ID A0A3Q3M4K4_9LABR Unreviewed; 771 AA.
AC A0A3Q3M4K4;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Complement C2-like {ECO:0000313|Ensembl:ENSLBEP00000015470.1};
OS Labrus bergylta (ballan wrasse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Labriformes; Labridae; Labrus.
OX NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000015470.1, ECO:0000313|Proteomes:UP000261660};
RN [1] {ECO:0000313|Ensembl:ENSLBEP00000015470.1}
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; A0A3Q3M4K4; -.
DR STRING; 56723.ENSLBEP00000015470; -.
DR Ensembl; ENSLBET00000016393.1; ENSLBEP00000015470.1; ENSLBEG00000012005.1.
DR GeneTree; ENSGT00940000165141; -.
DR InParanoid; A0A3Q3M4K4; -.
DR Proteomes; UP000261660; 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; 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; 3.
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:UP000261660};
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..771
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018664050"
FT DOMAIN 104..163
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 168..225
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 275..473
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 504..761
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 162..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 527
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 578
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR001154-1"
FT ACT_SITE 697
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 196..223
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 771 AA; 86155 MW; 824777CB9D12D997 CRC64;
MYVKPVLWIL LLVSVQEVFL QESEYDYGTY EDLQPLNCST TESIKGGHVT YSQGGMEGSV
LSYHCGLGRY PSPVSYRTCS ADGEWSSMRL PSGREVSRAT CKDVLCPAQL QLDHGDFWPR
DQWLHVGATQ SFFCQEGFIL SGSAQRNCTL TGEWTGTTPV CENDDSSDDC KDPGIPPGAQ
RSPGRFYTGQ KVTYWCQAGM DLLGSAERVC LENREWSGST PRCQAPNTFD SPSVVAAVMA
GSLAGKMDVL SPDAKQESDS SFGRTFRVAE GSRMNVFILL DTSGSITKED FEKSREATIA
LIRKLESYEV QLKFHVVSFA SVAIDIVNIT DSDISSSVGD VIWNLMDIYE KITISTNLHA
ALKRVSEMVA FLKQNSATNH FNETQNIIVI ETDGFTNTGS KPQLELARLR SLLGYHNIAP
DHTQETMLDV YVFGIGDRVK RDQLNSLASK KRGEEHVFVL KDYETLGAVF NSIISDKSVT
MCGVAQEHIS KKQKEDVKGI FTKPWHVSST PCVGSIVSSN WVLTAAHCFA RASTDSIRQQ
VFIQHSEGAV VPKKVIMHPK YNTRALRHRN VSEFYDYDVA LVQVNMSIPL SWKARPICLP
CTVPASRAMK RVNSTCQQHR EELLPDKETA AFFIHKNSLR KGTYIQTGSQ RPGCVEKAKQ
TLKEPTNVTL EEYVPDRFLC SGGSSGYHYT ISCKGDSGGS LFLEKRKRYF QVGVVSWGTT
DVCNNLNPAL RHYRSDKPPP DARDFHIDLF KIMPWLKRHL KDEIQFLPDI E
//
