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Database: UniProt
Entry: C3YBB3_BRAFL
LinkDB: C3YBB3_BRAFL
Original site: C3YBB3_BRAFL 
ID   C3YBB3_BRAFL            Unreviewed;      1274 AA.
AC   C3YBB3;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN62270.1};
GN   ORFNames=BRAFLDRAFT_83988 {ECO:0000313|EMBL:EEN62270.1};
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:EEN62270.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN62270.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN62270.1};
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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; GG666497; EEN62270.1; -; Genomic_DNA.
DR   RefSeq; XP_002606260.1; XM_002606214.1.
DR   AlphaFoldDB; C3YBB3; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   eggNOG; KOG3645; Eukaryota.
DR   eggNOG; KOG4292; Eukaryota.
DR   InParanoid; C3YBB3; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 2.
DR   CDD; cd00041; CUB; 2.
DR   CDD; cd00108; KR; 1.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd19051; LGIC_TM_cation; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 1.
DR   Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 2.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 2.70.170.10; Neurotransmitter-gated ion-channel ligand-binding domain; 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; 2.
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; IPR018056; Kringle_CS.
DR   InterPro; IPR038178; Kringle_sf.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR006202; Neur_chan_lig-bd.
DR   InterPro; IPR036734; Neur_chan_lig-bd_sf.
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; PTHR24255; COMPLEMENT COMPONENT 1, S SUBCOMPONENT-RELATED; 1.
DR   PANTHER; PTHR24255:SF28; SUPPRESSOR OF TUMORIGENICITY 14 PROTEIN ISOFORM X1; 1.
DR   Pfam; PF00431; CUB; 2.
DR   Pfam; PF01392; Fz; 2.
DR   Pfam; PF00051; Kringle; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF02931; Neur_chan_LBD; 1.
DR   Pfam; PF02932; Neur_chan_memb; 1.
DR   Pfam; PF00084; Sushi; 1.
DR   PRINTS; PR00018; KRINGLE.
DR   PRINTS; PR00261; LDLRECEPTOR.
DR   SMART; SM00032; CCP; 1.
DR   SMART; SM00042; CUB; 2.
DR   SMART; SM00063; FRI; 2.
DR   SMART; SM00130; KR; 1.
DR   SMART; SM00192; LDLa; 2.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 1.
DR   SUPFAM; SSF63501; Frizzled cysteine-rich domain; 2.
DR   SUPFAM; SSF57440; Kringle-like; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF90112; Neurotransmitter-gated ion-channel transmembrane pore; 1.
DR   SUPFAM; SSF63712; Nicotinic receptor ligand binding domain-like; 1.
DR   SUPFAM; SSF49854; Spermadhesin, CUB domain; 2.
DR   PROSITE; PS01180; CUB; 2.
DR   PROSITE; PS50038; FZ; 2.
DR   PROSITE; PS00021; KRINGLE_1; 1.
DR   PROSITE; PS50070; KRINGLE_2; 1.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS50923; SUSHI; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}; Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW   Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW   ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW   Protease {ECO:0000256|ARBA:ARBA00022825};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|PROSITE-ProRule:PRU00302};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..1274
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002933573"
FT   TRANSMEM        1039..1063
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1070..1090
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1096..1122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        1252..1271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..169
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          208..309
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          414..534
FT                   /note="CUB"
FT                   /evidence="ECO:0000259|PROSITE:PS01180"
FT   DOMAIN          573..705
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          701..772
FT                   /note="Kringle"
FT                   /evidence="ECO:0000259|PROSITE:PS50070"
FT   DOMAIN          765..834
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DISULFID        196..211
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        414..441
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00059"
FT   DISULFID        561..576
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        630..668
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        805..832
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   1274 AA;  140082 MW;  EA6C887C0D35C11F CRC64;
     MSWPWVVFSY LLLQSAVGVV FSTDCNPTYL NGSTGTFSSP NYPNKEYPRD LDCTWTITVH
     IEKKIKVTFD VFDVEYHDNC AYDHVILEEN GEPISLPDLG PTEIDGEPED YPDVDLVKRT
     QDGGKFCGTL PGDTTMRGNY TSVSNVMTVR FRSDTWVSKT GFSATYSAID KVPAVCTNVE
     KLCDDLLGCV ALAKICDGSD DCQDKSDERN CECVEIPTEL GICKGAIDYG NMVYPNLYGH
     QNKMALLDSD TFAELQSIQN NTCHADVFAM VCSMLAPKCV EEVGTGNARR GEIKPPCRTW
     CPEISTSCAD ANLFPDEICG TLPFSADCFI NRADDVTSPP QSPTGQGETG EFLETGEFPE
     TGEFLETGEF LETGEFPETG EFLETGEFLE TGEFLETGEF LETGEFLETG GGGCGGLLPP
     NTGTFSTPNF GSGHYSVNTD CVWSLRVNPG LVPRITFNTF KLEAGPSPGD CPFDYVRVFD
     GEWPGGKFKS ATNKLCGEVP PGTNVTTDSY ILTIIFSSDK GGTEEGFLAS YTTDDRGTLT
     CGVGEKLCGD GALCVSMARR CDGRFDCWDK SDERDCECDP LEGELQTLCE SRDESANFMT
     FPNLIGHVSS SSLTASPEFN VLKMLMTSTC HVDIAEFVCE MMAPRCDRLT KVIMAPSRSW
     CEEVRSSCKD EDQWPSSFPS CDVISENPEG IEGLRGTTDN ECYHGKGTNF RGGHSETETG
     RTCTAWADHV YEMNTFRWAN LDSNYCRNPG NIAERPWCYV GDQWEFCSVP PCSGLVCSDR
     GQPRSVTAGP RKQSYWPGDK VTYQCDPGYS LQGSAVIKCL ANATWDNDLP TCVVDERLGL
     RNDLFDFYSK DLSPSESDDH VTAVFSGQVL NVVSLDEKGP EVLTDIVLEL RWRDHRLTWS
     PATYGGQDIL RVSYDEVWTP TVVLQNNADR GFTSFPTVDV TITSGGEVIW LVQTLVSTTC
     VLDQYLFPFD SMMCPVCVKT GRKEERLSCP LPENITAENN LNCNSSASLV TGEWAVAISA
     DVSSSDMGCL NLNLQRNPTY HMCTTIAPTI VLAVLMCVTF LLPIDKGDRL SYGMAILLAM
     VVSLVVITDF LPRSTIIPFI GTFVIVSMSL MAVFMLATVG IINVSGKQGK VPPWARNVFL
     RCMAQCLLMG NLAKESDTPE AVPNKVYVEE SSHDNGAFAT FGEEQVLWDT SAKFRSTGDH
     PPDAPTMMPG MKVMIYAIRK SLDRLNVTIE GLRPNDEEES EWMLLSYVLD RLCLVLYIIG
     IIAAVPLSLF LGRS
//
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