ID C3YBD5_BRAFL Unreviewed; 1789 AA.
AC C3YBD5;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN62292.1};
GN ORFNames=BRAFLDRAFT_67521 {ECO:0000313|EMBL:EEN62292.1};
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:EEN62292.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN62292.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN62292.1};
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; GG666497; EEN62292.1; -; Genomic_DNA.
DR RefSeq; XP_002606282.1; XM_002606236.1.
DR eggNOG; KOG1217; Eukaryota.
DR eggNOG; KOG4475; Eukaryota.
DR InParanoid; C3YBD5; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00054; EGF_CA; 3.
DR Gene3D; 2.10.25.10; Laminin; 6.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 3.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
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; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR024731; EGF_dom.
DR InterPro; IPR001212; Somatomedin_B_dom.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR24049; CRUMBS FAMILY MEMBER; 1.
DR PANTHER; PTHR24049:SF22; DROSOPHILA CRUMBS HOMOLOG; 1.
DR Pfam; PF12947; EGF_3; 2.
DR Pfam; PF07645; EGF_CA; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00090; TSP_1; 3.
DR PRINTS; PR01705; TSP1REPEAT.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00181; EGF; 7.
DR SMART; SM00179; EGF_CA; 5.
DR SMART; SM00209; TSP1; 3.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 2.
DR PROSITE; PS50026; EGF_3; 6.
DR PROSITE; PS01187; EGF_CA; 2.
DR PROSITE; PS00524; SMB_1; 1.
DR PROSITE; PS50958; SMB_2; 1.
DR PROSITE; PS50092; TSP1; 3.
PE 4: Predicted;
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1789
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935386"
FT TRANSMEM 459..482
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..548
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..72
FT /note="SMB"
FT /evidence="ECO:0000259|PROSITE:PS50958"
FT DOMAIN 69..109
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 591..631
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1296..1334
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1336..1371
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1374..1413
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1414..1458
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 1660..1782
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 295..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1340..1350
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 1361..1370
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 1789 AA; 193462 MW; 22C7BE17864ACBE1 CRC64;
MLLLPKILAV VVLCLDVQGT AGQFCSLRGC CSGEDDSCST PDGNGGVCYC DHFCLLTGDC
CPDYAAICDE DECATEPSVC HVNATCHNTV GSYECVCKEG FVGNGEHCVD ETLGPCATHT
SINEPRRSSA FVPGPTDALI CDNVLPAGWY RFVTDDSGGK MPETCVEQFH CGTQVPVWLN
GAHPTDYQAV DREGCMNYGV PGDCCTLTVQ IQVQRCPASN GNPDFFVYNL QPTFACDIVY
CADPTPVDNT TTALPTRRIP RQTVGSSRST SEPSVTRTMT IGSATQRTAA MAARTSATPT
DSGGAPVSTL IGHSTTKSTS TKLEENIRTA GESTTPMNLR TRTSTPRTVS RSGSAQSVTR
TATIDNATPS HGTAAVAAKT SATPTDSGGT PINSHNTAKS TSMKPEENGR AAGESTTLIG
RRTWTGAPDE QQPTAPTSRR TATGDGVTDS PGAMSSKGVI IGATCAGLIF VLVTSIIICV
LCRKRKPSQN TEKVTPSGDD AVALGNLRNT DGNVYDVIVD TKGNIMMMQS WWLHVLVLLL
CLVAHQTTAQ EDDSCRAIGG CCTRFGCCGD EDDSCTVDRG DAGICYCDHF YEDECTNGNN
ACHEHATCTN TIGSYECACN AGFVGNGFHC AGWYRFVANT GGRIPETCVD QFHCGTQVPI
WLNGAHPTGY QAVDREGCMN YGVPDDCCTL TVQIQVQRCP APNGNPDFFV YNLQPTFGCS
LAYCADPVPQ ITQNPVLHPP ELNLNELRVT FTCELKHDVD STSARFKVRF LVNGNNYTEI
NSETKEPLTA AQKTIQLDAK YLGEFQPHPG FNDNIGWQSK MGEMVTMPSG NSVKAQLNYW
GMNVYLYAVG SQKYNTEGLC GVWDDNPGND YTKRDGTISN EGDVPTIFRD DWRIPIGRSM
FDLMHLPRDP NPEPLQFCTC SGADNIRCGG RAVNNGLEAQ FEVNPLMGNN DLENKRRRRK
RELPEELDED SPFYTDDVVY EETYVFDYGD GDSTEAPPPD TGITEEEAEN HCRMTIRNST
IANICEDLGI DIFEAIEDCI LDVQITGDFS IARASINDMK ERCVQKVFQN VSLYDVQDDG
QRVPPMVLKA ALCPEDCSGN GMCVDGVCEC DEGYTSVDCS LREDSPPAVT SVQNGGLCDI
RLRPCLKVLI EADGIAESAN LTCRVKQVQP GTCNIRGFCF ADGNPNPDNW CEQCLTDVST
ETFSDRVVNQ PPSFVTMGPI TKLPGETLDI SLEATDPEGR DVTYSITSAN PHGVMLQPSG
QLTWDTDPAP PVTSFPLDVT VTDECGQATT STFTFTLYEC PCQNNGNCAI DPDMPRGQGH
YNCECSGYTG ALCEEEVDEC ASNPCVNGAC NDEVNGFTCT CDAMYMGPLC DIPLEDHCGL
QPCFPGVPCT NVADGFECGD CPDGYNGDGV DCEDINECES NTTCAHVIIN GARVCVNTNG
SYYCTCTAGH VLIIDTCQDV VDGGWTDWSP WSDCSVTCGV GEQTRDRTCT NPAPANGGAD
CDGVTQETQA CDTGLLCPVD GGWTDWGSWS ACSVTCGVGE QTRDRTCTDP EPANGGADCD
GLAQETQACD TGVSCLVIVD GGWTDWGSWS ACSMTCEVGE QTRDRTCTNP APAHGGADCD
GLAQETQACD TGVSCPVLPT RDCSDVYPHL RPAGNFGRYQ NKYCFWSSAW RNRRLNYTKA
QQECESNGGT LAMIKDASVQ AFINNLLKTS SGRTQRNYWI GLDDLNREGV FEWNDGTKLG
SYRRFKSKRP HKIRDCVALW RTAKLSRWFP LKCKIHLPYI CQMGEQKAY
//
