ID   FSLG_DICDI              Reviewed;         574 AA.
AC   Q54J71;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Frizzled and smoothened-like protein G;
DE   Flags: Precursor;
GN   Name=fslG; ORFNames=DDB_G0288261;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AAFI02000109; EAL63312.1; -; Genomic_DNA.
DR   RefSeq; XP_636816.1; XM_631724.1.
DR   AlphaFoldDB; Q54J71; -.
DR   PaxDb; Q54J71; -.
DR   EnsemblProtists; EAL63312; EAL63312; DDB_G0288261.
DR   GeneID; 8626533; -.
DR   KEGG; ddi:DDB_G0288261; -.
DR   dictyBase; DDB_G0288261; fslG.
DR   eggNOG; ENOG502T166; Eukaryota.
DR   HOGENOM; CLU_030318_0_0_1; -.
DR   InParanoid; Q54J71; -.
DR   PhylomeDB; Q54J71; -.
DR   PRO; PR:Q54J71; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR   InterPro; IPR000539; Frizzled/Smoothened_TM.
DR   InterPro; IPR017981; GPCR_2-like.
DR   Pfam; PF01534; Frizzled; 1.
DR   PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..574
FT                   /note="Frizzled and smoothened-like protein G"
FT                   /id="PRO_0000371369"
FT   TOPO_DOM        20..246
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        247..267
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        268..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..324
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        346..358
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        359..379
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        380..401
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        402..422
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..445
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        446..466
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        467..502
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        503..523
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        524..574
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          30..181
FT                   /note="FZ"
FT   REGION          550..574
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        550..567
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        161
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        187
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        244
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        486
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        35..109
FT                   /evidence="ECO:0000250"
FT   DISULFID        48..102
FT                   /evidence="ECO:0000250"
FT   DISULFID        91..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        127..178
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   574 AA;  64284 MW;  BBD54F71A1BAC16C CRC64;
     MKSIIFITFF IFFLKKLNGL PNGYGVGLVD PNGQCMNYIG DSIDQPLCKN KLSNNGEFIY
     STIGNSLNSQ TLSQQTIAKS FEALTFIQNQ CQDLLFAEYG ICNIYLSPCI ITTVAPLKNI
     SLPQRLCNSA CQRMVTNCPR LGEKIDCSIS FLFPEVGTLY NLSDYGYKAN GGLYEVPCFN
     PTADYDNSSS LNEFIEICPS PLLLKNSSDP KYSKRGYTYL PPTNCVLPCP VPNYTKEKWN
     QIENLSKVLS TISFVCSIYN ILSFGILKKK KTKYTICISA LSASVALINL GDIIKIGVGY
     EKVLCPEPGR FATQVDDPLC GLTAALFHVG ICSTVLWTTT MAIYLYSAIK NIKLFKFRYF
     IIFNTGFSLT SLIIAASASK FEAGTGSIEC WIRDRWYSIC LFWLPCGICL LIGTICIASV
     IVEIYKVSKN IKLSESETIM RQIKPIISVI LVSGSFTYLF IIFFDIERNF GGYRSAVTDY
     VLCLLNSTDN GIECHTSGPS YNPYFMFYFF MRFFGILFFL IYGTSKNARD SWYELFIKIK
     VSLSETSSTI SNNSGGGSSQ QKQQQQNEIK LEKI