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FSLQ_DICDI
ID   FSLQ_DICDI              Reviewed;         578 AA.
AC   Q1ZXE4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-MAY-2006, sequence version 1.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=Frizzled and smoothened-like protein Q;
DE   Flags: Precursor;
GN   Name=fslQ; ORFNames=DDB_G0286609;
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; EAS66849.1; -; Genomic_DNA.
DR   RefSeq; XP_001134532.1; XM_001134532.1.
DR   AlphaFoldDB; Q1ZXE4; -.
DR   SMR; Q1ZXE4; -.
DR   PaxDb; Q1ZXE4; -.
DR   EnsemblProtists; EAS66849; EAS66849; DDB_G0286609.
DR   GeneID; 8625704; -.
DR   KEGG; ddi:DDB_G0286609; -.
DR   dictyBase; DDB_G0286609; fslQ.
DR   eggNOG; ENOG502RGJ6; Eukaryota.
DR   HOGENOM; CLU_447205_0_0_1; -.
DR   InParanoid; Q1ZXE4; -.
DR   OMA; FYLEERI; -.
DR   PhylomeDB; Q1ZXE4; -.
DR   PRO; PR:Q1ZXE4; -.
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..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..578
FT                   /note="Frizzled and smoothened-like protein Q"
FT                   /id="PRO_0000371378"
FT   TOPO_DOM        24..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        262..282
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..305
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        306..326
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        327..341
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        342..362
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..388
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..422
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        423..443
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        444..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..578
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          27..157
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          544..578
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        46
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        64
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        99
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
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        181
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        233
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        289
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        32..95
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        41..88
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        79..128
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        121..141
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   578 AA;  65439 MW;  B2D21815B36980B9 CRC64;
     MKNSFLINIL IIYYLFIILF VNSQDLKLGG SCELIDSNSP CFSKLNYTNF YLQPGDSITQ
     LNKNVSDIIR MLEFTTPECK PNAINIMCLK SYPKCETYNE TLSNNTNIIF NLPSLPCNSI
     CLKAETPCKI FIDNFIKDLS CNSNFSNGAP MFPINSTDYE FKESGNFNFN VECNDNIIYD
     NSSSVINCPA PLLNSKDHVI PGKTTYYYIT DSCILDCPFE IYPGKTKILD RTNYTLTSIS
     FITCIFMILT FGVLPNKITH RMESILSFAC GGCITALSLF IQSRQDNFNC SSDPGRFKSQ
     SDYLCLLTGL IFQFGAITSI FWSPMIAYDF YITSTLGKIR KFGLYRIVLW SFIFVLTALP
     AFGGKYSATV ATNCWINSDD GSAWQYVSFY IPSWCAMGLI CLFSILSVIN VSKMYIQTPN
     NRILFFNIKI LITLLLFLFV LTFASSLKFY MEERMDTYFD AIAVWVECIG KGDPSQCELH
     APGYDLKALN IVVIGILGFT VFIGYGLDPI VIHIWMESKK FQWVLKKCRL DKIIKLNNSI
     NNSNNNNNET ASTSSGNERK QTTVKMSNLK STEINQQP
 
 
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