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FSLN_DICDI
ID   FSLN_DICDI              Reviewed;         611 AA.
AC   Q55CY2;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Frizzled and smoothened-like protein N;
DE   Flags: Precursor;
GN   Name=fslN; ORFNames=DDB_G0270672;
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; AAFI02000005; EAL72686.1; -; Genomic_DNA.
DR   RefSeq; XP_646349.1; XM_641257.1.
DR   AlphaFoldDB; Q55CY2; -.
DR   PaxDb; Q55CY2; -.
DR   EnsemblProtists; EAL72686; EAL72686; DDB_G0270672.
DR   GeneID; 8617304; -.
DR   KEGG; ddi:DDB_G0270672; -.
DR   dictyBase; DDB_G0270672; fslN.
DR   eggNOG; ENOG502RBR8; Eukaryota.
DR   HOGENOM; CLU_447205_0_0_1; -.
DR   InParanoid; Q55CY2; -.
DR   OMA; ASENDSC; -.
DR   PhylomeDB; Q55CY2; -.
DR   PRO; PR:Q55CY2; -.
DR   Proteomes; UP000002195; Chromosome 1.
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..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..611
FT                   /note="Frizzled and smoothened-like protein N"
FT                   /id="PRO_0000371375"
FT   TOPO_DOM        25..230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        231..251
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..258
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        280..302
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        303..323
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        324..338
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        339..359
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        360..380
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        402..430
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        431..451
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        452..491
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        492..512
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        513..611
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          26..187
FT                   /note="FZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   REGION          538..611
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        538..554
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        569..611
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        140
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        179
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..98
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        40..91
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        82..125
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        114..184
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
FT   DISULFID        118..170
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00090"
SQ   SEQUENCE   611 AA;  69796 MW;  72F4D74993CC2203 CRC64;
     MKMKMKILLI FLKFFFLKKL FVNSLDIGSK CEILNPISMC SNYLGYKNIY LPYGYTQEII
     EANVTATLTN PMGFSAIPDL ICKENIIKLF CISTYRECNS NINGISFPLP SNPCQKNCFK
     VLETCVPFLS FFQGFSCQQN DTDGKDLYPI TENYYNLTSY GGSSNQSIQC SNPNQGSTNT
     TVSCVYPLVY VSTDDIKNGE KFHEVMPNCV LPCPLYVYTD KQYDAKFYTE VVFYCVSATI
     AVYLILTFGL IQNKITHRSW IIIYLGFTVL ALCASYATQQ YGNGDFRCSS QPGRYRSSQD
     GNCMLTGFFF QMGGLGTIFM LSLYSFDFFL TINMKTNKYF LQTSIGVWAL IFFFALLPIK
     HYESTIDSAG CWIGEYNNRF WLYFCFYIPA YIVTFLMVIF ITSSIYKVFK MTVLFKSIND
     RRILFLNLRS VTFLLVILFC ISFTSMYPLY VSYNGEVFYD AIEKWVYCLL EKGNDQCPRI
     QFSRFGLRYM NAFCMSIIGI LLLFGLGIDP HIATIYRESE RFNYLLHLVG IKWGNTPVPS
     KKSSTSSNSS GSSGEKTRET RKTRGQSISL KKIDQSNSNS NSNEIESSSI DKQPSSILNN
     HNNNDDKQSQ A
 
 
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