FSLA_DICDI
ID FSLA_DICDI Reviewed; 594 AA.
AC Q54P68;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Frizzled and smoothened-like protein A;
DE Flags: Precursor;
GN Name=fslA; ORFNames=DDB_G0284761;
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; AAFI02000071; EAL65033.1; -; Genomic_DNA.
DR RefSeq; XP_638390.1; XM_633298.1.
DR AlphaFoldDB; Q54P68; -.
DR PaxDb; Q54P68; -.
DR EnsemblProtists; EAL65033; EAL65033; DDB_G0284761.
DR GeneID; 8624759; -.
DR KEGG; ddi:DDB_G0284761; -.
DR dictyBase; DDB_G0284761; fslA.
DR eggNOG; ENOG502RCJA; Eukaryota.
DR HOGENOM; CLU_030318_0_0_1; -.
DR InParanoid; Q54P68; -.
DR OMA; CEGIGYN; -.
DR PhylomeDB; Q54P68; -.
DR PRO; PR:Q54P68; -.
DR Proteomes; UP000002195; Chromosome 4.
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 PROSITE; PS50038; FZ; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Membrane; Receptor; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..594
FT /note="Frizzled and smoothened-like protein A"
FT /id="PRO_0000371363"
FT TOPO_DOM 23..248
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 249..269
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 270..277
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 278..298
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 299..329
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 330..350
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..448
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..507
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 508..528
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 529..594
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 27..173
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT CARBOHYD 55
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 189
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 195
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 479
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 32..98
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 41..91
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 117..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 594 AA; 66964 MW; 5431D96E84937244 CRC64;
MVDIRKSLFF IIFFIFYNYV NSQKAINSDA FCQKKTITSI CDPYLFNTDS IYIFNSTTTQ
ESIELEIKRL LGFFSMLPST CQVPSTYRLI CNQYFQTCVP ISKTDNSSTI AIPLRPCRES
CDYGNGICGT QSITPCTGTF TEPTIYKFPV TSNVFDLSSL GGPSNYDLQC LNIDTMKAGN
LNGTYISNNE TVIVNQTCVY PLVYRNSTNR EDDIKKGYQY LTETSDCLLP CPVPFFTENE
WYQFKDLTTV TGVISFVCIF FNIFIYGFLN KKHDRHTIGI LCLSFSLWCC MLSDLIVASS
PDYSLVCPEP GRFARIHDSR CVANGIIFQW GAVCTTMFWS AMAIDLYLVI KKLSLPAFTV
KYFVAAIFTL ALLFTTVPLA WDDYGYGFGG VGCWIMSNSV QNGCFWIPML ICLLIGAVSI
CLIIYEIVKV FKNVGRSGIS IILANARLFG IVSFIFIEYI YLFVYHFWVQ ENTEKFTQNI
TDWVICVQTT GSSDGCPLPK AVPYATQFIF LFFLRLLGIE VCIFYGINSR SKNIILESDL
VNNKYFKAIR SKISSVGATS TTKNNTSTNN TSDQFNTSMF SVEVSKNGGD DDDL