Limulus clotting factor C heavy chain
Limulus clotting factor C light chain
Limulus clotting factor C chain A
Limulus clotting factor C chain B

Gene name

None

From

Tachypleus tridentatus (Japanese horseshoe crab)

[TaxID: 6853]

Taxonomy

Eukaryota; Metazoa; Arthropoda; Chelicerata; Merostomata; Xiphosura; Limulidae; Tachypleus.

Protein existence

1: Evidence at protein level;

References

[1]

NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PARTIAL PROTEIN SEQUENCE.
PubMed=2007602 [NCBI, ExPASy, EBI, Israel, Japan]
Muta T., Miyata T., Misumi Y., Tokunaga F., Nakamura T., Toh Y., Ikehara Y., Iwanaga S.;
"Limulus factor C. An endotoxin-sensitive serine protease zymogen with a mosaic structure of complement-like, epidermal growth factor-like, and lectin-like domains.";
J. Biol. Chem. 266:6554-6561(1991).

[2]

PARTIAL PROTEIN SEQUENCE (ISOFORM LONG), AND GLYCOSYLATION AT ASN-767.
PubMed=3308457 [NCBI, ExPASy, EBI, Israel, Japan]
Tokunaga F., Miyata T., Nakamura T., Morita T., Kuma K., Miyata T., Iwanaga S.;
"Lipopolysaccharide-sensitive serine-protease zymogen (factor C) of horseshoe crab hemocytes. Identification and alignment of proteolytic fragments produced during the activation show that it is a novel type of serine protease.";
Eur. J. Biochem. 167:405-416(1987).

Comments

FUNCTION: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system which may play important roles in both hemostasis and host defense mechanisms. Its active form catalyzes the activation of factor B.
CATALYTIC ACTIVITY: Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro-Arg-|-Xaa- bonds in synthetic substrates.
ENZYME REGULATION: Activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin.
SUBUNIT: Heterodimer of a light chain and a heavy chain linked by a disulfide bond.
SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.

ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.

Name	Long
Isoform ID	P28175-1
This is the isoform sequence displayed in this entry.

Name	Short
Isoform ID	P28175-2
Features which should be applied to build the isoform sequence: VSP_005413, VSP_005414.

SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 C-type lectin domain.
SIMILARITY: Contains 1 EGF-like domain.
SIMILARITY: Contains 1 LCCL domain.
SIMILARITY: Contains 1 peptidase S1 domain [view classification].
SIMILARITY: Contains 5 Sushi (CCP/SCR) domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

D90271; BAA14315.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
D90272; BAA14316.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A38738; A38738.

3D structure databases

HSSP

P00746; 1FDP. [HSSP ENTRY / PDB]

ModBase

P28175.

Protein family/group databases

MEROPS

S01.219; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0005529;	Molecular function: sugar binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007155;	Biological process: cell adhesion (inferred from electronic annotation from UniProtKB-KW).
GO:0042381;	Biological process: hemolymph coagulation (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR001304; C-type_lectin.
IPR016060; Complement_control_module.
IPR006210; EGF.
IPR000742; EGF_3.
IPR013111; EGF_extracell.
IPR013032; EGF_like_reg_CS.
IPR004043; LCCL.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
IPR000436; Sushi_SCR_CCP.
Graphical view of domain structure.

Gene3D

G3DSA:2.10.70.10; Complement_control_module; 1.
G3DSA:2.170.130.20; LCCL; 1.

Pfam

PF07974; EGF_2; 1.
PF03815; LCCL; 1.
PF00059; Lectin_C; 1.
PF00084; Sushi; 5.
PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00032; CCP; 5.
SM00034; CLECT; 1.
SM00181; EGF; 1.
SM00603; LCCL; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS00615; C_TYPE_LECTIN_1; FALSE_NEG.
PS50041; C_TYPE_LECTIN_2; 1.
PS00022; EGF_1; 1.
PS01186; EGF_2; FALSE_NEG.
PS50026; EGF_3; 1.
PS50820; LCCL; 1.
PS50923; SUSHI; 5.
PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Alternative splicing; Cell adhesion; Direct protein sequencing; EGF-like domain; Glycoprotein; Hemolymph clotting; Hydrolase; Lectin; Protease; Repeat; Secreted; Serine protease; Signal; Sushi.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`
`CHAIN`	`26 1019`	`994`	`Limulus clotting factor C.`	`PRO_0000028435`
`CHAIN`	`26 690`	`665`	`Limulus clotting factor C heavy chain.`	`PRO_0000028436`
`CHAIN`	`691 1019`	`329`	`Limulus clotting factor C light chain.`	`PRO_0000028437`
`CHAIN`	`691 762`	`72`	`Limulus clotting factor C chain A.`	`PRO_0000028438`
`CHAIN`	`763 1019`	`257`	`Limulus clotting factor C chain B.`	`PRO_0000028439`
`DOMAIN`	`102 137`	`36`	`EGF-like.`
`DOMAIN`	`140 197`	`58`	`Sushi 1.`
`DOMAIN`	`198 256`	`59`	`Sushi 2.`
`DOMAIN`	`258 323`	`66`	`Sushi 3.`
`DOMAIN`	`325 421`	`97`	`LCCL.`
`DOMAIN`	`436 568`	`133`	`C-type lectin.`
`DOMAIN`	`574 636`	`63`	`Sushi 4.`
`DOMAIN`	`689 750`	`62`	`Sushi 5.`
`DOMAIN`	`763 1019`	`257`	`Peptidase S1.`
`COMPBIAS`	`643 689`	`47`	`Pro-rich.`
`ACT_SITE`	`809 809`		`Charge relay system (By similarity).`
`ACT_SITE`	`865 865`		`Charge relay system (By similarity).`
`ACT_SITE`	`966 966`		`Charge relay system (By similarity).`
`BINDING`	`960 960`		`Substrate (By similarity).`
`CARBOHYD`	`523 523`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`534 534`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`624 624`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`740 740`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`767 767`		`N-linked (GlcNAc...).`
`CARBOHYD`	`912 912`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`106 118`		`By similarity.`
`DISULFID`	`112 125`		`By similarity.`
`DISULFID`	`127 136`		`By similarity.`
`DISULFID`	`142 182`		`By similarity.`
`DISULFID`	`168 195`		`By similarity.`
`DISULFID`	`199 241`		`By similarity.`
`DISULFID`	`227 254`		`By similarity.`
`DISULFID`	`260 308`		`By similarity.`
`DISULFID`	`294 321`		`By similarity.`
`DISULFID`	`331 350`		`By similarity.`
`DISULFID`	`354 374`		`By similarity.`
`DISULFID`	`436 447`		`By similarity.`
`DISULFID`	`464 564`		`By similarity.`
`DISULFID`	`538 556`		`By similarity.`
`DISULFID`	`576 621`		`By similarity.`
`DISULFID`	`607 634`		`By similarity.`
`DISULFID`	`720 748`		`By similarity.`
`DISULFID`	`794 810`		`By similarity.`
`DISULFID`	`932 951`		`By similarity.`
`DISULFID`	`962 996`		`By similarity.`
`VAR_SEQ`	`492 498`		`LTTTWIG -> TDNVTAT (in isoform Short).`	`VSP_005413`
`VAR_SEQ`	`499 1019`		`Missing (in isoform Short).`	`VSP_005414`

Sequence information

Length: 1019 AA [This is the length of the unprocessed precursor]

Molecular weight: 112346 Da [This is the MW of the unprocessed precursor]

CRC64: 5BC2864C6715289B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVLASFLVSG LVLGILAQQM RPVQSRGVDL GLCDETRFEC KCGDPGYVFN VPMKQCTYFY 

        70         80         90        100        110        120 
RWRPYCKPCD DLEAKDICPK YKRCQECKAG LDSCVTCPPN KYGTWCSGEC QCKNGGICDQ 

       130        140        150        160        170        180 
RTGACTCRDR YEGAHCEILK GCPLLPSDSQ VQEVRNPPDN PQTIDYSCSP GFKLKGVARI 

       190        200        210        220        230        240 
SCLPNGQWSS FPPKCIRECA KVSSPEHGKV NAPSGNMIEG ATLRFSCDSP YYLIGQETLT 

       250        260        270        280        290        300 
CQGNGQWSGQ IPQCKKLVFC PDLDPVNHAE HQVKIGVEQK YGQFPQGTEV TYTCSGNYFL 

       310        320        330        340        350        360 
MGFNTLKCNP DGSWSGSQPS CVKVADREVD CDSKAVDFLD DVGEPVRIHC PAGCSLTAGT 

       370        380        390        400        410        420 
VWGTAIYHEL SSVCRAAIHA GKLPNSGGAV HVVNNGPYSD FLGSDLNGIK SEELKSLARS 

       430        440        450        460        470        480 
FRFDYVSSST AGRSGCPDGW FEVEENCVYV TSKQRAWERA QGVCTNMAAR LAVLDKDLIP 

       490        500        510        520        530        540 
SSLTETLRGK GLTTTWIGLH RLDAEKPFVW ELMDRSNVVL NDNLTFWASG EPGNETNCVY 

       550        560        570        580        590        600 
LDIRDQLQPV WKTKSCFQPS SFACMMDLSD RNKAKCDDPG PLENGHATLH GQSIDGFYAG 

       610        620        630        640        650        660 
SSIRYSCEVL HYLSGTETVT CTTNGTWSAP KPRCIKVITC QNPPVPSYGS VEIKPPSRTN 

       670        680        690        700        710        720 
SISRVGSPFL RLPRLPLPLA RAAKPPPKPR SSQPSTVDLA SKVKLPEGHY RVGSRAIYTC 

       730        740        750        760        770        780 
ESRYYELLGS QGRRCDSNGN WSGRPASCIP VCGRSDSPRS PFIWNGNSTE IGQWPWQAGI 

       790        800        810        820        830        840 
SRWLADHNMW FLQCGGSLLN EKWIVTAAHC VTYSATAEII DPSQFKIYLG KYYRDDSRDD 

       850        860        870        880        890        900 
DYVQVREALE IHVNPNYDPG NLNFDIALIQ LKTPVTLTTR VQPICLPTDI TTREHLKEGT 

       910        920        930        940        950        960 
LAVVTGWGLN ENNTYSEMIQ QAVLPVVAAS TCEEGYKEAD LPLTVTENMF CAGYKKGRYD 

       970        980        990       1000       1010 
ACSGDSGGPL VFADDSRTER RWVLEGIVSW GSPSGCGKAN QYGGFTKVNV FLSWIRQFI

P28175 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools