FSCA_DICDI
ID FSCA_DICDI Reviewed; 549 AA.
AC Q54H37;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Frizzled/smoothened-like sans CRD protein A;
DE Flags: Precursor;
GN Name=fscA; ORFNames=DDB_G0289725;
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; AAFI02000148; EAL62574.1; -; Genomic_DNA.
DR RefSeq; XP_636081.1; XM_630989.1.
DR AlphaFoldDB; Q54H37; -.
DR SMR; Q54H37; -.
DR STRING; 44689.DDB0232056; -.
DR PaxDb; Q54H37; -.
DR PRIDE; Q54H37; -.
DR EnsemblProtists; EAL62574; EAL62574; DDB_G0289725.
DR GeneID; 8627293; -.
DR KEGG; ddi:DDB_G0289725; -.
DR dictyBase; DDB_G0289725; fscA.
DR eggNOG; ENOG502RFCB; Eukaryota.
DR HOGENOM; CLU_036764_0_0_1; -.
DR InParanoid; Q54H37; -.
DR OMA; WILDEID; -.
DR PhylomeDB; Q54H37; -.
DR PRO; PR:Q54H37; -.
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 Coiled coil; Glycoprotein; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..549
FT /note="Frizzled/smoothened-like sans CRD protein A"
FT /id="PRO_0000371354"
FT TOPO_DOM 23..89
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 111..119
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 141..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..198
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 220..241
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..308
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 309..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..367
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 368..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 417..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 432..475
FT /evidence="ECO:0000255"
FT COMPBIAS 535..549
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 549 AA; 63275 MW; 30F3E2E37B4E1280 CRC64;
MKFNFKLILI ILIINQILII NCKENKILEI YKSGNICPYP LHYRERTGSD DHDFDLGFVY
ARNDSNCLLP CPSPIYTSQE VNTLSLMIKI TGTISFIASL ILLLIYSPLI NRMGYNRHTI
GIFFLTFSVF LIMLTDIIYV HHGNDLICPQ SHRYSRQNDS GCTITGILFQ YGCIAAVLFW
ATLSLDLYLT LKKISTKKVE KWYLIILTLI ALILTFVPLV KKSYGYLVTG LACWILDSTD
QIIFFWAPFT AILGIGSILI VLVVYEIYKI SKITKQNRGI FQSHIRPLLM VLFIFGQFLF
ILAFNALINN KYDEYSARMD SYIDCLFSSS SYSYLCRLKT FPFEMEFIVL FFLRLIGIEV
LIFYGFTQQT KKILLHSFLV NNIFFKKYFI RLDGASLDFS TVDEELKVVN FSCNNNNNNN
NSNSNSNSNL NNNLNNNLNN NNLNNNNNLN NLNNLNINNN LKNSQNNLNN SQQNEPLSSQ
KLSENGNVNV FMVESFDNNN SMINQFKHLE EKNNIILNSI ISPVQEEQYE EDEINNKNIN
NNSNNDENN
