ID C3YI01_BRAFL Unreviewed; 529 AA.
AC C3YI01;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 03-MAY-2023, entry version 75.
DE RecName: Full=Kringle domain-containing protein {ECO:0000259|PROSITE:PS50070};
GN ORFNames=BRAFLDRAFT_71581 {ECO:0000313|EMBL:EEN60138.1};
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:EEN60138.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN60138.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN60138.1};
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).
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DR EMBL; GG666514; EEN60138.1; -; Genomic_DNA.
DR RefSeq; XP_002604127.1; XM_002604081.1.
DR AlphaFoldDB; C3YI01; -.
DR eggNOG; KOG0619; Eukaryota.
DR InParanoid; C3YI01; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR CDD; cd00108; KR; 2.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 2.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR PANTHER; PTHR24261:SF7; KRINGLE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR24261; PLASMINOGEN-RELATED; 1.
DR Pfam; PF00051; Kringle; 2.
DR Pfam; PF13855; LRR_8; 2.
DR PRINTS; PR00018; KRINGLE.
DR SMART; SM00130; KR; 2.
DR SMART; SM00364; LRR_BAC; 3.
DR SMART; SM00369; LRR_TYP; 5.
DR SUPFAM; SSF57440; Kringle-like; 2.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS00021; KRINGLE_1; 2.
DR PROSITE; PS50070; KRINGLE_2; 2.
DR PROSITE; PS51450; LRR; 3.
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}; Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..529
FT /note="Kringle domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002935636"
FT TRANSMEM 328..350
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 369..447
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 449..527
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT REGION 389..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 481..497
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 370..447
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 391..430
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 419..442
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 450..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 471..510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
FT DISULFID 499..522
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00121"
SQ SEQUENCE 529 AA; 58349 MW; 9B65454808517449 CRC64;
MAVCTLLTHT LALIVSKELF LSHTASASDR LCPPGWPKRC ECSESTGIVR CNKAGLTTIP
ASIPPYATSL TITGNSIPVI SGPMNSSSLL NLNLANNKIQ VIENSSFDLL PFLRKLNLDR
NPIKFVSRNG RGFIYSLGSL RELSMIGCGL GDGTSAKGNR SNVQSLVYTL AKSQLGSLKK
LNLASNRLSS LPALLLDALP SLEALHLRNN TISEIPQNLF LKTPELRVID LSFNRIRTVA
VETTEQFDKL ASRHSIKVNL TSNPFYCDCA LVGFISWMHQ TRNVTIVKNV TYKCTASQSG
PLSGRSIMNL IPKYLGCSST SRGTGLRLPY AGLVVIIVVL SLLFVTVMYL NRRGIARHCT
ELQNARKESC QTDRGKAYRG TVSVTNTGKT CQRWDSQTPH EHSRTPANNP SSGLEENYCR
NPDNEPGVWC YTTDPNSRWE PCDVPYCESC QTDRGKAYRG TVSVTNTGKT CQRWDSQTPH
EHSRTPANNP SSGLEENYCR NPDNEPGVWC YTTDPNSRWE PCDVPFCGI
//
