ID C3Y9G0_BRAFL Unreviewed; 901 AA.
AC C3Y9G0;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN63216.1};
GN ORFNames=BRAFLDRAFT_67996 {ECO:0000313|EMBL:EEN63216.1};
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:EEN63216.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN63216.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN63216.1};
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; GG666492; EEN63216.1; -; Genomic_DNA.
DR RefSeq; XP_002607206.1; XM_002607160.1.
DR AlphaFoldDB; C3Y9G0; -.
DR STRING; 7739.C3Y9G0; -.
DR eggNOG; KOG1217; Eukaryota.
DR InParanoid; C3Y9G0; -.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR CDD; cd00037; CLECT; 2.
DR CDD; cd00054; EGF_CA; 5.
DR Gene3D; 2.10.25.10; Laminin; 8.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
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; IPR013032; EGF-like_CS.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR003645; Fol_N.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR PANTHER; PTHR24033; EGF-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24033:SF151; PROTEIN EYES SHUT; 1.
DR Pfam; PF00008; EGF; 3.
DR Pfam; PF12661; hEGF; 3.
DR PRINTS; PR00010; EGFBLOOD.
DR SMART; SM00181; EGF; 8.
DR SMART; SM00179; EGF_CA; 6.
DR SMART; SM00274; FOLN; 3.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF57196; EGF/Laminin; 4.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR PROSITE; PS00010; ASX_HYDROXYL; 6.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 8.
DR PROSITE; PS01186; EGF_2; 6.
DR PROSITE; PS50026; EGF_3; 8.
DR PROSITE; PS01187; EGF_CA; 4.
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}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 97..132
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 134..169
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 171..207
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 388..426
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 428..464
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 622..658
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 662..763
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 735..773
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 775..811
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DISULFID 101..111
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 122..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 138..148
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 159..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 197..206
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 397..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 416..425
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 454..463
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 648..657
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 744..761
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 763..772
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
FT DISULFID 801..810
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 901 AA; 98944 MW; B44E0BA1F8AE7457 CRC64;
MRYPCHYSGA DGCPDDYWAS DCITFHHDAT CRTHQALFVE LCGHMAGYGS HCQPLDDTFV
YWPGPNGDCA WGVTYGEIHH GYGLNGFNYN NKYALCTVTT CARSPCAHGT CTDDGGNYTC
SCENGWTGHD CDQDIDECSS SPCSQGSCTD DVGSYTCKCE IGWAGHDCHQ DIDECASSPC
WLGGTCLDHV NSYSCVCPKD TTGKNCEAVP FAGDCYQFST TGATHLDATR ACSTKNSHLA
DMKDEQQQQF LASTIAFTTG VSNWLAMKTA PIPMFYSDGT PVICTYIMCH PDTLDQFSSV
HPSGDTMKFF HTTLSRMTDR RSPYTLDTMN KTERNTKMYY SHEEPPLQWL TDEPSTPLDL
CVLLDSSNSY KAKATFCTEQ HNYVCQDALK PCEPNVCQNG GNCTSCFGSS TTFCDCLEGY
GGKLCEINID ECASGPCQNG GSCYDDINSY TCQCPVGYQG DHCETDPDWC SQVTCPFGFV
CQDFTFYFQC VREQVYLTTV DNWSFWKIRA TGSMTDDNVK VTCEAAGMRY PCFRPGADGC
GEFYWASDCI KFHHIQCTTL KALSSELCGH TDGHGEQCQP LDDTFVYNPA WYDDSAYGVD
FETHDWGLQG ADYNNMYALC ADIDECASSP CWLGGTCLDH VNGYSCVCLK DVTGRNCETA
SFVGDCYQFS TSAFNHRDAT QACSTNDGRM VDVKDRQQQQ FLANSIAATT GVSNWLAMKT
APFPVFYSDG SPVTAQKPCE PNVCQNGGNC SSCFGGSTTF CDCLEGFGGK LCEINIDECA
SGPCQNGGSC HDDINSYHCI CPTGYQGDNC ESDTDWCSQV QCPFGFVCQD FTFYFQCVHT
DWCSQVQCPF GFVCQDFTLY FQCVHPSPVA RGLPYQCSST SCPDGMNCTP EGAAAFSCKP
E
//
