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Database: UniProt
Entry: P28175
LinkDB: P28175
Original site: P28175 
ID   LFC_TACTR               Reviewed;        1019 AA.
AC   P28175;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   05-DEC-2018, entry version 111.
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   Tachypleus tridentatus (Japanese horseshoe crab).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Merostomata;
OC   Xiphosura; Limulidae; Tachypleus.
OX   NCBI_TaxID=6853;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PARTIAL
RP   PROTEIN SEQUENCE.
RX   PubMed=2007602;
RA   Muta T., Miyata T., Misumi Y., Tokunaga F., Nakamura T., Toh Y.,
RA   Ikehara Y., Iwanaga S.;
RT   "Limulus factor C. An endotoxin-sensitive serine protease zymogen with
RT   a mosaic structure of complement-like, epidermal growth factor-like,
RT   and lectin-like domains.";
RL   J. Biol. Chem. 266:6554-6561(1991).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE (ISOFORM LONG), AND GLYCOSYLATION AT ASN-767.
RX   PubMed=3308457; DOI=10.1111/j.1432-1033.1987.tb13352.x;
RA   Tokunaga F., Miyata T., Nakamura T., Morita T., Kuma K., Miyata T.,
RA   Iwanaga S.;
RT   "Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of
RT   horseshoe crab hemocytes. Identification and alignment of proteolytic
RT   fragments produced during the activation show that it is a novel type
RT   of serine protease.";
RL   Eur. J. Biochem. 167:405-416(1987).
CC   -!- FUNCTION: This enzyme is closely associated with an endotoxin-
CC       sensitive hemolymph coagulation system which may play important
CC       roles in both hemostasis and host defense mechanisms. Its active
CC       form catalyzes the activation of factor B.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-
CC         Ile-125 bonds in Limulus clotting factor B to form activated
CC         factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic
CC         substrates.; EC=3.4.21.84;
CC   -!- ACTIVITY REGULATION: Activated by Gram-negative bacterial
CC       lipopolysaccharides and chymotrypsin.
CC   -!- SUBUNIT: Heterodimer of a light chain and a heavy chain linked by
CC       a disulfide bond.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=P28175-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=P28175-2; Sequence=VSP_005413, VSP_005414;
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00274}.
DR   EMBL; D90271; BAA14315.1; -; mRNA.
DR   EMBL; D90272; BAA14316.1; -; mRNA.
DR   PIR; A38738; A38738.
DR   ProteinModelPortal; P28175; -.
DR   SMR; P28175; -.
DR   MEROPS; S01.219; -.
DR   iPTMnet; P28175; -.
DR   PRIDE; P28175; -.
DR   KEGG; ag:BAA14315; -.
DR   KO; K22079; -.
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   CDD; cd00033; CCP; 5.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 2.170.130.20; -; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR004043; LCCL.
DR   InterPro; IPR036609; LCCL_sf.
DR   InterPro; IPR009003; Peptidase_S1_PA.
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   1: Evidence at protein level;
KW   Alternative splicing; Cell adhesion; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Hemolymph clotting;
KW   Hydrolase; Lectin; Protease; Repeat; Secreted; Serine protease;
KW   Signal; Sushi.
FT   SIGNAL        1     25
FT   CHAIN        26   1019       Limulus clotting factor C.
FT                                /FTId=PRO_0000028435.
FT   CHAIN        26    690       Limulus clotting factor C heavy chain.
FT                                /FTId=PRO_0000028436.
FT   CHAIN       691   1019       Limulus clotting factor C light chain.
FT                                /FTId=PRO_0000028437.
FT   CHAIN       691    762       Limulus clotting factor C chain A.
FT                                /FTId=PRO_0000028438.
FT   CHAIN       763   1019       Limulus clotting factor C chain B.
FT                                /FTId=PRO_0000028439.
FT   DOMAIN      102    137       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   DOMAIN      140    197       Sushi 1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      198    256       Sushi 2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      258    323       Sushi 3. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      325    421       LCCL. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00123}.
FT   DOMAIN      436    568       C-type lectin. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00040}.
FT   DOMAIN      574    636       Sushi 4. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      689    750       Sushi 5. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00302}.
FT   DOMAIN      763   1019       Peptidase S1. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00274}.
FT   COMPBIAS    643    689       Pro-rich.
FT   ACT_SITE    809    809       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    865    865       Charge relay system. {ECO:0000250}.
FT   ACT_SITE    966    966       Charge relay system. {ECO:0000250}.
FT   BINDING     960    960       Substrate. {ECO:0000250}.
FT   CARBOHYD    523    523       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    534    534       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    624    624       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    740    740       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    767    767       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000269|PubMed:3308457}.
FT   CARBOHYD    912    912       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    106    118       {ECO:0000250}.
FT   DISULFID    112    125       {ECO:0000250}.
FT   DISULFID    127    136       {ECO:0000250}.
FT   DISULFID    142    182       {ECO:0000250}.
FT   DISULFID    168    195       {ECO:0000250}.
FT   DISULFID    199    241       {ECO:0000250}.
FT   DISULFID    227    254       {ECO:0000250}.
FT   DISULFID    260    308       {ECO:0000250}.
FT   DISULFID    294    321       {ECO:0000250}.
FT   DISULFID    331    350       {ECO:0000250}.
FT   DISULFID    354    374       {ECO:0000250}.
FT   DISULFID    436    447       {ECO:0000250}.
FT   DISULFID    464    564       {ECO:0000250}.
FT   DISULFID    538    556       {ECO:0000250}.
FT   DISULFID    576    621       {ECO:0000250}.
FT   DISULFID    607    634       {ECO:0000250}.
FT   DISULFID    720    748       {ECO:0000250}.
FT   DISULFID    794    810       {ECO:0000250}.
FT   DISULFID    932    951       {ECO:0000250}.
FT   DISULFID    962    996       {ECO:0000250}.
FT   VAR_SEQ     492    498       LTTTWIG -> TDNVTAT (in isoform Short).
FT                                {ECO:0000303|PubMed:2007602}.
FT                                /FTId=VSP_005413.
FT   VAR_SEQ     499   1019       Missing (in isoform Short).
FT                                {ECO:0000303|PubMed:2007602}.
FT                                /FTId=VSP_005414.
SQ   SEQUENCE   1019 AA;  112346 MW;  5BC2864C6715289B CRC64;
     MVLASFLVSG LVLGILAQQM RPVQSRGVDL GLCDETRFEC KCGDPGYVFN VPMKQCTYFY
     RWRPYCKPCD DLEAKDICPK YKRCQECKAG LDSCVTCPPN KYGTWCSGEC QCKNGGICDQ
     RTGACTCRDR YEGAHCEILK GCPLLPSDSQ VQEVRNPPDN PQTIDYSCSP GFKLKGVARI
     SCLPNGQWSS FPPKCIRECA KVSSPEHGKV NAPSGNMIEG ATLRFSCDSP YYLIGQETLT
     CQGNGQWSGQ IPQCKKLVFC PDLDPVNHAE HQVKIGVEQK YGQFPQGTEV TYTCSGNYFL
     MGFNTLKCNP DGSWSGSQPS CVKVADREVD CDSKAVDFLD DVGEPVRIHC PAGCSLTAGT
     VWGTAIYHEL SSVCRAAIHA GKLPNSGGAV HVVNNGPYSD FLGSDLNGIK SEELKSLARS
     FRFDYVSSST AGRSGCPDGW FEVEENCVYV TSKQRAWERA QGVCTNMAAR LAVLDKDLIP
     SSLTETLRGK GLTTTWIGLH RLDAEKPFVW ELMDRSNVVL NDNLTFWASG EPGNETNCVY
     LDIRDQLQPV WKTKSCFQPS SFACMMDLSD RNKAKCDDPG PLENGHATLH GQSIDGFYAG
     SSIRYSCEVL HYLSGTETVT CTTNGTWSAP KPRCIKVITC QNPPVPSYGS VEIKPPSRTN
     SISRVGSPFL RLPRLPLPLA RAAKPPPKPR SSQPSTVDLA SKVKLPEGHY RVGSRAIYTC
     ESRYYELLGS QGRRCDSNGN WSGRPASCIP VCGRSDSPRS PFIWNGNSTE IGQWPWQAGI
     SRWLADHNMW FLQCGGSLLN EKWIVTAAHC VTYSATAEII DPSQFKIYLG KYYRDDSRDD
     DYVQVREALE IHVNPNYDPG NLNFDIALIQ LKTPVTLTTR VQPICLPTDI TTREHLKEGT
     LAVVTGWGLN ENNTYSEMIQ QAVLPVVAAS TCEEGYKEAD LPLTVTENMF CAGYKKGRYD
     ACSGDSGGPL VFADDSRTER RWVLEGIVSW GSPSGCGKAN QYGGFTKVNV FLSWIRQFI
//
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