ID C4A0U5_BRAFL Unreviewed; 1269 AA.
AC C4A0U5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=G-protein coupled receptors family 2 profile 2 domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=BRAFLDRAFT_111801 {ECO:0000313|EMBL:EEN41586.1};
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:EEN41586.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN41586.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN41586.1};
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; GG666827; EEN41586.1; -; Genomic_DNA.
DR RefSeq; XP_002585575.1; XM_002585529.1.
DR AlphaFoldDB; C4A0U5; -.
DR eggNOG; KOG3627; Eukaryota.
DR eggNOG; KOG4193; Eukaryota.
DR InParanoid; C4A0U5; -.
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; cd00108; KR; 2.
DR CDD; cd12819; LbR_vir_like; 1.
DR CDD; cd00112; LDLa; 3.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 3.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR000832; GPCR_2_secretin-like.
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; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR PANTHER; PTHR20851:SF0; APOLIPOPROTEIN(A); 1.
DR PANTHER; PTHR20851; DORSAL INTERACTING PROTEIN 3; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00051; Kringle; 2.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00130; KR; 2.
DR SMART; SM00192; LDLa; 3.
DR SUPFAM; SSF101967; Adhesin YadA, collagen-binding domain; 1.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 3.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50958; SMB_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121};
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 764..786
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 798..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 821..854
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 866..887
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 907..932
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 953..974
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 980..1000
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 389..465
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 507..563
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 572..616
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 760..1002
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 90..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1046
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1104..1133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1133
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 295..313
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 307..322
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 327..345
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 339..354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 359..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 371..386
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 408..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 436..459
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 507..546
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 535..558
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 1269 AA; 138634 MW; 769CC944D44A5540 CRC64;
MAPRKKGRKA EDIARKFKSH RTEYVRLKRL KKGKSGSGKV LLTSLQRWKL ERYQFLDPFC
VSKLPEDLGS QCIEQHHALM LQIFNTENSE EGIEEEAEED GNVVAGTSTG GTTPCGSHAI
GSKGVKRPNS SDNPNSKKKA VTTSSLSDVL AKFLHDTEKE KSRAQKEVEN LAKESQQPVD
ERFAWSQWLT STCFRVPPAH FYQYQRETFE TTMRWLPNEP AALPGRPMPG PPVLAPPRHY
TPHQGYTPLQ PPTQHNTPDF AQLHGEEQQH SVMGWMPAAP QARQTACSGV ERTVCKDGDC
DVLEVVCDGI VDCDDGSDEN DCDKEICPSG VTINKAEVCD GTDDCGDNTD EQSCSPSACD
NGALFHQLSR CDGRDDCGDN SDEQNCICYY IQDRGTSYRG LANRDNSCQL WTSQYPHPHK
HTPQAYPRAG LERNYCRNPD GKDRPWCYLN NPLIRWMYCE EVFACDGQVT GCVRDWTPSP
LTAISIHHRL FTRLYTVYLY RAGDRMCQRW DSQSPHSHPH TPQAHPDAGL DENFCRNPDN
KERPWCYTTD ESQRWDYCDV MECADPLSPD SVGQDCHRDY TCAKYFLLRL CYCDEDCSFF
GDCCEDFEGG SESQMPSDHH HLKWDCVSGL SPVIESNKIN KESYWMVADC PDEWTDDVTR
DKCLKQVDPF NPNTCRLFSS SRRTHGSLNN TTPLQNCSEP ALTFTAEEFR VLPNGSVLLL
GSNVSCSAEQ VAILNTTASI CGECILQYFS NYTQTANPWD ATQGWLTLGL VIVSAVAVVG
YVVHNIRSGQ WEKVPEKLKV QVLVCMAFAE VLFMVRVRVP LGSACAAFAI ILHYFLLTAF
TSMNALAMDL FLTFRDALER AKLYQYLLYT WLMPVPIVIV TVIVEFGSSV SVGYGENCWI
GNPVANLVAF GVPVFSAILI NAVLATFVLL AIRKSFVIAD KAKSRSNSSK AWVYLRICFL
TGFTWILGFI YPYVNSRAVE YIFIVLNASQ GLLLALMLTI TSKVVQKWKV AIRERFGLAE
PNKDNRATTA AIKQRTTATA SETSSSADIP LTTFTDVEEN RARIQLDSPN RASGCTATVS
NRKTTVCATC TEMPKTTLAD VEKTARSHLN KPQQDNGATA AASTKLASTG GTDAVASGSD
VVAGGSDEVA GGSDVVAGGS DVVAGGSDEV AGGNDVVAGG SDVVAGGSEV VAGGSDVVAG
GSDVVAGGTD VEVGESDALA GENDVVAGGI DVVAGGTDVV AGGTDVVAGG TDEVGSITAP
DIDEKETSF
//
