FSLL_DICDI
ID FSLL_DICDI Reviewed; 619 AA.
AC Q54PF8;
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 L;
DE Flags: Precursor;
GN Name=fslL; ORFNames=DDB_G0284585;
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; AAFI02000067; EAL65147.1; -; Genomic_DNA.
DR RefSeq; XP_638502.1; XM_633410.1.
DR AlphaFoldDB; Q54PF8; -.
DR SMR; Q54PF8; -.
DR PaxDb; Q54PF8; -.
DR EnsemblProtists; EAL65147; EAL65147; DDB_G0284585.
DR GeneID; 8624666; -.
DR KEGG; ddi:DDB_G0284585; -.
DR dictyBase; DDB_G0284585; fslL.
DR eggNOG; ENOG502RF31; Eukaryota.
DR HOGENOM; CLU_030318_0_0_1; -.
DR InParanoid; Q54PF8; -.
DR OMA; IFCIRIY; -.
DR PhylomeDB; Q54PF8; -.
DR PRO; PR:Q54PF8; -.
DR Proteomes; UP000002195; Chromosome 4.
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; IPR020067; Frizzled_dom.
DR InterPro; IPR017981; GPCR_2-like.
DR PROSITE; PS50038; FZ; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..619
FT /note="Frizzled and smoothened-like protein L"
FT /id="PRO_0000371373"
FT TOPO_DOM 25..245
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 246..266
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 267..278
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 279..299
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 300..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..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..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 445..465
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 466..497
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..619
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 31..169
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 581..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..605
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 4
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 63
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 143
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..106
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 48..99
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 619 AA; 70185 MW; E3BC122116759F2D CRC64;
MITNKSKYYF FLILIFINFY LINCQEEYPI DQTGKCEPYI GDSQITKCST FLPNINSIYV
SANSTQKDSM KTLDNYFGLL LAVGSEKCKD SSLTYQTLCS MYLKECESFT DNSTLKTVSI
PKRICRKTCN DVTKLCNIES LFNCSQNEPI NNLPLCPLNY SIYDLSLVNG DSNYELQCYS
PLSNDSIEIP VTNYCPFPLI YINSTDHSAD EDRGYMFVSG NSNCVVPNPV PLYTPKQWDR
LYDLSNSLSV LSCVGTLFLL FTFNILNKKI NRFDRMNSLF NGSVFMMSLS GVIILFAGGP
RALIKDGGAR ISVWQDPLCS ATGFIFQLFS IAAILFWVVM SFELWYKIKF MTKKLDLKKY
YIPFIIIVSL VFSIIPLATK NYRMIRGNMH CWVHTTKLQN SLFWIPLGIA ITIGTIFIGL
VMFEIHRIVS ANSKGGVLKL EIKSILNVAL IYLTFIYLFA FNFYMNGQEG VVYGQIESFY
QCTLENDASE CTIQGPSIGS LGFFIFCIRI YGVYCFILQG LNYRAYNIWK ESIFFNNRFV
SYIKNNILNI ETSSTGSGGT STTASATTTT TTKKHNGIDS LNIDSAFSKN NESDDEDDYD
PYKKSKNNIT LKDIEVSKS
