NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND DISULFIDE BONDS.
TISSUE=Hemocyte;
PubMed=2266134 [NCBI, ExPASy, EBI, Israel, Japan]
Muta T., Hashimoto R., Miyata T., Nishimura H., Toh Y., Iwanaga S.;
"Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning, disulfide locations, and subcellular localization.";
J. Biol. Chem. 265:22426-22433(1990).

Comments

FUNCTION: This enzyme is closely associated with an endotoxin-sensitive hemolymph coagulation system in limulus. Its active form catalyzes the conversion of coagulogen to insoluble coagulin gel.
CATALYTIC ACTIVITY: Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments.
SUBUNIT: Upon activation by factor B, it is converted to a two-chain active form composed of a light and a heavy chain.
SUBCELLULAR LOCATION: Secreted. Note=Secreted in hemolymph.
PTM: Contains six O-linked carbohydrate chains in the N-terminal light chain generated after activation.
SIMILARITY: Belongs to the peptidase S1 family [view classification].
SIMILARITY: Contains 1 peptidase S1 domain [view classification].

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

M58366; AAA30094.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A23689; A23689.

3D structure databases

HSSP

P00750; 1RTF. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

P21902.

Protein family/group databases

MEROPS

S01.221; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
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

IPR006604; CLIP.
IPR001254; Peptidase_S1_S6.
IPR001314; Peptidase_S1A.
Graphical view of domain structure.

Pfam

PF00089; Trypsin; 1.
Pfam graphical view of domain structure.

PRINTS

PR00722; CHYMOTRYPSIN.

SMART

SM00680; CLIP; 1.
SM00020; Tryp_SPc; 1.
SMART graphical view of domain structure.

PROSITE

PS50240; TRYPSIN_DOM; 1.
PS00134; TRYPSIN_HIS; 1.
PS00135; TRYPSIN_SER; 1.
PROSITE graphical view of domain structure (profiles).

ProtoNet

P21902.

Other

UniRef

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

Keywords

Cleavage on pair of basic residues; Direct protein sequencing; Glycoprotein; Hemolymph clotting; Hydrolase; Protease; Pyrrolidone carboxylic acid; Secreted; Serine protease; Signal; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 17`	`17`	`Or 25 (Potential).`
`PROPEP`	`18 29`	`12`	`Potential.`	`PRO_0000028427`
`CHAIN`	`30 127`	`98`	`Proclotting enzyme light chain.`	`PRO_0000028428`
`CHAIN`	`128 375`	`248`	`Proclotting enzyme heavy chain.`	`PRO_0000028429`
`DOMAIN`	`128 375`	`248`	`Peptidase S1.`
`ACT_SITE`	`172 172`		`Charge relay system (By similarity).`
`ACT_SITE`	`228 228`		`Charge relay system (By similarity).`
`ACT_SITE`	`326 326`		`Charge relay system (By similarity).`
`MOD_RES`	`30 30`		`Pyrrolidone carboxylic acid.`
`CARBOHYD`	`122 122`		`N-linked (GlcNAc...).`
`CARBOHYD`	`235 235`		`N-linked (GlcNAc...).`
`CARBOHYD`	`304 304`		`N-linked (GlcNAc...).`
`DISULFID`	`40 83`
`DISULFID`	`50 73`
`DISULFID`	`56 84`
`DISULFID`	`118 248`		`Interchain (between light and heavy chains).`
`DISULFID`	`157 173`
`DISULFID`	`295 311`
`DISULFID`	`322 351`

Sequence information

Length: 375 AA [This is the length of the unprocessed precursor]

Molecular weight: 41592 Da [This is the MW of the unprocessed precursor]

CRC64: 94209E514DFCF8FB [This is a checksum on the sequence]

        10         20         30         40         50         60 
MLVNNVFSLL CFPLLMSVVR CSTLSRQRRQ FVFPDEEELC SNRFTEEGTC KNVLDCRILL 

        70         80         90        100        110        120 
QKNDYNLLKE SICGFEGITP KVCCPKSSHV ISSTQAPPET TTTERPPKQI PPNLPEVCGI 

       130        140        150        160        170        180 
HNTTTTRIIG GREAPIGAWP WMTAVYIKQG GIRSVQCGGA LVTNRHVITA SHCVVNSAGT 

       190        200        210        220        230        240 
DVMPADVFSV RLGEHNLYST DDDSNPIDFA VTSVKHHEHF VLATYLNDIA ILTLNDTVTF 

       250        260        270        280        290        300 
TDRIRPICLP YRKLRYDDLA MRKPFITGWG TTAFNGPSSA VLREVQLPIW EHEACRQAYE 

       310        320        330        340        350        360 
KDLNITNVYM CAGFADGGKD ACQGDSGGPM MLPVKTGEFY LIGIVSFGKK CALPGFPGVY 

       370 
TKVTEFLDWI AEHMV

P21902 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