ID C3XUY7_BRAFL Unreviewed; 1576 AA.
AC C3XUY7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE RecName: Full=CUB domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_88946 {ECO:0000313|EMBL:EEN68212.1};
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:EEN68212.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN68212.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN68212.1};
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:PRU00124}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GG666467; EEN68212.1; -; Genomic_DNA.
DR RefSeq; XP_002612203.1; XM_002612157.1.
DR STRING; 7739.C3XUY7; -.
DR eggNOG; KOG0260; Eukaryota.
DR eggNOG; KOG1575; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; C3XUY7; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR CDD; cd15039; 7tmB3_Methuselah-like; 1.
DR CDD; cd00112; LDLa; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 1.
DR Gene3D; 1.20.1250.20; MFS general substrate transporter like domains; 1.
DR Gene3D; 3.20.20.100; NADP-dependent oxidoreductase domain; 1.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR Gene3D; 2.60.120.290; Spermadhesin, CUB domain; 1.
DR InterPro; IPR000859; CUB_dom.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR InterPro; IPR035914; Sperma_CUB_dom_sf.
DR PANTHER; PTHR20851:SF0; APOLIPOPROTEIN(A); 1.
DR PANTHER; PTHR20851; DORSAL INTERACTING PROTEIN 3; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR Pfam; PF00057; Ldl_recept_a; 1.
DR PRINTS; PR01217; PRICHEXTENSN.
DR SMART; SM00042; CUB; 1.
DR SMART; SM00192; LDLa; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 1.
DR SUPFAM; SSF51430; NAD(P)-linked oxidoreductase; 1.
DR SUPFAM; SSF49854; Spermadhesin, CUB domain; 1.
DR PROSITE; PS01180; CUB; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50068; LDLRA_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 551..570
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 627..648
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 668..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..736
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1005..1026
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1033..1052
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1092..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1415..1440
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 606..763
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT DOMAIN 1233..1353
FT /note="CUB"
FT /evidence="ECO:0000259|PROSITE:PS01180"
FT REGION 398..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 780..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 860..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1450..1576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..807
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 865..880
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1456..1576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1363..1375
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 1370..1388
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1576 AA; 173913 MW; C3BC39C8063C5E76 CRC64;
MATEMVSMNG KAGLSSLFPP RRKEDSLHDH VKVLIQRSKA DFFRGLDDDQ LRRLPDHVRP
RVPVTDVTYS RCVTKSVRVR CTKLVFAYEY ETQEAWGAVF REKLQKPKDE GGFGTLEATY
KDAERLWREH SPDYKPGRSV ARPGKLPDGR LNIRRTRQPE DTEAGYRKRL RQESMAELDT
VSQMDAFYPY NMIKRRNKDR VWSSFVKQYK VDMADKTEYR FLGGSGLKVS NICLGTLTFG
NWALFPGQCD EAASHAILDR YVELGGNFID TADIYAEGRS EETIGTWLEK QQREKFVVAT
KVRFNTSKDI NSVGLSRHHI MQSIDDSLRR LRTAYVDLYQ VTIAVLPRLN MEELMFELNR
RIQNLNKENS IKDRLVSILR DVMLEEYCQL KSQSEMTMPE RDCSGLDIKN SEENNDTSNE
VLTPKEELAL HAVQVQMKTT LSPSDTSLIR SMNTAVDSLA LKKKKMLLWR PRMKQDTRPG
VLMKKGLPVP LPNCSEPTLT FTAEEFHILP NGSIHLVSSN VSCPAEQVAI LNTTASICGE
CILSWDSHQS WSTVTGLVIA SVVAVFGFVA HTVRSGQWKK IGLYSVCNHS ALSPVDGLHV
NERTIAIDLF LTFSDGLVIE RVKLYKYLLY TWLMSMPVVV VTVIVEFGTF VRVGYGERCW
IGNPTASLLA FFVPVLCALI VNTVLVTFVL RAIRKSFQIA NAALSRSQSS KAWVYIRISF
LMGFTWIIGF IYPYVQSRVM ELIFIALNAS QGLLLTVMMT MTGEVVQIWR SAIKARFGFG
NQTDRPTTTA GNQQQTTTSG TQETAGRAVS TVVNVGENRA PGESHQDSEQ IATMGTEPGE
VGSAVDITMA TVVDIEETTR ARLQPGESHQ DSNYESPQGE LRQSRPGHVF NLVSRIRTVI
SGATATRGTE AGDEVGYATD IPMTTVVDIE EARARLQPVC GQVGPRCFCR LSLQLVQGLP
LRLLHSPGVH SVTRSVHLLS CSLATCPAQW YLAPHVEYSQ FQVGVILSSV YAGLLPSSFI
GGFLAYRYSA TRVFLTSIGI SSVVHCVAPI MFQRFGTAVT QRVLAGLAEG QAEPAAYGVL
GEYMIPRQSA RVAPFVFSGC LGIVWTTVSI GFEATGVAKK REKDETAKQD KDEITNMAGV
LAGIPILAFG ALEPVFALLG NFLCKYVTTT VTRKAMAVTV ADANAFDIAP RYASVISGLC
RVLCRIVGLT FPLLVAALTK DKACNILYMY NMCGQSKNVG MKDSGTIKWR IGDGYQANMD
CVMTLTSADP RVRVNLRIEK IDLRGSSIAC MDTLTAYDGR GATGRTLFTG CDDDYVGKNM
VFSSSGNAVS LRLSSTMGFG NVGDGFRIAY NMFYDASTSG GKCQPGEFRC TNNRCIDEVL
KCDFDDDCGD RSDESDNKAE AGCDFTKVFK GIMKIGVTGL VLVVLGIVLV CCCCCGAVYL
MNKRRGNSGQ TVTIPMEPQQ PPPQPSPQPS PYPGGKPDQP YPPDQPYPPP QPGYPPQQPG
YPPQPGYPPQ QPGYPPQQPG YPPQQPGYPP QPGYPPQQPA YPPQQPGYPP QGEPAPPPYH
PSAPPPPQDP AYPPPQ
//
