ID C3YCR3_BRAFL Unreviewed; 758 AA.
AC C3YCR3;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=CUB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_90827 {ECO:0000313|EMBL:EEN61864.1};
OS Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC Branchiostomatidae; Branchiostoma.
OX NCBI_TaxID=7739;
RN [1] {ECO:0000313|EMBL:EEN61864.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61864.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61864.1};
RX PubMed=18563158; DOI=10.1038/nature06967;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA Satoh N., Rokhsar D.S.;
RT "The amphioxus genome and the evolution of the chordate karyotype.";
RL Nature 453:1064-1071(2008).
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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DR EMBL; GG666502; EEN61864.1; -; Genomic_DNA.
DR RefSeq; XP_002605854.1; XM_002605808.1.
DR AlphaFoldDB; C3YCR3; -.
DR STRING; 7739.C3YCR3; -.
DR eggNOG; KOG3645; Eukaryota.
DR eggNOG; KOG3714; Eukaryota.
DR InParanoid; C3YCR3; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0098794; C:postsynapse; IEA:GOC.
DR GO; GO:0045202; C:synapse; IBA:GO_Central.
DR GO; GO:0022848; F:acetylcholine-gated monoatomic cation-selective channel activity; IBA:GO_Central.
DR CDD; cd00033; CCP; 1.
DR CDD; cd07066; CRD_FZ; 1.
DR CDD; cd00041; CUB; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 1.20.58.390; Neurotransmitter-gated ion-channel transmembrane domain; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR036719; Neuro-gated_channel_TM_sf.
DR InterPro; IPR038050; Neuro_actylchol_rec.
DR InterPro; IPR006029; Neurotrans-gated_channel_TM.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR PANTHER; PTHR46335; CUBILIN; 1.
DR PANTHER; PTHR46335:SF3; CUBILIN HOMOLOG; 1.
DR Pfam; PF00431; CUB; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR Pfam; PF02932; Neur_chan_memb; 1.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00032; CCP; 1.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 526..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..108
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT DOMAIN 149..281
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 277..348
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 351..418
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
SQ SEQUENCE 758 AA; 83923 MW; 9CF848D1D76180BE CRC64;
MSLTADSGSF TSPNYTNNYP DNSNCTYKIS VTPPKVIRLT FTDFNTEEDY DFVYVYDGDT
VDPSQLIGKF HGASLPDPRT SSGSVMTVRF TSDEYETRKG FQANYAAEDK VFARCGVGQY
RCANGVTCID AWRRCDGNND CRDRSDEDAS SCACQDIPSS LTICRGLEWG SKMTLPNPLD
YSHTTLDMVT NSAAFTDLES LAESDCHPRV RELVCATIVP RCEASPNLRQ KLPCRSWCEE
VKYSCNNEDS WEAFPNCEIF PYTNCNNIKT SMKDGVECFD GNGANYRGDE SRAPIAGVDC
SAWSDEQGII AYYPWANLVG NKCRNPDDWN RPWCYKPDGY EDCDIVPCNI KGCKDPGKPQ
FGQRSPKLKF YWPDDTITYT CDTGYKFKKD TTPNRALCVT DDETGEVDWE TDKPECEVDQ
KFQLQKDLLS ANVYNKAVSP TTSLNIKAYV VNVINLDNMT CAVCWRAGEE YTIDCSNSTT
HKDSNFLTCQ NYEADIVTGE WSGKTTLSAR NNTACLTMTL KRDPTYHYST TISPCLILII
LMIITFIMPI DKGDRIGFGV TVLLSMVVSL VVVTGFLPVS STLPFIAMLI IVCMALMALF
MLTTLFIIII HDKKGPVPKW ARTIFLKHIA RALLMGDLTK KLKKEDPAKY ANDIERHTKA
GGQDPAIGGA NPPLNVKNEV GATLIGLKGS VDELKASVEQ LSGSIDAMAS GGDDDEEVGE
YALLAKVLDR LSLVLYIVAI AVAIPCTLLI GRPKITPS
//
