ID C3ZQ87_BRAFL Unreviewed; 2821 AA.
AC C3ZQ87;
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:EEN45280.1};
GN ORFNames=BRAFLDRAFT_130073 {ECO:0000313|EMBL:EEN45280.1};
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:EEN45280.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN45280.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN45280.1};
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 -!- FUNCTION: Receptor that may have an important role in cell/cell
CC signaling during nervous system formation.
CC {ECO:0000256|ARBA:ARBA00002066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 2 family. LN-TM7
CC subfamily. {ECO:0000256|ARBA:ARBA00010933}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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; GG666660; EEN45280.1; -; Genomic_DNA.
DR RefSeq; XP_002589269.1; XM_002589223.1.
DR STRING; 7739.C3ZQ87; -.
DR eggNOG; KOG4289; Eukaryota.
DR InParanoid; C3ZQ87; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR CDD; cd15441; 7tmB2_CELSR_Adhesion_IV; 1.
DR CDD; cd11304; Cadherin_repeat; 10.
DR CDD; cd00054; EGF_CA; 4.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00110; LamG; 2.
DR Gene3D; 2.60.120.200; -; 2.
DR Gene3D; 2.60.220.50; -; 1.
DR Gene3D; 2.60.40.60; Cadherins; 9.
DR Gene3D; 4.10.1240.10; GPCR, family 2, extracellular hormone receptor domain; 1.
DR Gene3D; 2.10.25.10; Laminin; 5.
DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR046338; GAIN_dom_sf.
DR InterPro; IPR017981; GPCR_2-like_7TM.
DR InterPro; IPR036445; GPCR_2_extracell_dom_sf.
DR InterPro; IPR001879; GPCR_2_extracellular_dom.
DR InterPro; IPR000832; GPCR_2_secretin-like.
DR InterPro; IPR017983; GPCR_2_secretin-like_CS.
DR InterPro; IPR000203; GPS.
DR InterPro; IPR001791; Laminin_G.
DR InterPro; IPR002049; LE_dom.
DR PANTHER; PTHR24026; FAT ATYPICAL CADHERIN-RELATED; 1.
DR PANTHER; PTHR24026:SF51; PROTOCADHERIN-LIKE WING POLARITY PROTEIN STAN; 1.
DR Pfam; PF00002; 7tm_2; 1.
DR Pfam; PF00028; Cadherin; 8.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF01825; GPS; 1.
DR Pfam; PF02793; HRM; 1.
DR Pfam; PF00053; Laminin_EGF; 1.
DR Pfam; PF02210; Laminin_G_2; 2.
DR PRINTS; PR00205; CADHERIN.
DR PRINTS; PR00249; GPCRSECRETIN.
DR SMART; SM00112; CA; 8.
DR SMART; SM00181; EGF; 6.
DR SMART; SM00179; EGF_CA; 4.
DR SMART; SM00180; EGF_Lam; 1.
DR SMART; SM00303; GPS; 1.
DR SMART; SM00008; HormR; 1.
DR SMART; SM00282; LamG; 2.
DR SUPFAM; SSF49313; Cadherin-like; 9.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 3.
DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 2.
DR PROSITE; PS00232; CADHERIN_1; 6.
DR PROSITE; PS50268; CADHERIN_2; 9.
DR PROSITE; PS00022; EGF_1; 4.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01248; EGF_LAM_1; 1.
DR PROSITE; PS50027; EGF_LAM_2; 1.
DR PROSITE; PS00650; G_PROTEIN_RECEP_F2_2; 1.
DR PROSITE; PS50227; G_PROTEIN_RECEP_F2_3; 1.
DR PROSITE; PS50261; G_PROTEIN_RECEP_F2_4; 1.
DR PROSITE; PS50221; GPS; 1.
DR PROSITE; PS50025; LAM_G_DOMAIN; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE-
KW ProRule:PRU00043}; Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW G-protein coupled receptor {ECO:0000256|ARBA:ARBA00023040};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Laminin EGF-like domain {ECO:0000256|ARBA:ARBA00023292,
KW ECO:0000256|PROSITE-ProRule:PRU00460};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transducer {ECO:0000256|ARBA:ARBA00023224};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..2821
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002936725"
FT TRANSMEM 2215..2242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2254..2275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2281..2300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2321..2341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2361..2383
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2403..2424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2430..2453
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..443
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 444..549
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 550..654
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 655..759
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 760..861
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 862..963
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 964..1069
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1070..1171
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1190..1290
FT /note="Cadherin"
FT /evidence="ECO:0000259|PROSITE:PS50268"
FT DOMAIN 1429..1465
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1469..1508
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1509..1716
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1719..1755
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1761..1929
FT /note="Laminin G"
FT /evidence="ECO:0000259|PROSITE:PS50025"
FT DOMAIN 1931..1967
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1968..2005
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 2015..2062
FT /note="Laminin EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50027"
FT DOMAIN 2047..2120
FT /note="G-protein coupled receptors family 2 profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50227"
FT DOMAIN 2217..2454
FT /note="G-protein coupled receptors family 2 profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50261"
FT REGION 2504..2598
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2614..2797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2504..2533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2582..2598
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2633..2650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2679..2695
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2696..2713
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2734..2750
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1455..1464
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1745..1754
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1902..1929
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00122"
FT DISULFID 1957..1966
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 2015..2027
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2017..2034
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
FT DISULFID 2036..2045
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00460"
SQ SEQUENCE 2821 AA; 312110 MW; 6AC8A8CEC7CA3101 CRC64;
MEMPFVWLGG CLYTLLLYFT LSASSELDVP GSSPYTVHLE NSTSVGKAVF DAWLGPGWRY
RWVPGPGTHQ ARRFFSLDPV TGVLSVSREL DCSRLYHNPF TAHIGARTAK IASKHASGRK
SASLLSEPRH EEVFVWTDLD AESPGRTLDS VISRTHEDVD YTSIPVELWI HGENCRFRHR
KNLNQALQSL GVQTVHLHRH ANHHANNAVQ NGAATNLCLS ENQLLFSPAD YVPMNILQSC
QVSYDILNSS LSLGHTGFGI VTNEALCTDE DNPSITVQVM LDLVCDVGSV PMSSQMLLHV
MLGRRVQPDF VPVRTLHHMF KFRRKRSSNS FPSFGPSPAF VVQVPENEDP GYVVTLVTAT
DPDPGEAGRL QYSMVALQNS RSQDLFSIDP ASGEVTTQEV LDREDMNRHF FRVTARDNGS
PPRSATATLQ IDILDMNDHD PEFEENSYRE AVLEGIEIGS NVLTVRATDQ DIGPNSDIRY
SIINPSGTNT AFQISRRDGV ITTTEALDRE TTASYRLEVR ASDQGTPPRT SDVVVTITVL
DENDNEPQFE QQSYAKDVPE NVRPDTVIQT VAATDPDEGT NSQIRYSLIG GNSQGHFTID
SATGDISVIT NLDFESTPRY RLIVKAQDSG RPSMWSSVVL TVSVIDVNDH DPQFVSTPFE
TSVFEDVRVG FSVIHIQAID ADSGSNAELT YSLANVPARM PFEIDGDTGW IVTNAELDRE
AHAIYDFNVQ AADQGSPART AAARVSINIL DVNDNAPVFN PKVYYINVPE DANPGTSVLT
VTANDADEVG TVSYQITGGN VRNRFSITSQ NGLGTISVAL PLDYKQETRF VLTVQATDRM
LSDDAQVYIN ITDANTHRPV FQQSPYSVYV DEDVPIGTTI LVVSATDGDE GENARISYSM
DILNAFEIEP STGAIKTKQR LDHEAQASFA VSVTATDHGV PSKFDESYVD IIVNDVNDNA
PVFLLESYSG SVREDCSRGT SVTQISATDA DSGTNGQIRY TFTGGDNGED AFVIDERSGI
IRTDKRLDRE LIPVYNLVAY AEDQGQPEQK TPVDIIVTIE DVNDNAPQFP SDTIDIYVPE
NRVVGSVVAR ITANDPDEGQ NAEVMYYITK GNNPELFQLD IFSGELVTLI DLDYEARNFY
EITVQARSMP LFSEAIVNIH IQDENDNIPV LQDFEIVFNN YRNHFPTDYI GRIPAFDPDV
SDRLAYSFTF GNNANLLHLN QSTGEIKLSP QLDSDRAFEA QLGVSVTDGI NKVSAQCLLK
VSVVTDEMLS NSITVRLGNM TQELFLSPRY NRFVEGLAAI LQTPQDHIHI FNVRDDVDVS
HKILNVSFSA RDPTQIRTVY YTPQYLRERV YLRRTLLNQL TAATVLPFDD NVCLIEPCPN
YERCVSVLKF DSTAPFVTSD TVLFRAIHPI NGLRCKCPLG FTGSYCETEI NLCYSSPCGG
NGNCMRKEGG YTCVCNEDYA GDNCEINARE GRCTDYVCKN GGVCTNLLVG GFRCNCGMQG
NHVTDFCEVS TRSFPPRSFL TFPALQQRFR MQLSLTFASQ NRNALLLYNG RYNVKHDYLA
LEIVDGQIKF SFSTGQETTV VQPHVPGGVN DGQWHTVTIN YMNKPCSADE PCSNIPYGPS
DRKVATVSID DCDTAIAVKY GSVIGNYSCA AQGVQLSGKK SLDLTGPMIM GGLPSLEEQF
PVKNRDYVGC IKDFYIDNKF VDLASYMSNN GTTAGCPERQ QFCTSNPCRN GGTCENDWDR
FYCSCPTGYG GPTCNRQMRA PKRYSGNSVM DYSVSNLPVI SLPWYNGLMF RTRQANGLMM
RINIGDFNVI NLELVNGFLQ YRFTLETITM TNRRVNDGDW HAVEVRWTDS GELVVDLDYG
GSVNSTTIAD WISQLRIRKV NVGGLKQGAG NNIVVENGFR GCIQGVTLGG ARDQLDPNTA
TSHNVEDNCV VDDLCDSSPC PANSFCNDEW ESYSCQCDIG YVGRGCVSAC ELNPCEHGST
CVAMPSASHG YSCECTDLYQ EHHYQPKDSE VCYPCDCYME GSNSMDCDQE TGQCSCGNGV
IGRRCDSCHN PFAEVTGRSC EVIYDGCPKS YAEGKWWPQT RFGLTSREEC PSGASGIAER
QCSEETGWLP PNMFNCTSRN FIPLKTALEG LRGKLSSEQA QNIAQDLRNA TVDTPDLYGN
DVNISHHNGA GAWTTRGCRL MERNLTHIKC GCDHLSSFAI LMDDSPSEFG LNRPVALMVV
TYVGIGISLV LLVAAFLTFM CLKNLQSNTN TIHKNLVASI FIAELIFLVG VNATHNQLMC
TLVAILLHYS FLTAFAWMFL EALHIYRMLT EIRNINQGHM RFYYSIGWGA PAIIVGLAFG
VKPESYGNRD FCWLQVNDRL FWTLAGPILL VVLINLFVFI FAVRRLLRMA RKDPEHQSLK
SGLMATAILI PMLGTTWVFG VLAVNQDLET FHYMFAILTC MQGLFVFLFH CIFNPSVRQG
WSRCWGRCRG KKGTYEDSVT TRTTLMSRSA LAYNNTSSAD GGLHRINIGT STNSTGSRST
SKTSTSQLWR TDGMLRTGYN PNDYKPNHPM FLDGKVNKGG EEGDSDSDSD MSLNDPDEEL
SLASSHSSDD EEYDGQPNWE KTIKLSEVVM EDAPKSLRPI LKSPKSSRSS RSRSSKSSRE
RRERQMSDEG SESNSDSSAA KELKQILKKP GSRKGIAKSA SGNFYSSSSS SDDSESEYEF
LQKDPKDATQ KHLKPPVHGP LHSTPKDPVP VNRVPREKPP LMPKPKPKWP GEPLSASERE
SLGSLDRLKV EPKVNGDKPS PPVSQHGGSI HGSQPDVVRI QPVPVKWRMG HNLSLSRSLQ
T
//
