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Database: UniProt
Entry: C3Y020_BRAFL
LinkDB: C3Y020_BRAFL
Original site: C3Y020_BRAFL 
ID   C3Y020_BRAFL            Unreviewed;       361 AA.
AC   C3Y020;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 77.
DE   SubName: Full=Trypsin-3-like isoform X1 {ECO:0000313|RefSeq:XP_035669810.1};
GN   Name=LOC118411560 {ECO:0000313|RefSeq:XP_035669810.1};
GN   ORFNames=BRAFLDRAFT_277744 {ECO:0000313|EMBL:EEN66386.1};
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:EEN66386.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN66386.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN66386.1};
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).
RN   [2] {ECO:0000313|RefSeq:XP_035669810.1}
RP   IDENTIFICATION.
RC   STRAIN=S238N-H82 {ECO:0000313|RefSeq:XP_035669810.1};
RC   TISSUE=Testes {ECO:0000313|RefSeq:XP_035669810.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR   EMBL; GG666477; EEN66386.1; -; Genomic_DNA.
DR   RefSeq; XP_002610376.1; XM_002610330.1.
DR   RefSeq; XP_035669810.1; XM_035813917.1.
DR   STRING; 7739.C3Y020; -.
DR   MEROPS; S01.079; -.
DR   KEGG; bfo:118411560; -.
DR   eggNOG; KOG3627; Eukaryota.
DR   InParanoid; C3Y020; -.
DR   OMA; SINQAGC; -.
DR   OrthoDB; 2996498at2759; -.
DR   Proteomes; UP000001554; Chromosome 3.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00112; LDLa; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR   InterPro; IPR036055; LDL_receptor-like_sf.
DR   InterPro; IPR023415; LDLR_class-A_CS.
DR   InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR   PANTHER; PTHR24252:SF13; TRANSMEMBRANE SERINE PROTEASE 12; 1.
DR   Pfam; PF00057; Ldl_recept_a; 2.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00192; LDLa; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF57424; LDL receptor-like module; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS01209; LDLRA_1; 2.
DR   PROSITE; PS50068; LDLRA_2; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00124}; Hydrolase {ECO:0000256|RuleBase:RU363034};
KW   Protease {ECO:0000256|RuleBase:RU363034};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001554};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           17..361
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5041116425"
FT   DOMAIN          130..359
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   DISULFID        21..33
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        28..46
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        40..55
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        82..97
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   361 AA;  38203 MW;  9FB21431AB83D9DA CRC64;
     MIWCLLLLAL AARGDAWLFS CSASDFQCSN GNCIPGSWEC DGEADCSDGS DEASCSGGGT
     CQQGVHFFCA NGLYCIDSNW VCDGDNDCGD MSDEQNCGGG STGTTGTTAP ITSFTGDCGQ
     PAISPQNVRV VGGVQAVQGS WPWQASLKLY GGHVCGGQII APNWIVTAAH CVDGQSNPSQ
     WRVSLGSHRR TSTDSTQQDF SVTRIIMHES YDSNRINNDV ALMKLSGNAQ FNNYVSPICL
     PTQDVAAGTN CVTTGWGDTG SGASTYLMQA TVPIMEWNKC NSAQYMNGAI TDKMICAGYD
     QGGKDACQGD SGGPLVCNYS GKWTLDGIVS WGYGCAQAYK PGIYTRVTQF VSWINNKMAS
     N
//
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