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
//