LFC_CARRO
ID LFC_CARRO Reviewed; 1019 AA.
AC Q26422;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Limulus clotting factor C;
DE Short=FC;
DE EC=3.4.21.84;
DE Contains:
DE RecName: Full=Limulus clotting factor C heavy chain;
DE Contains:
DE RecName: Full=Limulus clotting factor C light chain;
DE Contains:
DE RecName: Full=Limulus clotting factor C chain A;
DE Contains:
DE RecName: Full=Limulus clotting factor C chain B;
DE Flags: Precursor;
OS Carcinoscorpius rotundicauda (Mangrove horseshoe crab) (Limulus
OS rotundicauda).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC Xiphosura; Limulidae; Carcinoscorpius.
OX NCBI_TaxID=6848;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7538401;
RA Ding J.L., Navas M.A. III, Ho B.;
RT "Molecular cloning and sequence analysis of factor C cDNA from the
RT Singapore horseshoe crab, Carcinoscorpius rotundicauda.";
RL Mol. Mar. Biol. Biotechnol. 4:90-103(1995).
CC -!- FUNCTION: This enzyme is closely associated with an endotoxin-sensitive
CC hemolymph coagulation system which may play important roles in both
CC hemostasis and host defense mechanisms. Its active form catalyzes the
CC activation of factor B.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125
CC bonds in Limulus clotting factor B to form activated factor B.
CC Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.;
CC EC=3.4.21.84;
CC -!- ACTIVITY REGULATION: Activated by Gram-negative bacterial
CC lipopolysaccharides and chymotrypsin. {ECO:0000250}.
CC -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a
CC disulfide bond. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.
CC -!- SIMILARITY: Belongs to the peptidase S1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00274}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; S77063; AAB34361.1; -; mRNA.
DR AlphaFoldDB; Q26422; -.
DR SMR; Q26422; -.
DR MEROPS; S01.219; -.
DR BRENDA; 3.4.21.84; 6973.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0042381; P:hemolymph coagulation; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00033; CCP; 5.
DR CDD; cd00055; EGF_Lam; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.170.130.20; -; 1.
DR Gene3D; 2.40.10.10; -; 1.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR004043; LCCL.
DR InterPro; IPR036609; LCCL_sf.
DR InterPro; IPR002049; LE_dom.
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; IPR033116; TRYPSIN_SER.
DR Pfam; PF03815; LCCL; 1.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00084; Sushi; 5.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR SMART; SM00032; CCP; 5.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00603; LCCL; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF56436; SSF56436; 1.
DR SUPFAM; SSF57535; SSF57535; 5.
DR SUPFAM; SSF69848; SSF69848; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS50026; EGF_3; 1.
DR PROSITE; PS50820; LCCL; 1.
DR PROSITE; PS50923; SUSHI; 5.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 2: Evidence at transcript level;
KW Cell adhesion; Disulfide bond; EGF-like domain; Glycoprotein;
KW Hemolymph clotting; Hydrolase; Lectin; Protease; Repeat; Secreted;
KW Serine protease; Signal; Sushi.
FT SIGNAL 1..25
FT /evidence="ECO:0000250"
FT CHAIN 26..1019
FT /note="Limulus clotting factor C"
FT /id="PRO_0000028430"
FT CHAIN 26..690
FT /note="Limulus clotting factor C heavy chain"
FT /id="PRO_0000028431"
FT CHAIN 691..1019
FT /note="Limulus clotting factor C light chain"
FT /id="PRO_0000028432"
FT CHAIN 691..762
FT /note="Limulus clotting factor C chain A"
FT /id="PRO_0000028433"
FT CHAIN 763..1019
FT /note="Limulus clotting factor C chain B"
FT /id="PRO_0000028434"
FT DOMAIN 102..137
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 140..197
FT /note="Sushi 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 198..256
FT /note="Sushi 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 258..323
FT /note="Sushi 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 325..421
FT /note="LCCL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00123"
FT DOMAIN 436..568
FT /note="C-type lectin"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT DOMAIN 574..636
FT /note="Sushi 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 689..750
FT /note="Sushi 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00302"
FT DOMAIN 763..1019
FT /note="Peptidase S1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00274"
FT ACT_SITE 809
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 865
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT ACT_SITE 966
FT /note="Charge relay system"
FT /evidence="ECO:0000250"
FT BINDING 960
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CARBOHYD 523
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 534
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 624
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 740
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 767
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 912
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 106..118
FT /evidence="ECO:0000250"
FT DISULFID 112..125
FT /evidence="ECO:0000250"
FT DISULFID 127..136
FT /evidence="ECO:0000250"
FT DISULFID 142..182
FT /evidence="ECO:0000250"
FT DISULFID 168..195
FT /evidence="ECO:0000250"
FT DISULFID 199..241
FT /evidence="ECO:0000250"
FT DISULFID 227..254
FT /evidence="ECO:0000250"
FT DISULFID 260..308
FT /evidence="ECO:0000250"
FT DISULFID 294..321
FT /evidence="ECO:0000250"
FT DISULFID 331..350
FT /evidence="ECO:0000250"
FT DISULFID 354..374
FT /evidence="ECO:0000250"
FT DISULFID 436..447
FT /evidence="ECO:0000250"
FT DISULFID 464..564
FT /evidence="ECO:0000250"
FT DISULFID 538..556
FT /evidence="ECO:0000250"
FT DISULFID 576..621
FT /evidence="ECO:0000250"
FT DISULFID 607..634
FT /evidence="ECO:0000250"
FT DISULFID 720..748
FT /evidence="ECO:0000250"
FT DISULFID 794..810
FT /evidence="ECO:0000250"
FT DISULFID 932..951
FT /evidence="ECO:0000250"
FT DISULFID 962..996
FT /evidence="ECO:0000250"
SQ SEQUENCE 1019 AA; 112430 MW; 918A1ED8B817B6C3 CRC64;
MVLASFLVSG LVLGLLAQKM RPVQSKGVDL GLCDETRFEC KCGDPGYVFN IPVKQCTYFY
RWRPYCKPCD DLEAKDICPK YKRCQECKAG LDSCVTCPPN KYGTWCSGEC QCKNGGICDQ
RTGACACRDR YEGVHCEILK GCPLLPSDSQ VQEVRNPPDN PQTIDYSCSP GFKLKGMARI
SCLPNGQWSN FPPKCIRECA MVSSPEHGKV NALSGDMIEG ATLRFSCDSP YYLIGQETLT
CQGNGQWNGQ IPQCKNLVFC PDLDPVNHAE HKVKIGVEQK YGQFPQGTEV TYTCSGNYFL
MGFDTLKCNP DGSWSGSQPS CVKVADREVD CDSKAVDFLD DVGEPVRIHC PAGCSLTAGT
VWGTAIYHEL SSVCRAAIHA GKLPNSGGAV HVVNNGPYSD FLGSDLNGIK SEELKSLARS
FRFDYVRSST AGKSGCPDGW FEVDENCVYV TSKQRAWERA QGVCTNMAAR LAVLDKDVIP
NSLTETLRGK GLTTTWIGLH RLDAEKPFIW ELMDRSNVVL NDNLTFWASG EPGNETNCVY
MDIQDQLQSV WKTKSCFQPS SFACMMDLSD RNKAKCDDPG SLENGHATLH GQSIDGFYAG
SSIRYSCEVL HYLSGTETVT CTTNGTWSAP KPRCIKVITC QNPPVPSYGS VEIKPPSRTN
SISRVGSPFL RLPRLPLPLA RAAKPPPKPR SSQPSTVDLA SKVKLPEGHY RVGSRAIYTC
ESRYYELLGS QGRRCDSNGN WSGRPASCIP VCGRSDSPRS PFIWNGNSTE IGQWPWQAGI
SRWLADHNMW FLQCGGSLLN EKWIVTAAHC VTYSATAEII DPNQFKMYLG KYYRDDSRDD
DYVQVREALE IHVNPNYDPG NLNFDIALIQ LKTPVTLTTR VQPICLPTDI TTREHLKEGT
LAVVTGWGLN ENNTYSETIQ QAVLPVVAAS TCEEGYKEAD LPLTVTENMF CAGYKKGRYD
ACSGDSGGPL VFADDSRTER RWVLEGIVSW GSPSGCGKAN QYGGFTKVNV FLSWIRQFI
