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Database: UniProt
Entry: A0A3B3DV28_ORYME
LinkDB: A0A3B3DV28_ORYME
Original site: A0A3B3DV28_ORYME 
ID   A0A3B3DV28_ORYME        Unreviewed;       686 AA.
AC   A0A3B3DV28;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Complement factor B-like {ECO:0000313|Ensembl:ENSOMEP00000033299.1};
OS   Oryzias melastigma (Marine medaka).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC   Oryzias.
OX   NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000033299.1, ECO:0000313|Proteomes:UP000261560};
RN   [1] {ECO:0000313|Ensembl:ENSOMEP00000033299.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR   AlphaFoldDB; A0A3B3DV28; -.
DR   Ensembl; ENSOMET00000034857.1; ENSOMEP00000033299.1; ENSOMEG00000019236.1.
DR   GeneTree; ENSGT00940000158605; -.
DR   OMA; YDCYSGY; -.
DR   Proteomes; UP000261560; Unplaced.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
DR   GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00033; CCP; 2.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.10.70.10; Complement Module, domain 1; 2.
DR   Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR011360; Compl_C2_B.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR   InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR46393:SF6; COMPLEMENT COMPONENT BFB-RELATED; 1.
DR   PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00084; Sushi; 2.
DR   Pfam; PF00089; Trypsin; 2.
DR   Pfam; PF00092; VWA; 1.
DR   PIRSF; PIRSF001154; Compl_C2_B; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   SMART; SM00032; CCP; 2.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
DR   PROSITE; PS50923; SUSHI; 2.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS50234; VWFA; 1.
PE   4: Predicted;
KW   Complement pathway {ECO:0000256|ARBA:ARBA00022875};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Immunity {ECO:0000256|ARBA:ARBA00022859};
KW   Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW   Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW   ProRule:PRU00302}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..686
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5017368794"
FT   DOMAIN          19..78
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          82..139
FT                   /note="Sushi"
FT                   /evidence="ECO:0000259|PROSITE:PS50923"
FT   DOMAIN          185..384
FT                   /note="VWFA"
FT                   /evidence="ECO:0000259|PROSITE:PS50234"
FT   DOMAIN          402..672
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        444
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT   ACT_SITE        496
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT   ACT_SITE        615
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT   DISULFID        49..76
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT   DISULFID        110..137
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ   SEQUENCE   686 AA;  76388 MW;  72509607D4B6550E CRC64;
     MCFCVCNICY SSLFCAADVE CPDPNVLENG NVSPPLERYL AGNTTTFECY SGYTLRGSES
     RTCLPNGKWS GSTTICSRDS GETCPDPGVP PGASRRGNTF DVGYDVSYSC NGNLFLVGSK
     VRVCQENGHW SGREPACYSK FTYDTSQEVS EAFGSSIRET LTTLQSTNDT QAGRKIRISK
     NGTLNIYIAL DISESIEEKH FKKAKEAIIT LIKKISTFTV TPNYEIIFFS SEVFEVANIV
     DFYSGTENLI SVIKKLEAFK IGDKSTGTDV NAALKTFEDR MAWIEEREKE NFRKHRHVFL
     LFTDGAYNMG GSPLPTLARI KSRVYMSPTG DPGSRLEYLE SYVFGIGAVI FDDDLQPLTA
     GTEEEKHYFR LEKETNLAAT FDSIIDENEV IGLCGLHRTY DLLGNKASIK AMYPWVVFIN
     IQGESPKKCL GSLVSPEFVL TAAHCFIFSD EPKNVQVEIE DGHGSKNKKV KTFKLHPQYN
     VTARKNQGVE EFYDYDVALI QLEKPVNISH SARPICIPCT KQTKDALRLP PSSTCKDQEE
     LLLKNQQERL SFLTRLEPLV GEKDVYAKLG DSRDLCIKKA LEAKGIKAKD PKIPVTDNFL
     CTGGEREHIA CTGDSGGAVF KNYEDRTIQI ALVSWGTQEL CTGGGMIEST EKSRDFHINL
     FKMIPFLKEI MGNDDSDDFA SIGFID
//
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