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Reviewed, UniProtKB/Swiss-Prot Q26422 (LFC_CARRO)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Limulus clotting factor C
      Short name=FC
    EC=3.4.21.84
Cleaved into the following 4 chains:
    1- Recommended name:
            Limulus clotting factor C heavy chain
    2- Recommended name:
            Limulus clotting factor C light chain
    3- Recommended name:
            Limulus clotting factor C chain A
    4- Recommended name:
            Limulus clotting factor C chain B
OrganismCarcinoscorpius rotundicauda (Southeast Asian horseshoe crab)
Taxonomic identifier6848 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Arthropoda › Chelicerata › Merostomata › Xiphosura › Limulidae › Carcinoscorpius

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Protein attributes

Sequence length1019 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (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 By similarity.

Subunit structure

Heterodimer of a light chain and a heavy chain linked by a disulfide bond By similarity.

Subcellular location

Secreted. Note: Secreted in hemolymph.

Sequence similarities

Belongs to the peptidase S1 family.

Contains 1 C-type lectin domain.

Contains 1 EGF-like domain.

Contains 1 LCCL domain.

Contains 1 peptidase S1 domain.

Contains 5 Sushi (CCP/SCR) domains.

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Ontologies

Keywords
   Biological processCell adhesion
Hemolymph clotting
   Cellular componentSecreted
   DomainEGF-like domain
Repeat
Signal
Sushi
   LigandLectin
   Molecular functionHydrolase
Protease
Serine protease
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

hemolymph coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionprotein binding

Inferred from electronic annotation. Source: UniProtKB-KW

serine-type endopeptidase activity

Inferred from electronic annotation. Source: InterPro

sugar binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 By similarity
Chain26 – 1019994Limulus clotting factor C
PRO_0000028430
Chain26 – 690665Limulus clotting factor C heavy chain
PRO_0000028431
Chain691 – 1019329Limulus clotting factor C light chain
PRO_0000028432
Chain691 – 76272Limulus clotting factor C chain A
PRO_0000028433
Chain763 – 1019257Limulus clotting factor C chain B
PRO_0000028434

Regions

Domain102 – 13736EGF-like
Domain140 – 19758Sushi 1
Domain198 – 25659Sushi 2
Domain258 – 32366Sushi 3
Domain325 – 42197LCCL
Domain436 – 568133C-type lectin
Domain574 – 63663Sushi 4
Domain689 – 75062Sushi 5
Domain763 – 1019257Peptidase S1
Compositional bias643 – 68947Pro-rich

Sites

Active site8091Charge relay system By similarity
Active site8651Charge relay system By similarity
Active site9661Charge relay system By similarity
Binding site9601Substrate By similarity

Amino acid modifications

Glycosylation5231N-linked (GlcNAc...) Potential
Glycosylation5341N-linked (GlcNAc...) Potential
Glycosylation6241N-linked (GlcNAc...) Potential
Glycosylation7401N-linked (GlcNAc...) Potential
Glycosylation7671N-linked (GlcNAc...) Potential
Glycosylation9121N-linked (GlcNAc...) Potential
Disulfide bond106 ↔ 118 By similarity
Disulfide bond112 ↔ 125 By similarity
Disulfide bond127 ↔ 136 By similarity
Disulfide bond142 ↔ 182 By similarity
Disulfide bond168 ↔ 195 By similarity
Disulfide bond199 ↔ 241 By similarity
Disulfide bond227 ↔ 254 By similarity
Disulfide bond260 ↔ 308 By similarity
Disulfide bond294 ↔ 321 By similarity
Disulfide bond331 ↔ 350 By similarity
Disulfide bond354 ↔ 374 By similarity
Disulfide bond436 ↔ 447 By similarity
Disulfide bond464 ↔ 564 By similarity
Disulfide bond538 ↔ 556 By similarity
Disulfide bond576 ↔ 621 By similarity
Disulfide bond607 ↔ 634 By similarity
Disulfide bond720 ↔ 748 By similarity
Disulfide bond794 ↔ 810 By similarity
Disulfide bond932 ↔ 951 By similarity
Disulfide bond962 ↔ 996 By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q26422-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 918A1ED8B817B6C3

FASTA1,019112,430
        10         20         30         40         50         60 
MVLASFLVSG LVLGLLAQKM RPVQSKGVDL GLCDETRFEC KCGDPGYVFN IPVKQCTYFY 

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

       130        140        150        160        170        180 
RTGACACRDR YEGVHCEILK GCPLLPSDSQ VQEVRNPPDN PQTIDYSCSP GFKLKGMARI 

       190        200        210        220        230        240 
SCLPNGQWSN FPPKCIRECA MVSSPEHGKV NALSGDMIEG ATLRFSCDSP YYLIGQETLT 

       250        260        270        280        290        300 
CQGNGQWNGQ IPQCKNLVFC PDLDPVNHAE HKVKIGVEQK YGQFPQGTEV TYTCSGNYFL 

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

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

       430        440        450        460        470        480 
FRFDYVRSST AGKSGCPDGW FEVDENCVYV TSKQRAWERA QGVCTNMAAR LAVLDKDVIP 

       490        500        510        520        530        540 
NSLTETLRGK GLTTTWIGLH RLDAEKPFIW ELMDRSNVVL NDNLTFWASG EPGNETNCVY 

       550        560        570        580        590        600 
MDIQDQLQSV WKTKSCFQPS SFACMMDLSD RNKAKCDDPG SLENGHATLH 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 DPNQFKMYLG KYYRDDSRDD 

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

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

       970        980        990       1000       1010 
ACSGDSGGPL VFADDSRTER RWVLEGIVSW GSPSGCGKAN QYGGFTKVNV FLSWIRQFI

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References

[1]"Molecular cloning and sequence analysis of factor C cDNA from the Singapore horseshoe crab, Carcinoscorpius rotundicauda."
Ding J.L., Navas M.A. III, Ho B.
Mol. Mar. Biol. Biotechnol. 4:90-103(1995) [PubMed: 7538401] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Blood.

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Cross-references

Sequence databases

S77063 mRNA. Translation: AAB34361.1.

3D structure databases

HSSPHSSP built from PDB template 1FDP based on UniProtKB P00746.
ModBaseSearch...

Protein family/group databases

MEROPSS01.219.

Enzyme and pathway databases

BRENDA3.4.21.84. 294954.

Family and domain databases

InterProIPR001304. C-type_lectin.
IPR018378. C-type_lectin_CS.
IPR016060. Complement_control_module.
IPR006210. EGF-like.
IPR013032. EGF-like_reg_CS.
IPR000742. EGF_3.
IPR013111. EGF_extracell.
IPR004043. LCCL.
IPR018114. Peptidase_S1/S6_AS.
IPR001254. Peptidase_S1_S6.
IPR001314. Peptidase_S1A.
IPR000436. Sushi_SCR_CCP.
[Graphical view]
Gene3DG3DSA:2.10.70.10. Complement_control_module. 1 hit.
G3DSA:2.170.130.20. LCCL. 1 hit.
PfamPF07974. EGF_2. 1 hit.
PF03815. LCCL. 1 hit.
PF00059. Lectin_C. 1 hit.
PF00084. Sushi. 5 hits.
PF00089. Trypsin. 1 hit.
[Graphical view]
PRINTSPR00722. CHYMOTRYPSIN.
SMARTSM00032. CCP. 5 hits.
SM00034. CLECT. 1 hit.
SM00181. EGF. 1 hit.
SM00603. LCCL. 1 hit.
SM00020. Tryp_SPc. 1 hit.
[Graphical view]
PROSITEPS00615. C_TYPE_LECTIN_1. False negative.
PS50041. C_TYPE_LECTIN_2. 1 hit.
PS00022. EGF_1. 1 hit.
PS01186. EGF_2. False negative.
PS50026. EGF_3. 1 hit.
PS50820. LCCL. 1 hit.
PS50923. SUSHI. 5 hits.
PS50240. TRYPSIN_DOM. 1 hit.
PS00134. TRYPSIN_HIS. 1 hit.
PS00135. TRYPSIN_SER. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameLFC_CARRO
AccessionPrimary (citable) accession number: Q26422
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents