ID H2T8C1_TAKRU Unreviewed; 776 AA.
AC H2T8C1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Complement factor B-like {ECO:0000313|Ensembl:ENSTRUP00000020911.3};
GN Name=LOC101064033 {ECO:0000313|Ensembl:ENSTRUP00000020911.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000020911.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000020911.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000020911.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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; H2T8C1; -.
DR STRING; 31033.ENSTRUP00000063268; -.
DR MEROPS; S01.B91; -.
DR Ensembl; ENSTRUT00000020998.3; ENSTRUP00000020911.3; ENSTRUG00000008352.3.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000165141; -.
DR OrthoDB; 3594820at2759; -.
DR TreeFam; TF330194; -.
DR Proteomes; UP000005226; Chromosome 11.
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; 3.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
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:SF8; COMPLEMENT C2; 1.
DR PANTHER; PTHR46393; SUSHI DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00084; Sushi; 2.
DR Pfam; PF00089; Trypsin; 1.
DR Pfam; PF00092; VWA; 1.
DR PIRSF; PIRSF001154; Compl_C2_B; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SMART; SM00327; VWA; 1.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
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 Reference proteome {ECO:0000313|Proteomes:UP000005226};
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..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..776
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5030172340"
FT DOMAIN 106..165
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 168..225
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 276..477
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 477..766
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 532
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 583
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 704
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT DISULFID 136..163
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 196..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 776 AA; 85976 MW; 3D970E81EE516B17 CRC64;
MHAKSILWIV LCVSAGGGSQ LDYGYDGEEY EDWTQGPVNC STTEAVKGGQ VTYSQGGLEG
SVLSYHCSPG QYPHPLSYRL CGPDGDWSPM RSASGRLVSH ATCRDILCPA QLQLDHGDIW
PRNQWFRVGA TQSFSCQEGF TLYGSAQRNC TLTGGWTGLT PICDNHAEDC SDPGIPPGAQ
RSAGPFQVGQ KFSYSCQTGL DLLGSAERVC LENREWSGSM PRCLGRNTYD SPSDVAKAMT
GSLAGLMDVL SPEEKKTIAE KSFARTFNVA KGSRMNVYIL LDTSGSIQRK DFEKSRNATI
ALIEKLDSYE VKLKFHVLSF ASEAKDIVDI TESEISGSTD DVIWNLRNFN YHSHGEKTGT
NLYAALQRVN EVMSYFKENS AQYHFNETQN VIVIATDGFS NTGKDPQIAL LKIRNLLGYH
SMSSEQKDET LLDVYAFGIG EQVNKEQLNA LASQKSGETH VFFLKDYETL GEVFNSIISD
KSVTMCGVAQ EVTPEDGVKA YTNPWHVTVV TGTSLSCFGS ILSQNWVLTA AHCFARASTD
RVSQQVQIEH GDGMAVSKAV VLHPQFNIRA LKHRNVSEFY DYDVALIQVN ESIPLSWKAR
PICLPCTVPA SRAMKSVNTN CQQHRKALLP HQQTEASFIN SHRNPKRRVT HIQTQAQRQS
CVEKARQVIH EPTDVRLDEY VTDRFLCSGG SSGYKDAVSC KGDSGGSLFL QQKNRYFQVG
VLSWGITNVC DPANRGKYSS EDPPPNARDF HIDLFQIMPW LKQHLGEEIQ FLPDVD
//
