AAFI02000023; EAS66898.1; -; Genomic_DNA.
DR   RefSeq; XP_001134582.1; XM_001134582.1.
DR   AlphaFoldDB; Q1ZXI9; -.
DR   PaxDb; Q1ZXI9; -.
DR   EnsemblProtists; EAS66898; EAS66898; DDB_G0278289.
DR   GeneID; 8621475; -.
DR   KEGG; ddi:DDB_G0278289; -.
DR   dictyBase; DDB_G0278289; fslO.
DR   eggNOG; ENOG502RBR8; Eukaryota.
DR   HOGENOM; CLU_447205_0_0_1; -.
DR   InParanoid; Q1ZXI9; -.
DR   OMA; MARPDPC; -.
DR   PhylomeDB; Q1ZXI9; -.
DR   PRO; PR:Q1ZXI9; -.
DR   Proteomes; UP000002195; Chromosome 3.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.2000.10; -; 1.
DR   InterPro; IPR020067; Frizzled_dom.
DR   InterPro; IPR036790; Frizzled_dom_sf.
DR   SUPFAM; SSF63501; SSF63501; 1.
DR   PROSITE; PS50038; FZ; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Disulfide bond; Glycoprotein; Membrane; Receptor;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..695
FT                   /note="Frizzled and smoothened-like protein O"
FT                   /id="PRO_0000371376"
FT   TOPO_DOM        24..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..262
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        263..283
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        284..307
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        329..343
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        344..364
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        365..387
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        388..408
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        409..435
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        436..456
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        457..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..695
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          28..173
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          545..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          653..691
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        545..573
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..695
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        137
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        178
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..96
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        42..89
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        80..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        114..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        118..138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   695 AA;  77709 MW;  A603D1A96B69EC69 CRC64;
     MKKLNYLLIV SFIFILNLLI SKSQVLIDVT AKCELIDSLS PCKDNLNYTH IYLPTGYTQA
     AISAQITPLF QQASILPTDC QSNLKNLLCI SSYMECNENI PNISPSFPLP SYPCNKYCEK
     VKDVCSAYMA ILGPYVNCSA VQNGNEFFPH TGTDYDLTAY GGSANEEIQC SGPNLASNST
     SAPIKFCPSP LIWVDSDTIN NKRAYQETTP NCVLPCPTNV YTEKEYKTKF YSEAILFSFS
     TACSFYLIFT FGVFPNKYTN RNWIIVYLGI TAICLAISYA VQEARYGGGD WRCTSDPGRY
     KSSEDGTCIL GGFFFQIGGL GTILFLSLYS FDMFLTMNMM TNKYFIQTSV GMWALIIFYA
     LLPIKHYESS IASAGCWLSN EDNMFWQYFC FYVPSYVATF FLGVFIITSI YKVFKMTVMF
     KSIKDKRILL LNIRSIIFLI AIMFCVSFST MYPLYVTYNG DDFSKSVEVY VTCLYANIPN
     GNEVCPQIVF PQFSLRYMNA ITMAIIGIVG LIGLGIDPHI LQIYRESIRF KFLLGLVGIQ
     WGTNSPQPLK QGSTTDSSSG SGSGNGSNSG NNRENRKSQR KSRGVSIGMK KINLSASSES
     SNNLLNQSTP GNLNINESIS SIDTSNNNNN NNNNNNNNNN NNNNNNNNNN NNNNNNNNNN
     NNNNNNNNNN NNYSNNNNNN NNNNNNIERI NSDNV