FSLF_DICDI
ID FSLF_DICDI Reviewed; 591 AA.
AC Q54J77;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Frizzled and smoothened-like protein F;
DE Flags: Precursor;
GN Name=fslF; ORFNames=DDB_0231315;
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; AAFI02000109; EAL63308.1; -; Genomic_DNA.
DR RefSeq; XP_636810.1; XM_631718.1.
DR AlphaFoldDB; Q54J77; -.
DR PaxDb; Q54J77; -.
DR EnsemblProtists; EAL63308; EAL63308; DDB_G0288253.
DR GeneID; 8626527; -.
DR KEGG; ddi:DDB_G0288253; -.
DR dictyBase; DDB_G0288253; fslF.
DR eggNOG; ENOG502T166; Eukaryota.
DR HOGENOM; CLU_030318_0_0_1; -.
DR InParanoid; Q54J77; -.
DR PhylomeDB; Q54J77; -.
DR PRO; PR:Q54J77; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR Pfam; PF00002; 7tm_2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..591
FT /note="Frizzled and smoothened-like protein F"
FT /id="PRO_0000371368"
FT TOPO_DOM 18..244
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..275
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 297..321
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 322..342
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..397
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 419..442
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 443..463
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 464..495
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 496..516
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 517..591
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 30..177
FT /note="FZ"
FT REGION 538..573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 167
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 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 35..105
FT /evidence="ECO:0000250"
FT DISULFID 48..98
FT /evidence="ECO:0000250"
FT DISULFID 123..174
FT /evidence="ECO:0000250"
SQ SEQUENCE 591 AA; 66711 MW; DA4ABBAA2B2CD988 CRC64;
MKILIIFIIF IISYISGFEI PKGFGIGLVI PDAECLNYIG DPIDQQLCNS KLQNNGDRIY
TTTNSQIDSQ TNIKKSFEAI TFLQDQCKDL LFAQFGICDI YLAPCIEVTL TPLKSISLPQ
RFCKSVCDRM VSNCPRLEEQ MDCSNSFLFP EIGTFYDLSP YGYTIDNGTF AVPCSDPTIF
FNQVSSNSSF IEICPSPLLL KNSSDPEYAA NKGYSYLSPS NCVLPCPVPN YSNQKWDQLL
TMSKILSTIS FILSLYNVLT FGIINKKVSD PHKCTCFFSG SIALVNLCDI ITYGIGYEEL
LCPEPGRSAK QQLDPVCGLT GAFFHLGITY CVLWSMTMGL VLYCSVKRQK WFKFNYFLIG
NTTFTITTVV IAAATSKFEA GLGSIECWIR DRWYAISLFW IPCGIALLIG SFCIIAVIHE
VYKTSKKSIS NRNDLLQREL KPLLIVIFIS GSFLYLFIFF FDIERKFGGY RSAVEDYVLC
LLNGSQEECF TTGPSYVPYF LFYLVIRWFG IIFFLFYGTS NIARKIWVQN KIWKSISSSI
SPKSTPKSSP KNSDSKINSN STNNNNMILN DNNDKNLNEK KAVELESIKI N
