FSLP_DICDI
ID FSLP_DICDI Reviewed; 587 AA.
AC Q54LJ7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Frizzled and smoothened-like protein P;
DE Flags: Precursor;
GN Name=fslP; ORFNames=DDB_G0286607;
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; AAFI02000089; EAL64059.1; -; Genomic_DNA.
DR RefSeq; XP_637564.1; XM_632472.1.
DR AlphaFoldDB; Q54LJ7; -.
DR SMR; Q54LJ7; -.
DR STRING; 44689.DDB0232054; -.
DR PaxDb; Q54LJ7; -.
DR EnsemblProtists; EAL64059; EAL64059; DDB_G0286607.
DR GeneID; 8625703; -.
DR KEGG; ddi:DDB_G0286607; -.
DR dictyBase; DDB_G0286607; fslP.
DR eggNOG; ENOG502RGJ6; Eukaryota.
DR HOGENOM; CLU_447205_0_0_1; -.
DR InParanoid; Q54LJ7; -.
DR OMA; MYFSRDE; -.
DR PhylomeDB; Q54LJ7; -.
DR PRO; PR:Q54LJ7; -.
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 SUPFAM; SSF63501; SSF63501; 1.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..587
FT /note="Frizzled and smoothened-like protein P"
FT /id="PRO_0000371377"
FT TOPO_DOM 21..232
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 282..304
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 305..325
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 326..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..387
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 388..408
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 409..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..587
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 24..154
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 539..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..556
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 568..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 43
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 61
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 180
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 232
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 288
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 29..92
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 38..85
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 76..125
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 118..138
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 587 AA; 65872 MW; F3922918DD905894 CRC64;
MKKLNFLICI INILFLFVNS QDLKLGGSCE LIDSNSPCFS KLNYTDFYLQ PGDSITQLNK
NVSDIIRMLE FTTPECKPNA INLICLKSYP KCETHNETLS NNTNIIFNLP SLPCNSICLI
AETPCKIFID NFLKDLSCSS KFSNGVPMFP INSTDFEFKE SGNFDFNFNV ECNDNIIYDN
SSSVINCPAP LLNSKDHVIP GKTTYYYITD SCILDCPFEI YPGKTKILDK TNYTLTSISF
ITCFFMILTF GVLPNKITHR MESILSFACG GCITALSLFI QSRQDNFNCS SDPGRFKSQS
DYLCLLTGLI FQFGAITSIF WAPMIAYDFY ITSRLSKIRK FGLYRIGIWS LIFVLTALPA
FGGKYSATVA TSCWINSDDG SAWQYISFYI PSWCAMGLLC LFSILSVINV SKMYMKSPNR
RILFFNIKII ITSLILLFNL TFASSLKFYM EDKMDTYFDA IAVWAECISK GDPSQCELHA
PGYELKALNV VVVSILGFCI FIGYGLDPIV IQIWKESEKL KWILKKCGLN DFIKLGSETT
STTNTSGSSG SGSEKRQSKI RMSKLSPPPP SIDTTNDIPI NDTLGEN
