FSLE_DICDI
ID FSLE_DICDI Reviewed; 609 AA.
AC Q54J78;
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 E;
DE Flags: Precursor;
GN Name=fslE; ORFNames=DDB_G0288269;
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; EAL63316.1; -; Genomic_DNA.
DR RefSeq; XP_636809.1; XM_631717.1.
DR AlphaFoldDB; Q54J78; -.
DR PaxDb; Q54J78; -.
DR EnsemblProtists; EAL63316; EAL63316; DDB_G0288269.
DR GeneID; 8626526; -.
DR KEGG; ddi:DDB_G0288269; -.
DR dictyBase; DDB_G0288269; fslE.
DR eggNOG; ENOG502T166; Eukaryota.
DR HOGENOM; CLU_030318_0_0_1; -.
DR InParanoid; Q54J78; -.
DR PhylomeDB; Q54J78; -.
DR PRO; PR:Q54J78; -.
DR Proteomes; UP000002195; Chromosome 5.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..609
FT /note="Frizzled and smoothened-like protein E"
FT /id="PRO_0000371367"
FT TOPO_DOM 21..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..288
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 289..309
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..337
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 338..358
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 359..365
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 366..386
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 387..408
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..429
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 430..457
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 458..478
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 479..511
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 533..609
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 35..192
FT /note="FZ"
FT REGION 559..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 559..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 172
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 198
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 217
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 40..118
FT /evidence="ECO:0000250"
FT DISULFID 53..111
FT /evidence="ECO:0000250"
FT DISULFID 100..149
FT /evidence="ECO:0000250"
FT DISULFID 138..189
FT /evidence="ECO:0000250"
SQ SEQUENCE 609 AA; 69006 MW; 99C5FAE320F25F1C CRC64;
MEMIRIFLIY LILKIIIING ENNEYSKGYG VGIVFPGSKC LNYVGDSIGQ PLCNNRLFNG
GKKIYSTVTL VDNKNISSQE LSKIEILKSF EALTFLQDQC DDLLFTQFGL CDLNFSPCVE
TIPKITPLQN VSLPQRLCKS VCERMVSNCP RLSLKIDCSI SFLFPEIGTE YNLTLYGYTE
NKGLYKVPCI DPTDGYNNIS NQMELIQACP YPLLLKNSSD PKYSPNKGYT YLPPTNCVLT
CPMPNYTKTQ WKRVYDMAKT LSSISFICAC YNILTFGILN RKRKSKYNIC ITLMSTSIAL
VYLTDIIKFG YGIEEFLCPE PGRSAVQNDA ACGITGAMFH FGITYCCCWA MTMSIVLFCS
VKRIKLFYFR HFMIGNTIFT IITTVILLSA KKMVAGTGYI ECWVRERWFV ITLFWLPCGI
GLSIGIFCIG GVIHEIYNIS KKVNIRESEF ILRQIKPFSL VFSVAGSFLY LFIFFFDVER
KIDSYKAAVA DYVLCLLSGG SEETCFTTGP NYASFFIFYF FIRVFGVLFF SIYGTSRVAR
DIWSEVVFDE VRSRLSQSES GISRNNSRTD ISFGKNNNSK NSNNSKNSNN SKNSNNSDND
SKSIELEKK
