ID C3YDL6_BRAFL Unreviewed; 1769 AA.
AC C3YDL6;
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:EEN61485.1};
GN ORFNames=BRAFLDRAFT_92892 {ECO:0000313|EMBL:EEN61485.1};
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:EEN61485.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN61485.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN61485.1};
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: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; GG666504; EEN61485.1; -; Genomic_DNA.
DR RefSeq; XP_002605475.1; XM_002605429.1.
DR eggNOG; KOG4297; Eukaryota.
DR InParanoid; C3YDL6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR CDD; cd10909; ChtBD1_GH18_2; 1.
DR CDD; cd00037; CLECT; 2.
DR CDD; cd00108; KR; 3.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 5.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 3.
DR Gene3D; 3.10.250.10; SRCR-like domain; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR018378; C-type_lectin_CS.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR006585; FTP1.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR PANTHER; PTHR45713:SF6; F5_8 TYPE C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR45713; FTP DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00051; Kringle; 3.
DR Pfam; PF00059; Lectin_C; 2.
DR Pfam; PF00530; SRCR; 1.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00034; CLECT; 2.
DR SMART; SM00607; FTP; 5.
DR SMART; SM00130; KR; 3.
DR SMART; SM00202; SR; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 5.
DR SUPFAM; SSF57440; Kringle-like; 3.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 2.
DR PROSITE; PS00021; KRINGLE_1; 3.
DR PROSITE; PS50070; KRINGLE_2; 3.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS00420; SRCR_1; 1.
DR PROSITE; PS50287; SRCR_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1769
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935536"
FT DOMAIN 276..354
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 356..434
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 623..701
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 1192..1270
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 1316..1416
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 1488..1605
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 1617..1765
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT REGION 1303..1324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1699..1718
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1303..1319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 277..354
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 298..337
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 326..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 357..434
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 378..417
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 406..429
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1193..1270
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1214..1253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1242..1265
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 1341..1405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1354..1415
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
FT DISULFID 1385..1395
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1769 AA; 192714 MW; BEF347E7050DE1D0 CRC64;
MGVQNRYQTA LILLLFYVLW LGRGDSAITV QQAEHLKSRI ERLKSKVDAV NLKMAQTAGT
LNNMAETGLP EMPEFNIAEG KTAFQTSTQA YHTPATGQQY PGDARLAVDG NTNGIHWENS
CIHTKGEANP AWWVDLGQSY MIKRVEIYNR MDCCSERLNP FNIHIGSSST VTSNPKCGGD
HQVDLSQPSI SVSCQGMTGR YVGVRLPGSR TLTLCEVQVF STSGRIERLK AKVDAVSLNV
ARAAGTLNNM ADTGLPKPLV VPALLPTSST TPAPGPCQVG DGASYRGTVS VTQTGKTCQR
WDSQTPHWSY NTPENHPSSG LVENYCRNPD GDLRVWCYTT DPDERWDYCD VPVCKSCQVG
DGASYRGTVS VTQTGKTCQR WDSQTPHWSY NTPENHPSSG LVENYCRNPD GDLGVWCYTT
DPDERWDYCD VPVCGRIERL KSKVDAVNLK MAQTAGTLNN MAETGLPEMP EFNIAEGKTA
FQTSTQGYHT PATGQQYPGD ARLAVDGNTN GIHWENSCIH TKGEANPAWW VDLGQSYMIK
RVEIYNRMDC CSERLNPFNI HIGSSSTVTS NPKCGGDHQI DVNQPSISVS CQGMTGRYVG
VRLPGSRTLT LCEVQVFSTS ETCGLSTFIH VPQSDCAGSR IDIAAHGGVT LQFCADACCA
DPTCLSFQHN AQSTCYLKNK LCSAGEKGYA GGGNMYDRQD VAVQSAPAPA PTPAPGVNVA
QGKTAFQTST SGYWIPVTGE VFSGEAHLAV DGNTNGDHGA NSCTHTNGEG NDAWWVDLGR
SYVINSVVIF NRMDCCSERL NPFNIHIGDS DQVIANPKCG GDHQIDLSQP SISVSCQGMT
GRGDSAITKQ QALHLKSRIE NLKARIDAVN LKVAQTAGTL NNMAETGLPK IPEVPEVNIA
EGKTAFQTST QASHWPPTGE FSGEPRHAVN GITNGWQGIG NSCTNTKDEA NPAWWVDLGQ
SYMIKRVEIY KRLDCCPGRL NPFNLHIGDS NQVTSNPKCG GDLQIDLSQP SISVSCQGMT
GRYVGVRLLG PSRSMMLCEV QVFPNSEVNV AQGKTAFQTS IQAYHTTTGK QFSGEPHHSV
NGITTGTGDC SWTKSEANPA WWVDLGQSYV INRVVIYYIS CCKDRLNPFN IHIGDSNQIS
TNPKCGGDHH ISERFISVSC QGMTGRYVGV RLPGSSRTLH LCEVQVFSNS GDCQVGNGMS
YRGTVAVTGT GRTCQRWDSQ TPQGHRWTPA DHPSFGLEQN YCRNPDSDSG VWCYTTDPDK
RWDFCDVPFC DVAVQSAPIS SNTPATTQAT TPATTSATIP ATTQATTPAT TSAPGIRLMG
GSSSSEGRVE VYHDGQWGTV CDDFFDMNDA NVICRQLGYG GAVATRPEAA FGAGSDPIWL
DDLNCGGSET SIEDCTHNGW GSHNCGHHED AGVVCSGGGL QKWRDDGRCG AAFPAPGANP
GQCNPLSKAH CCSRYTWCGD SRLHCECHGC VDYRKISGSL NTIGYTERAG SFYKVFRTRR
DYTRAQQTCE ADGGHLAVVN NEAINNFIIE LISEPANFWI GLNDKDTEGT WMWADGTRLV
GCAFTNWAPY EPNNNGGQNC VHMWWEYDYK WDDDFCDYQK YFICQIDGVC QSGWTEHNSH
CYRLGDGPAD WDTADKMCKE AGANLASVEN DAENNAILSV VGAINTEFPV VWVGLQDVNK
GGALTWTDGS PVSYTNWAPH EPESTRTRRS TSWSDVGSSG LRDPGNCIAV YHRDAYAYHP
TAGGQKRKGQ WKDDFCHHKY LYICERSQL
//
