FSLJ_DICDI
ID FSLJ_DICDI Reviewed; 607 AA.
AC Q556J4; Q86K08;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Frizzled and smoothened-like protein J;
DE AltName: Full=Cell number regulator protein A;
DE Flags: Precursor;
GN Name=fslJ-1; Synonyms=cnrA; ORFNames=DDB_G0272885;
GN and
GN Name=fslJ-2; ORFNames=DDB_G0274011;
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=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
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 [3]
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 -!- DOMAIN: Lys-Thr-X-X-X-Trp motif interacts with the PDZ domain of Dvl
CC (Disheveled) family members and is involved in the activation of the
CC Wnt/beta-catenin signaling pathway. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor Fz/Smo family.
CC {ECO:0000305}.
CC -!- CAUTION: The gene for this protein is duplicated in strains AX3 and
CC AX4. These strains contain a duplication of a segment of 750 kb of
CC chromosome 2 compared to the corresponding sequence in strain AX2.
CC {ECO:0000305}.
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DR EMBL; AAFI02000011; EAL70439.1; -; Genomic_DNA.
DR EMBL; AAFI02000009; EAL71080.1; -; Genomic_DNA.
DR RefSeq; XP_644364.1; XM_639272.1.
DR RefSeq; XP_645050.1; XM_639958.1.
DR AlphaFoldDB; Q556J4; -.
DR PaxDb; Q556J4; -.
DR EnsemblProtists; EAL70439; EAL70439; DDB_G0274011.
DR EnsemblProtists; EAL71080; EAL71080; DDB_G0272885.
DR GeneID; 8618726; -.
DR GeneID; 8619250; -.
DR KEGG; ddi:DDB_G0272885; -.
DR KEGG; ddi:DDB_G0274011; -.
DR dictyBase; DDB_G0272885; fslJ-1.
DR dictyBase; DDB_G0274011; fslJ-2.
DR eggNOG; ENOG502RD8Q; Eukaryota.
DR HOGENOM; CLU_030318_0_0_1; -.
DR InParanoid; Q556J4; -.
DR OMA; LFIYDQW; -.
DR PhylomeDB; Q556J4; -.
DR PRO; PR:Q556J4; -.
DR Proteomes; UP000002195; Chromosome 2.
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 Gene3D; 1.10.2000.10; -; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..607
FT /note="Frizzled and smoothened-like protein J"
FT /id="PRO_0000371371"
FT TOPO_DOM 27..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..276
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..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..401
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 402..422
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..451
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 473..508
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 509..529
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 530..607
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 32..182
FT /note="FZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT REGION 559..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 532..537
FT /note="Lys-Thr-X-X-X-Trp motif, mediates interaction with
FT the PDZ domain of Dvl family members"
FT /evidence="ECO:0000250"
FT COMPBIAS 559..586
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 133
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 190
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 222
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 298
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 37..108
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 50..101
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT DISULFID 127..179
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ SEQUENCE 607 AA; 68945 MW; 9216C7BFDABFC10F CRC64;
MVSNKNLLPI IYIFFIILYF GDVAKSQYFP LDKGATCQKY RGDSPGIQLC DGFLSNPNSI
YINSTSSQEA IQAQGNLVRQ YINFYKSFES CKNPRTFALL CAFLFPECEK YTDPVSKVTY
AYPILPCYNN CLNMTTSCQI STSRLSCATK YTFENISYSV FPKNTTTYQI DSLSYTNTCE
NTDLIANSQN TSIQQCFEPL VYHVSTDEIH DKSIGYIFPS TNTTCVVGCP APLYYANQWR
NIYRLSDVLS ILSCILTLFL VITLGIINPK VSRFDKINVM LLSSIFLQAF SGALMTFNGT
ENTLCPEDGR FASYIDRMCV ATGFLLHGSS LLVVQWWCVL SFEVWFTIFQ VGKKQKDRFI
YYLVASLIIA WIPPIVSISK NEYSGGPANP FCWLTTFNYR RFAFWLPMGI FLCLGGVFLI
LLMREIYVIV SGNVQSTKES RFKVLKMEAK PIISLIMYFS CLLYLFIYDQ WINNHMHVYT
DSIPSYALCL LTSTSTNDCL LKAPDITGLG YFIYSIRVFG VYAFIIYGIS KKTLQIWKYN
YFVVFIGQKI EQFTNATTTA KSSNSNNSST TNNISVKASS NMEYETRQEN ENGDSQSVEL
DSNSDAL
