ID C3Y9D4_BRAFL Unreviewed; 550 AA.
AC C3Y9D4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:EEN63190.1};
GN ORFNames=BRAFLDRAFT_68025 {ECO:0000313|EMBL:EEN63190.1};
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:EEN63190.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN63190.1};
RC TISSUE=Testes {ECO:0000313|EMBL:EEN63190.1};
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 -!- SIMILARITY: Belongs to the WFIKKN family.
CC {ECO:0000256|ARBA:ARBA00005743}.
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DR EMBL; GG666492; EEN63190.1; -; Genomic_DNA.
DR RefSeq; XP_002607180.1; XM_002607134.1.
DR AlphaFoldDB; C3Y9D4; -.
DR STRING; 7739.C3Y9D4; -.
DR eggNOG; KOG4597; Eukaryota.
DR InParanoid; C3Y9D4; -.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0048019; F:receptor antagonist activity; IBA:GO_Central.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0050431; F:transforming growth factor beta binding; IBA:GO_Central.
DR GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IBA:GO_Central.
DR CDD; cd00104; KAZAL_FS; 1.
DR CDD; cd00109; Kunitz-type; 2.
DR Gene3D; 2.40.50.120; -; 1.
DR Gene3D; 3.30.60.30; -; 1.
DR Gene3D; 4.10.75.10; Elafin-like; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 2.
DR InterPro; IPR036645; Elafin-like_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR002350; Kazal_dom.
DR InterPro; IPR036058; Kazal_dom_sf.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR001134; Netrin_domain.
DR InterPro; IPR018933; Netrin_module_non-TIMP.
DR InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR InterPro; IPR008993; TIMP-like_OB-fold.
DR InterPro; IPR008197; WAP_dom.
DR PANTHER; PTHR45938; ACP24A4-RELATED; 1.
DR PANTHER; PTHR45938:SF11; PAPILIN; 1.
DR Pfam; PF13927; Ig_3; 1.
DR Pfam; PF07648; Kazal_2; 1.
DR Pfam; PF00014; Kunitz_BPTI; 2.
DR Pfam; PF01759; NTR; 1.
DR Pfam; PF00095; WAP; 1.
DR PRINTS; PR00759; BASICPTASE.
DR SMART; SM00643; C345C; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00280; KAZAL; 1.
DR SMART; SM00131; KU; 2.
DR SMART; SM00217; WAP; 1.
DR SUPFAM; SSF57362; BPTI-like; 2.
DR SUPFAM; SSF57256; Elafin-like; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
DR SUPFAM; SSF100895; Kazal-type serine protease inhibitors; 1.
DR SUPFAM; SSF50242; TIMP-like; 1.
DR PROSITE; PS00280; BPTI_KUNITZ_1; 2.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51465; KAZAL_2; 1.
DR PROSITE; PS50189; NTR; 1.
DR PROSITE; PS51390; WAP; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Immunoglobulin domain {ECO:0000256|ARBA:ARBA00023319};
KW Metalloenzyme inhibitor {ECO:0000256|ARBA:ARBA00023215};
KW Metalloprotease inhibitor {ECO:0000256|ARBA:ARBA00022608};
KW Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..550
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002934897"
FT DOMAIN 26..74
FT /note="WAP"
FT /evidence="ECO:0000259|PROSITE:PS51390"
FT DOMAIN 110..163
FT /note="Kazal-like"
FT /evidence="ECO:0000259|PROSITE:PS51465"
FT DOMAIN 192..283
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 305..355
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 363..413
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 413..546
FT /note="NTR"
FT /evidence="ECO:0000259|PROSITE:PS50189"
SQ SEQUENCE 550 AA; 60703 MW; 3CA556C58B9C68EE CRC64;
MAARIALLGS FLVRACLAVT VPPTGSTLHL GVCPRFYVDS LSTCNNRCLT DDDCREQEKC
CNNACGDRSC VTAAEETVPT TMTTTTMEDS LAGTCRGYDC MQQGAVCTVV DGRPKCMCES
LCPVDKEPSF VCASDGMTYF NECYMNATAC ELGKAINVVP CKAVIRNTGA PTSTWTHEVP
SIVPSQPATS APIIISEPII HMVREDDNIT LECQVSGVPT PRVFWQKQGD TNILIGPGNS
FHHFEVSEIG ALTISYIQME DQGNYTCVAV NVAGDTSVEF PVEVIPTSTP EPSTDGSTFS
PEDVCSLPKD EGSCEDSVPK WYYNQERQVC ERFVYSGCGG NDNRFDSIHE CIMACPDVTA
ATCRLQAAAG PCKRYRTRWY YDISKGVCSW FIYGGCQGND NNFVTMDSCN DACPYHVANA
CHKCPNRYGM VEYYCMSDFA IVGTVLEIID YNTDERPKAV IMLEDVYKDN MGMFESAESA
FALEISLNFT MRQPCPCPEL KVEEKYIIMG TVQDGYPMVE KDSFVKTLSE KRKQRLMHTS
RSTNVCENLK
//
