ID A0A3P9NPC1_POERE Unreviewed; 810 AA.
AC A0A3P9NPC1;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Complement C2-like {ECO:0000313|Ensembl:ENSPREP00000011420.1};
OS Poecilia reticulata (Guppy) (Acanthophacelus reticulatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Cyprinodontiformes; Poeciliidae; Poeciliinae;
OC Poecilia.
OX NCBI_TaxID=8081 {ECO:0000313|Ensembl:ENSPREP00000011420.1, ECO:0000313|Proteomes:UP000242638};
RN [1] {ECO:0000313|Proteomes:UP000242638}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Guanapo {ECO:0000313|Proteomes:UP000242638};
RA Kuenstner A., Dreyer C.;
RT "The genomic landscape of the Guanapo guppy.";
RL Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPREP00000011420.1}
RP IDENTIFICATION.
RC STRAIN=Guanapo {ECO:0000313|Ensembl:ENSPREP00000011420.1};
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; A0A3P9NPC1; -.
DR STRING; 8081.ENSPREP00000011420; -.
DR Ensembl; ENSPRET00000011548.1; ENSPREP00000011420.1; ENSPREG00000007788.1.
DR GeneTree; ENSGT00940000165141; -.
DR OMA; PRSILWI; -.
DR Proteomes; UP000242638; Unassembled WGS sequence.
DR Bgee; ENSPREG00000007788; Expressed in caudal fin and 1 other cell type or tissue.
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 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; 3.
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:UP000242638};
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..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..810
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018299268"
FT DOMAIN 36..103
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 104..163
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 169..226
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 277..478
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 499..737
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 541
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 592
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 711
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT DISULFID 134..161
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
FT DISULFID 197..224
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 810 AA; 89805 MW; 175D3BDF0CD9BD02 CRC64;
MSVKSALWIL VSILVLEVAA QDFDYYSETY DDQGPLNCST TETIKGGSVT YSEGGMEGSV
MTYHCDPGKF PHPVSDRICG ADGEWSPMRL PSGRLVSRPT CKDMMCPGQL QLDNGDFWPR
DQWFPVGMTQ SFSCHSGFSL HGSEQRNCTL SGEWTGTTPI CRNHVFAASE CTDPGIPPGA
KRSGDRFQIE DKVTYRCQAG MHLLGSAERV CLENEEWSGS SPRCQAPQTF DTPSSVAEAM
AGSLAGVMDV LSPDSKKKNV SRTFGRSFLV GEVSRMNIYI LLDTSGSIKK EKFELARNAT
IALIRKLDSY DVQLNFHVLS FASETKVIVS IHETDISGDS EEVIDLMTHF NYNSHGRKTG
TNLYSALENV VNTISFLNEN RNKNHFNETQ NIIIIETDGY SNTGKKPEAA LVRIRSLLGY
STTQHDQTHE KLLDVYVFGV GDQVNKDELN SLASKKSGER HFFVLKDFSL LGEVFNSIIS
DKSVTMCGIA QEDITENQML DGLKAYTRPW HVIVSSNEWP PDKLHCTGSI VSQTWVLTAA
HCFGKVSTSR VPSQLKIQYG GGEVDGIRVI THPEFNTLKL KGRNVSEFYD YDVALVETKQ
KIPLSWEARP ICLPCTVAAS RAMKKINSTC EQHREQLLSL TATPAFFIHK AKERKQTYIH
LKNQRPSCVE KARLTLTQPT NVSLDEYVTE NFLCSGGTER YQDGISCRGD SGGSLYLQKR
KRFFQVGVLS WGTINVCEIP KVIPHSHHGF PVDTRAAGDK HLKRGTGDQS LLDAEGICDE
NLGPTCTGSC SVVKHTAEAG TIRPVNHKLY
//
